CAZypedia - User contributions [en-ca]

Glycoside Hydrolase Family 5

2012-10-29T19:41:04Z

Karen Eddy:

Glycoside Hydrolase Family 5

2012-10-29T19:39:13Z

Karen Eddy:

Glycoside Hydrolase Family 5

2012-10-29T19:37:52Z

Karen Eddy:

Template:Hl2

2012-09-09T23:08:27Z

Karen Eddy:

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Template:Prettytable

2012-09-09T23:06:13Z

Karen Eddy:

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Lexicon tooltip

2012-09-09T22:24:21Z

Karen Eddy: Created page with "{{#dpl: |category=Definitions and explanations |order=ascending |columns = 3 |redirects=include |allowcachedresults=yes }}"

{{#dpl:
|category=Definitions and explanations
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Glycoside hydrolase tooltip

2012-09-09T22:22:50Z

Karen Eddy: Created page with "{{#dpl: |category=Glycoside Hydrolase Families |category=Curator approved{{!}}Under construction{{!}}Unassigned pages |columns=5 |rowcolformat=width=100% |ordermethod=sortkey ..."

{{#dpl:
|category=Glycoside Hydrolase Families
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MediaWiki:Cite text

2012-09-09T21:07:57Z

Karen Eddy:

__NOTOC__
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== Full bibliographic details for "{{FULLPAGENAME}}" ==

* '''Article title:''' {{FULLPAGENAME}}
* '''Author:''' ''Please use the [[Author]](s) listed in the '''"{{FULLPAGENAME}}"''' page header.''
* '''Editor:''' ''Please use the [[Responsible Curator]](s) listed in the '''"{{FULLPAGENAME}}"''' page header.''
* '''Source:''' ''{{SITENAME}}''
* '''Source URL:''' http://www.cazypedia.org/
* '''Date retrieved:''' {{#time:j F Y H:i}} UTC
* '''Date of last revision:''' {{CURRENTDAY}} {{CURRENTMONTHNAME}} {{CURRENTYEAR}} {{CURRENTTIME}} UTC
* '''Page Version ID:''' {{REVISIONID}}
* '''Permanent URL to this Version:''' {{fullurl:{{FULLPAGENAME}}|oldid={{REVISIONID}}}}
* '''Copyright information:''' {{int:sitesubtitle}} ''(Please see [[Cazypedia:Copyright]] for additional information)''

Please check the style manual for the exact format required by the publication in which you'd like to cite this page. Some guidelines for how to cite a ''CAZypedia'' article are available at [[Cazypedia:Citing]]
</div>

CAZypedia:Citing

2012-09-09T18:17:27Z

Karen Eddy:

''Please take a moment to read ''CAZypedia's'' [[Cazypedia:Copyright|copyright statement]].''

''CAZypedia'' is intended to be a concise gateway to the key publications on individual CAZyme families or topics. Readers are therefore generally advised to cite the primary literature entries when possible.

However, we recognize that it may be practical to cite ''CAZypedia'' pages directly in some cases (''e.g.'' CAZypedians may wish to include their contributions in curricula vitae; space limitations in presentations may preclude extensive literature lists; ''etc.'').

Individual articles (pages) in ''CAZypedia'' can therefore be cited, much as one would cite a review article or, perhaps more analogously, a book chapter. In the "toolbox" section (lower left corner) of all encyclopedic pages, you will find a link entitled ''Cite this page'', which will give you the full bibliographic information for that page.

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*If you would like to include a reference to a ''CAZypedia'' page in a published work, please use something like the following format:
<blockquote class="toccolours" style="float:none; padding: 10px 15px 10px 15px; display:table;">
'''Page Author(s)''' "'''Page Title'''" in '''''CAZypedia''''', available at '''URL <nowiki>http://www.cazypedia.org/</nowiki>''', accessed '''date'''.
</blockquote>

*For example, a reference to the [[Glycoside Hydrolase Family 8]] page might look like this:
<blockquote class="toccolours" style="float:none; padding: 10px 15px 10px 15px; display:table;">
Kitaoka, M. and Fushinobu, S. "Glycoside Hydrolase Family 8" in ''CAZypedia'', available at URL <nowiki>http://www.cazypedia.org/</nowiki>, accessed 11 August 2009.
</blockquote>

* The format should of course be altered to fit the style of the work in which you'd like to cite a ''CAZypedia'' article, but please make sure to include the following as a minimum:''
<blockquote class="toccolours" style="float:none; padding: 10px 15px 10px 15px; display:table;">
* '''Page Author(s)'''
* '''Page Title'''
* Reference to '''''CAZypedia'''''
* The ''CAZypedia'' '''URL''' (<nowiki>http://www.cazypedia.org/</nowiki>)
* The '''date''' you accessed the work.
* If the publication in which you reference ''CAZypedia'' specifically requires that an '''editor''' be given, please use the [[Responsible Curator]] for the page.
</blockquote>
</div>

CAZypedia:Assigned pages

2012-09-09T18:12:36Z

Karen Eddy:

'''This page is a working document from the [[Board of Curators]] that lists the [[Responsible Curator]]s and [[Author]]s for various ''CAZypedia'' pages.'''

* If you see that a page is missing and you want to act as [[Responsible Curator]] to edit and actively maintain that page, please contact the [[Board of Curators]] using [[Special:Contact|this e-mail form]].

* If you would like to contribute to an existing page either as an [[Author]] or by suggesting improvements, please contact the [[Responsible Curator]] for that page. You may use this [[Special:Contact|this e-mail form]] to contact a [[Responsible Curator]] (if you know the Curator, you may also e-mail them directly).

__TOC__

== [[Glycoside Hydrolase Families]] ==
Each column is sortable by clicking on the icons in the header (''javascript must be turned on in your browser''). To reset the page to be sorted by GH family, click the <span id="projectPage" style="color:blue">'''project page'''</span> tab at the very top of the page.
{| cellspacing="0" cellpadding="4" border="0" class="sortable"
|-
! '''Family'''
! '''[[Responsible Curator]]'''
! '''Curator status'''
! '''[[Author]](s)'''
! '''Page status'''
! '''Date [[:Category:Curator approved|Curator Approved]]'''
|-
| [[Glycoside Hydrolase Family 1]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Steve Withers^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2007-05-21 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 2]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Steve Withers^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2007-05-25 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 3]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
| ^^^Geoff Fincher^^^<br>^^^Brian Mark^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-06-20
|-
| [[Glycoside Hydrolase Family 4]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Vivian Yip^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-23 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 5]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Gideon Davies^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-10-06
|-
| [[Glycoside Hydrolase Family 6]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Gideon Davies^^^<br>^^^Kathleen Piens^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-10-06
|-
| [[Glycoside Hydrolase Family 7]]
| ^^^Jerry Stahlberg^^^
| ''Accepted''
| ^^^Jerry Stahlberg^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-06-29
|-
| [[Glycoside Hydrolase Family 8]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Shinya Fushinobu^^^<br>^^^Motomitsu Kitaoka^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-10-27 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 9]]
| ^^^David Wilson^^^
| ''Accepted''
| ^^^David Wilson^^^<br>^^^Breeanna Urbanowicz^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-08-24
|-
| [[Glycoside Hydrolase Family 10]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Steve Withers^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2007-05-21 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 11]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Steve Withers^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2007-05-21 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 12]]
| ^^^Mats Sandgren^^^
| ''Accepted''
| ^^^Mats Sandgren^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 13]]
| ^^^Birte Svensson^^^
| ''Accepted''
| ^^^Stefan Janecek^^^<br>^^^Birte Svensson^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-02-02
|-
| [[Glycoside Hydrolase Family 14]]
| ^^^Kousaku Murata^^^
| ''Accepted''
| ^^^Bunzo Mikami^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 15]]
| ^^^Pedro Coutinho^^^
| ''Accepted''
| ^^^Pedro Coutinho^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-11-06 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 16]]
| ^^^Harry Brumer^^^
| ''Accepted''
| ^^^Jens Eklof^^^<br>^^^Jan-Hendrik Hehemann^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-30 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 17]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
| ^^^Geoff Fincher^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-04-27
|-
| [[Glycoside Hydrolase Family 18]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Gideon Davies^^^<br>^^^Nathalie Juge^^^<br>^^^Vincent Eijsink^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-10-12
|-
| [[Glycoside Hydrolase Family 19]]
| ^^^Vincent Eijsink^^^
| ''Accepted''
| ^^^Vincent Eijsink^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-04-16
|-
| [[Glycoside Hydrolase Family 20]]
| ^^^Dave Vocadlo^^^
| ''Accepted''
| ^^^Ian Greig^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-02-24
|-
| [[Glycoside Hydrolase Family 21]]
| ^^^Bernard Henrissat^^^
|
|
| ''[[:Category:Deleted families|Deleted family]]''
| 2010-01-06
|-
| [[Glycoside Hydrolase Family 22]]
| ^^^Dave Vocadlo^^^
| ''Accepted''
| ^^^Dave Vocadlo^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 23]]
| ^^^Anthony Clarke^^^
| ''Accepted''
| ^^^Anthony Clarke^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-18
|-
| [[Glycoside Hydrolase Family 24]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 25]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Ed Taylor^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-05-25
|-
| [[Glycoside Hydrolase Family 26]]
| ^^^Harry Gilbert^^^
| ''Accepted''
| ^^^Harry Gilbert^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-06-30 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 27]]
| ^^^Harry Brumer^^^
| ''Accepted''
| ^^^Harry Brumer^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2007-07-12 (stamped 2009-10-28)
|-
| [[Glycoside Hydrolase Family 28]]
| ^^^Richard Pickersgill^^^
| ''Accepted''
| ^^^Richard Pickersgill^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-16 (stamped 2010-05-18)
|-
| [[Glycoside Hydrolase Family 29]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Gerlind Sulzenbacher^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-01-16
|-
| [[Glycoside Hydrolase Family 30]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Brian Rempel^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-30 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 31]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Ran Zhang^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-14 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 32]]
| ^^^Mirjam Czjzek^^^
| ''Accepted''
| ^^^Mirjam Czjzek^^^<br>^^^Wim Van den Ende^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-01-11
|-
| [[Glycoside Hydrolase Family 33]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Tom Wennekes^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 34]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Tom Wennekes^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 35]]
| ^^^Anna Kulminskaya^^^
| ''Accepted''
| ^^^Anna Kulminskaya^^^<br>^^^Mirko Maksimainen^^^<br>^^^Juha Rouvinen^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-03-21
|-
| [[Glycoside Hydrolase Family 36]]
| ^^^Harry Brumer^^^
| ''Accepted''
| ^^^Harry Brumer^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2007-06-10 (stamped 2009-10-28)
|-
| [[Glycoside Hydrolase Family 37]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Tracey Gloster^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-10-08
|-
| [[Glycoside Hydrolase Family 38]]
| ^^^David Rose^^^
| ''Accepted''
| ^^^David Rose^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-08-21 (stamped 2010-11-08)
|-
| [[Glycoside Hydrolase Family 39]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Brian Rempel^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-30 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 40]]
| ^^^Bernard Henrissat^^^
|
|
| ''[[:Category:Deleted families|Deleted family]]''
| 2010-01-06
|-
| [[Glycoside Hydrolase Family 41]]
| ^^^Bernard Henrissat^^^
|
|
| ''[[:Category:Deleted families|Deleted family]]''
| 2010-01-06
|-
| [[Glycoside Hydrolase Family 42]]
| ^^^Marco Moracci^^^
| ''Accepted''
| ^^^Marco Moracci^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-11-03 (stamped 2009-11-28)
|-
| [[Glycoside Hydrolase Family 43]]
| ^^^Harry Gilbert^^^
| ''Accepted''
| ^^^Harry Gilbert^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-11-08
|-
| [[Glycoside Hydrolase Family 44]]
| ^^^Peter Reilly^^^
| ''Accepted''
| ^^^Peter Reilly^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-01-17
|-
| [[Glycoside Hydrolase Family 45]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Gideon Davies^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-10-06
|-
| [[Glycoside Hydrolase Family 46]]
| ^^^Ryszard Brzezinski^^^
| ''Accepted''
| ^^^Ryszard Brzezinski^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-10
|-
| [[Glycoside Hydrolase Family 47]]
| ^^^Kelley Moremen^^^
| ''Accepted''
| ^^^Kelley Moremen^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 48]]
| ^^^Ed Bayer^^^
| ''Accepted''
| ^^^Bareket Dassa^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-16
|-
| [[Glycoside Hydrolase Family 49]]
| ^^^Takashi Tonozuka^^^
| ''Accepted''
| ^^^Takashi Tonozuka^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-05-18
|-
| [[Glycoside Hydrolase Family 50]]
| ^^^Mirjam Czjzek^^^
| ''Accepted''
|
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-06-30
|-
| [[Glycoside Hydrolase Family 51]]
| ^^^Yuval Shoham^^^
| ''Accepted''
| ^^^Yuval Shoham^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-05-10
|-
| [[Glycoside Hydrolase Family 52]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 53]]
| ^^^Leila Lo Leggio^^^
| ''Accepted''
| ^^^Leila Lo Leggio^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-10
|-
| [[Glycoside Hydrolase Family 54]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Shinya Fushinobu^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-28 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 55]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Kiyohiko Igarashi^^^<br>^^^Takuya Ishida^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-10-27 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 56]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 57]]
| ^^^Stefan Janecek^^^
| ''Accepted''
| ^^^Stefan Janecek^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-01-15
|-
| [[Glycoside Hydrolase Family 58]]
| ^^^Warren Wakarchuk^^^
| ''Accepted''
| ^^^Warren Wakarchuk^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-01-19
|-
| [[Glycoside Hydrolase Family 59]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 60]]
| ^^^Bernard Henrissat^^^
|
|
| ''[[:Category:Deleted families|Deleted family]]''
| 2010-01-06
|-
| [[Glycoside Hydrolase Family 61]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 62]]
| ^^^Harry Gilbert^^^
| ''Accepted''
| ^^^Harry Gilbert^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-30 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 63]]
| ^^^Takashi Tonozuka^^^
| ''Accepted''
| ^^^Takashi Tonozuka^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-04-28
|-
| [[Glycoside Hydrolase Family 64]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 65]]
| ^^^Hiroyuki Nakai^^^
| ''Accepted''
| ^^^Hiroyuki Nakai^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-05-29
|-
| [[Glycoside Hydrolase Family 66]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 67]]
| ^^^Harry Gilbert^^^
| ''Accepted''
| ^^^Harry Gilbert^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-10-26 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 68]]
| ^^^Wim Van den Ende^^^
| ''Accepted''
| ^^^Tirso Pons^^^<br>^^^Wim Van den Ende^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-19
|-
| [[Glycoside Hydrolase Family 69]]
| ^^^Bernard Henrissat^^^
|
|
| ''[[:Category:Deleted families|Deleted family]]''
| 2010-01-06
|-
| [[Glycoside Hydrolase Family 70]]
| ^^^Stefan Janecek^^^
| ''Accepted''
| ^^^Magali Remaud-Simeon^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2012-09-05
|-
| [[Glycoside Hydrolase Family 71]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 72]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
| ^^^Jean-Paul Latge^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 73]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
| ^^^Florence Vincent^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-10-28
|-
| [[Glycoside Hydrolase Family 74]]
| ^^^Katsuro Yaoi^^^
| ''Accepted''
| ^^^Katsuro Yaoi^^^<br>^^^Takuya Ishida^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-05-09
|-
| [[Glycoside Hydrolase Family 75]]
| ^^^Ryszard Brzezinski^^^
| ''Accepted''
|
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 76]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 77]]
| ^^^Stefan Janecek^^^
| ''Accepted''
|
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 78]]
| ^^^Kousaku Murata^^^
| ''Accepted''
| ^^^Wataru Hashimoto^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 79]]
| ^^^Satoshi Kaneko^^^
| ''Accepted''
| ^^^Hitomi Ichinose^^^<br>^^^Satoshi Kaneko^^^
| ''[[:Category:Curator approved|Curator approved]]''
| 2012-03-09
|-
| [[Glycoside Hydrolase Family 80]]
| ^^^Ryszard Brzezinski^^^
| ''Accepted''
|
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-07-15
|-
| [[Glycoside Hydrolase Family 81]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 82]]
| ^^^Mirjam Czjzek^^^
| ''Accepted''
| ^^^Gurvan Michel^^^<br>^^^Mirjam Czjzek^^^<br>^^^Etienne Rebuffet^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-17
|-
| [[Glycoside Hydrolase Family 83]]
| ^^^Steve Withers^^^
| ''Accepted''
| ^^^Tom Wennekes^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 84]]
| ^^^Dave Vocadlo^^^
| ''Accepted''
| ^^^Ian Greig^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-02-24
|-
| [[Glycoside Hydrolase Family 85]]
| ^^^Al Boraston^^^
| ''Accepted''
| ^^^Wade Abbott^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-10-28 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 86]]
| ^^^Mirjam Czjzek^^^
| ''Accepted''
| ^^^Mirjam Czjzek^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-11-19
|-
| [[Glycoside Hydrolase Family 87]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 88]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 89]]
| ^^^Al Boraston^^^
| ''Accepted''
| ^^^Ficko-Blean^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-01-06
|-
| [[Glycoside Hydrolase Family 90]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 91]]
| ^^^Bernard Henrissat^^^
|
|
| ''[[:Category:Deleted families|Deleted family]]''
|-
| [[Glycoside Hydrolase Family 92]]
| ^^^Harry Gilbert^^^
| ''Accepted''
| ^^^Harry Gilbert^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-01-04
|-
| [[Glycoside Hydrolase Family 93]]
| ^^^Annabelle Varrot^^^
| ''Accepted''
| ^^^Annabelle Varrot^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-08-05 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 94]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Masafumi Hidaka^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-30 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 95]]
| ^^^Takane Katayama^^^
| ''Accepted''
| ^^^Takane Katayama^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-05-09
|-
| [[Glycoside Hydrolase Family 96]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 97]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Tracey Gloster^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-10-05 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 98]]
| ^^^Al Boraston^^^
| ''Accepted''
| ^^^Fathima Shaikh^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-10-28 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 99]]
| ^^^Gideon Davies^^^
| ''Accepted''
| ^^^Spencer Williams^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2012-01-11
|-
| [[Glycoside Hydrolase Family 100]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 101]]
| ^^^Warren Wakarchuk^^^
| ''Accepted''
| ^^^Warren Wakarchuk^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-10 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 102]]
| ^^^Anthony Clarke^^^
| ''Accepted''
| ^^^Anthony Clarke^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-20
|-
| [[Glycoside Hydrolase Family 103]]
| ^^^Anthony Clarke^^^
| ''Accepted''
| ^^^Anthony Clarke^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-20
|-
| [[Glycoside Hydrolase Family 104]]
| ^^^Anthony Clarke^^^
| ''Accepted''
| ^^^Anthony Clarke^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-02-21
|-
| [[Glycoside Hydrolase Family 105]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 109]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
| ^^^Bernard Henrissat^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-05 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 110]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
| ^^^Bernard Henrissat^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-10 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 111]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 112]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Motomitsu Kitaoka^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2009-07-15 (stamped 2009-11-08)
|-
| [[Glycoside Hydrolase Family 113]]
| ^^^Bernard Henrissat^^^
| ''Accepted''
|
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 114]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 115]]
| ^^^Satoshi Kaneko^^^
| ''Accepted''
| ^^^Satoshi Kaneko^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-05-12
|-
| [[Glycoside Hydrolase Family 116]]
| ^^^Marco Moracci^^^
| ''Accepted''
| ^^^Beatrice Cobucci-Ponzano^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-07-22
|-
| [[Glycoside Hydrolase Family 117]]
| ^^^Mirjam Czjzek^^^
| ''Accepted''
| ^^^Etienne Rebuffet^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2011-05-09
|-
| [[Glycoside Hydrolase Family 118]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 119]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 120]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 121]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Kiyotaka Fujita^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 122]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 123]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 124]]
| ^^^Harry Gilbert^^^
| ''Accepted''
| ^^^Harry Gilbert^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2012-04-27
|-
| [[Glycoside Hydrolase Family 125]]
| ^^^Alisdair Boraston^^^
| ''Accepted''
| ^^^Katie Gregg^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 126]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 127]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Kiyotaka Fujita^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 128]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|-
| [[Glycoside Hydrolase Family 129]]
| ^^^Shinya Fushinobu^^^
| ''Accepted''
| ^^^Hisashi Ashida^^^
| ''[[:Category:Under construction|Under Construction]]''
|-
| [[Glycoside Hydrolase Family 130]]
|
|
|
| ''[[:Category:Unassigned pages|Unassigned]]''
|}

== [[:Category:Glycosyltransferase Families|Glycosyltransferase Families]] ==
Each column is sortable by clicking on the icons in the header (''javascript must be turned on in your browser'').
{| cellspacing="0" cellpadding="4" border="0" class="sortable"
|-
! '''Family'''
! '''[[Responsible Curator]]'''
! '''Curator status'''
! '''[[Author]](s)'''
! '''Page status'''
! '''Date [[:Category:Curator approved|Curator Approved]]'''
|-
| [[Glycosyltransferase Family 42]]
| ^^^Warren Wakarchuk^^^
| ''Accepted''
| ^^^Warren Wakarchuk^^^
| ''[[:Category:Curator approved|Curator Approved]]''
| 2010-07-08
|}

== [[Lexicon]] ==

^^^Steve Withers^^^ and ^^^Spencer Williams^^^ are responsible for the various pages in the [[Lexicon]].

MediaWiki:Sitenotice

2012-09-09T18:07:33Z

Karen Eddy:

<span id="copyright">© 2007-2012 The Authors and Curators of ''CAZypedia''. All rights reserved.</span><br><span id="howToCite" style="color:green">''Contributors and readers: You can cite CAZypedia!</span> [[Cazypedia:Citing|Here's how.]]''

MediaWiki:Sitenotice

2012-09-09T18:05:34Z

Karen Eddy:

Main Page

2012-09-09T18:00:17Z

Karen Eddy:

__NOTOC__

{| id="topbanner" style="width:100%; background:#fcfcfc; margin-top:1.2em; border:1px solid #ccc;"
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<div style="font-size:160%; border:none; margin:0; padding:.1em; color:#000;">Welcome to ''CAZypedia!''</div>
<div style="top:+0.2em; font-size:100%;">The Encyclopedia of Carbohydrate-Active Enzymes.</div>
<div id="articlecount" style="width:100%; text-align:center; font-size:85%;">
Now containing {{CuratorApprovedGHPages}} [[:Category:Curator approved|Curator-approved]] [[Glycoside Hydrolase Families|GH family pages]],
<br>{{CuratorApprovedGTPages}} [[:Category:Curator approved|Curator-approved]] [[Glycosyltransferase Families|GT family pages<sup>''(beta)''</sup>]],<br>
and {{CuratorApprovedLexiconPages}} [[:Category:Curator approved|Curator-approved]] [[Lexicon|lexicon pages]]!

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| style="font-size:95%; padding:10px 0; margin:0; text-align:left; white-space:nowrap; color:#000;" | [[Cazypedia:About|About ''CAZypedia'']] '''·''' [[Cazypedia:Citing|Citing]] '''·''' [[Special:Contact|Contact]] '''·''' [[Help:Contents|Help!]]
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[[Glycoside Hydrolase Families|GH Families]] '''·''' [[Glycosyltransferase Families|GT Families<sup>''(beta)''</sup>]] '''·''' [[Lexicon]] '''·''' [[Special:RecentChanges|Recent changes]]
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|-
| style="color:#000;padding: 2px 5px 5px" | ''CAZypedia'' is dedicated to the late [[Bruce Stone|Prof. Bruce Stone]], whose enthusiasm to create a comprehensive encyclopedia of carbohydrate-active enzymes was essential in the genesis of this project.
|}
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Main Page

2012-09-09T17:59:00Z

Karen Eddy:

__NOTOC__

{| id="topbanner" style="width:100%; background:#fcfcfc; margin-top:1.2em; border:1px solid #ccc;"
| style="width:60%; color:#000;" |

{| style="width:100%; border:none; background:none;"
| style="width:100%; text-align:center; white-space:nowrap; color:#000;" |
<div style="font-size:160%; border:none; margin:0; padding:.1em; color:#000;">Welcome to ''CAZypedia!''</div>
<div style="top:+0.2em; font-size:100%;">The Encyclopedia of Carbohydrate-Active Enzymes.</div>
<div id="articlecount" style="width:100%; text-align:center; font-size:85%;">
Now containing {{CuratorApprovedGHPages}} [[:Category:Curator approved|Curator-approved]] [[Glycoside Hydrolase Families|GH family pages]],
<br>{{CuratorApprovedGTPages}} [[:Category:Curator approved|Curator-approved]] [[Glycosyltransferase Families|GT family pages<sup>''(beta)''</sup>]],<br>
and {{CuratorApprovedLexiconPages}} [[:Category:Curator approved|Curator-approved]] [[Lexicon|lexicon pages]]!

</div>
|}

| style="width:40%; font-size:95%;"|
[[Image:cazypedia_logo_big.png|right]]
|}

{| id="strapline" style="width:100%; background:none; margin:-.8em 0 -.7em 0;"
| style="font-size:95%; padding:10px 0; margin:0; text-align:left; white-space:nowrap; color:#000;" | [[Cazypedia:About|About ''CAZypedia'']] '''·''' [[Cazypedia:Citing|Citing]] '''·''' [[Special:Contact|Contact]] '''·''' [[Help:Contents|Help!]]
| style="font-size:95%; padding:10px 0; margin:0; text-align:right; white-space:nowrap; color:#000;" |
[[Glycoside Hydrolase Families|GH Families]] '''·''' [[Glycosyltransferase Families|GT Families<sup>''(beta)''</sup>]] '''·''' [[Lexicon]] '''·''' [[Special:RecentChanges|Recent changes]]
|}


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|-
| style="color:#000;font-size:95%;padding:2px 5px 5px" | <div id="RightColumnText2">{{News}}<small>[[News|''> older news'']]</small></div>
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|-
| style="color:#000;padding: 2px 5px 5px" | ''CAZypedia'' is dedicated to the late [[Bruce Stone|Prof. Bruce Stone]], whose enthusiasm to create a comprehensive encyclopedia of carbohydrate-active enzymes was essential in the genesis of this project.
|}
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Template:ContentDescriptionForMainPage

2012-09-09T17:57:36Z

Karen Eddy:

''CAZypedia'' is presently focussed on the [[Glycoside Hydrolase Families]] defined in the [http://www.cazy.org/fam/acc_GH.html CAZy Database]. Other catabolic and anabolic CAZymes, as well as carbohydrate-binding modules, may be included in the future. In addition, there is a [[:Category:Definitions_and_explanations|lexicon]] of terms relevant to CAZymes and carbohydrate chemistry.<br><div class="mainPageSubline">''These and other aspects of CAZypedia's content can be accessed through the menus on the left side of each page.''</div>

Template:Purpose

2012-09-09T17:57:02Z

Karen Eddy:

''CAZypedia'' has been initiated as a community-driven resource to assemble a comprehensive encyclopedia of the "CAZymes," the [[Carbohydrate-active enzymes|<u>c</u>arbohydrate-<u>a</u>ctive en<u>zymes</u>]] and binding proteins involved in the synthesis and degradation of complex carbohydrates. ''CAZypedia'' is inspired by, and closely connected with, the actively curated [http://www.cazy.org CAZy Database].<br><div class="mainPageSubline">''It's probably fair to say that CAZypedians are, like our friends at the [http://www.cazy.org CAZy DB], a group of [http://dx.doi.org/10.1371/journal.pcbi.0020142 "biocurators."]''</div>

Template:HowCAZypediaWorks

2012-09-09T17:56:13Z

Karen Eddy:

''CAZypedia'' is built on authoring and editing principles similar to those of other expert-based online encyclopedias (''cf. [http://www.citizendium.org/ Citizendium]''). All contributors to ''CAZypedia'', from the [[Author|Authors]] to the [[Board of Curators]], are selected experts in the field. Transparency is achieved through the use of contributors' real names and [[:Category:Contributors|published biographies]] in ''CAZypedia''. Individual entries in ''CAZypedia'' are managed by [[Responsible Curator|Responsible Curators]], who are responsible for selecting expert [[Author|Authors]] and coordinating author contributions on individual pages. Selection of [[Responsible Curator|Responsible Curators]], based on their specialist expertise and ability to participate in the ''active maintenance'' of entry content, is handled by the [[Board of Curators|Senior Curators]].<br><div class="mainPageSubline">''More information on CAZypedia's content and editorial policies is available [[Cazypedia:About|here]].''</div>

Glycoside Hydrolase Family 115

2012-06-21T22:28:39Z

Karen Eddy:

{{CuratorApproved}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH115'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH115.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH115 display α-glucuronidase activity. In particular, members of this family catalyze the cleavage of 4-''O''-methyl D-glucuronic acid sidechains from native xylan polysaccharides (EC [{{EClink}}3.2.1.131 3.2.1.131)]. In contrast to [[GH67]] enzymes, which only cleave glucuronosyl linkages at the non-reducing ends of xylooligosaccharides, GH115 enzymes remove glucuronic acid from the both terminal and internal regions of xylooligosaccharides and xylans <cite>Ryabova2009</cite>. This substrate specificity was first demonstrated by an α-glucuronidase purified from ''Thermoascus aurantiacus'' <cite>Khandke1989</cite>, and later for a ''Schizophyllum commune'' α-glucuronidase <cite>Tenkanen2000</cite>. Although GH115 was established on the basis of biochemical and sequence analysis of ''Pichia stipitis'' (4-''O''-methyl)-α-glucuronidase <cite>Ryabova2009</cite>, available N-terminal protein sequence of the ''S. commune'' enzyme <cite>Tenkanen2000</cite> allowed the tentative assignment of this enzyme to GH115 <cite>Ryabova2009</cite>, which was later confirmed by the full protein sequence <cite>Chong2011</cite>. A GH115 member from ''Streptomyces pristinaespiralis'' produces both 4-''O''-methyl-D-glucuronic acid and non-methylated D-glucuronic acid from xylan and xylo-oligosaccharides <cite>Fujimoto2011</cite>.

== Kinetics and Mechanism ==
Using reduced aldopentauronic acid (MeGlcA3Xyl4-ol) as a substrate, analysis by <sup>1</sup>H-NMR spectroscopy revealed that the enzymes from both ''S. commune'' and ''P. stipitis'' release the β-anomer of 4-O-methyl-D-glucuronic acid (MeGlcA) as the first-formed product, thus suggesting a one step, [[inverting]] mechanism <cite>Kolenova2010</cite>.

== Catalytic Residues ==
The catalytic residues have not yet been identified in a member of this family.

== Three-dimensional structures ==
No 3D structure has been solved for this family at present, although crystallization of a ''Streptomyces pristinaespiralis'' homolog has been reported <cite>Fujimoto2011</cite>.

== Family Firsts ==
;First stereochemistry determination: Release of the β-anomer of 4-methyl-D-glucuronic acid by both the ''Schizophyllum commune'' and ''Pichia stipitis'' enzymes using <sup>1</sup>H NMR <cite>Kolenova2010</cite>.
;First [[general acid]] residue identification: Not yet identified.
;First [[general base]] residue identification: Not yet identified.
;First 3-D structure: Crystallization of the ''Streptomyces pristinaespiralis'' family member has been reported <cite>Fujimoto2011</cite>.

== References ==
<biblio>
#Khandke1989 pmid=2802623
#Tenkanen2000 pmid=10725538
#Ryabova2009 pmid=19344716
#Kolenova2010 pmid=20804758
#Fujimoto2011 pmid=21206027
#Chong2011 pmid=21442271
</biblio>

[[Category:Glycoside Hydrolase Families|GH115]]

Glycoside Hydrolase Family 115

2012-06-21T22:28:09Z

Karen Eddy:

{{CuratorApproved}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH115'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH115.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH115 display α-glucuronidase activity. In particular, members of this family catalyze the cleavage of 4-''O''-methyl D-glucuronic acid sidechains from native xylan polysaccharides (EC [{{EClink}}3.2.1.131 3.2.1.131)]. In contrast to [[GH67]] enzymes, which only cleave glucuronosyl linkages at the non-reducing ends of xylooligosaccharides, GH115 enzymes remove glucuronic acid from the both terminal and internal regions of xylooligosaccharides and xylans <cite>Ryabova2009</cite>. This substrate specificity was first demonstrated by an α-glucuronidase purified from ''Thermoascus aurantiacus'' <cite>Khandke1989</cite>, and later for a ''Schizophyllum commune'' α-glucuronidase <cite>Tenkanen2000</cite>. Although GH115 was established on the basis of biochemical and sequence analysis of ''Pichia stipitis'' (4-''O''-methyl)-α-glucuronidase <cite>Ryabova2009</cite>, available N-terminal protein sequence of the ''S. commune'' enzyme <cite>Tenkanen2000</cite> allowed the tentative assignment of this enzyme to GH115 <cite>Ryabova2009</cite>, which was later confirmed by the full protein sequence <cite>Chong2011</cite>. A GH115 member from ''Streptomyces pristinaespiralis'' produces both 4-''O''-methyl-D-glucuronic acid and non-methylated D-glucuronic acid from xylan and xylo-oligosaccharides <cite>Fujimoto2011</cite>.

== Kinetics and Mechanism ==
Using reduced aldopentauronic acid (MeGlcA3Xyl4-ol) as a substrate, analysis by <sup>1</sup>H-NMR spectroscopy revealed that the enzymes from both ''S. commune'' and ''P. stipitis'' release the β-anomer of 4-O-methyl-D-glucuronic acid (MeGlcA) as the first-formed product, thus suggesting a one step, [[inverting]] mechanism <cite>Kolenova2010</cite>.

== Catalytic Residues ==
The catalytic residues have not yet been identified in a member of this family.

== Three-dimensional structures ==
No 3D structure has been solved for this family at present, although crystallization of a ''Streptomyces pristinaespiralis'' homolog has been reported <cite>Fujimoto2011</cite>.

== Family Firsts ==
;First stereochemistry determination: Release of the β-anomer of 4-methyl-D-glucuronic acid by both the ''Schizophyllum commune'' and ''Pichia stipitis'' enzymes using <sup>1</sup>H NMR <cite>Kolenova2010</cite>.
;First [[general acid]] residue identification: Not yet identified.
;First [[general base]] residue identification: Not yet identified.
;First 3-D structure: Crystallization of the ''Streptomyces pristinaespiralis'' family member has been reported <cite>Fujimoto2011</cite>.

== References ==
<biblio>
#Khandke1989 pmid=2802623
#Tenkanen2000 pmid=10725538
#Ryabova2009 pmid=19344716
#Kolenova2010 pmid=20804758
#Fujimoto2011 pmid=21206027
#Chong2011 Chong SL, Battaglia E, Coutinho PM, Henrissat B, Tenkanen M, de Vries RP. ''The α-glucuronidase Agu1 from Schizophyllum commune is a member of a novel glycoside hydrolase family (GH115).'' Appl Microbiol Biotechnol. 2011 May;90(4):1323-1332. //''Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out:'' [http://dx.doi.org/10.1007/s00253-011-3157-y DOI:10.1007/s00253-011-3157-y] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21442271 PMID: 21442271]
</biblio>

[[Category:Glycoside Hydrolase Families|GH115]]

Glycoside Hydrolase Family 115

2012-06-21T22:27:22Z

Karen Eddy:

{{CuratorApproved}}
* [[Author]]: ^^^Satoshi Kaneko^^^
* [[Responsible Curator]]: ^^^Satoshi Kaneko^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH115'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|inverting
|-
|'''Active site residues'''
|not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH115.html
|}
</div>


== Substrate specificities ==
[[Glycoside hydrolases]] of GH115 display α-glucuronidase activity. In particular, members of this family catalyze the cleavage of 4-''O''-methyl D-glucuronic acid sidechains from native xylan polysaccharides (EC [{{EClink}}3.2.1.131 3.2.1.131)]. In contrast to [[GH67]] enzymes, which only cleave glucuronosyl linkages at the non-reducing ends of xylooligosaccharides, GH115 enzymes remove glucuronic acid from the both terminal and internal regions of xylooligosaccharides and xylans <cite>Ryabova2009</cite>. This substrate specificity was first demonstrated by an α-glucuronidase purified from ''Thermoascus aurantiacus'' <cite>Khandke1989</cite>, and later for a ''Schizophyllum commune'' α-glucuronidase <cite>Tenkanen2000</cite>. Although GH115 was established on the basis of biochemical and sequence analysis of ''Pichia stipitis'' (4-''O''-methyl)-α-glucuronidase <cite>Ryabova2009</cite>, available N-terminal protein sequence of the ''S. commune'' enzyme <cite>Tenkanen2000</cite> allowed the tentative assignment of this enzyme to GH115 <cite>Ryabova2009</cite>, which was later confirmed by the full protein sequence <cite>Chong2011</cite>. A GH115 member from ''Streptomyces pristinaespiralis'' produces both 4-''O''-methyl-D-glucuronic acid and non-methylated D-glucuronic acid from xylan and xylo-oligosaccharides <cite>Fujimoto2011</cite>.

== Kinetics and Mechanism ==
Using reduced aldopentauronic acid (MeGlcA3Xyl4-ol) as a substrate, analysis by <sup>1</sup>H-NMR spectroscopy revealed that the enzymes from both ''S. commune'' and ''P. stipitis'' release the β-anomer of 4-O-methyl-D-glucuronic acid (MeGlcA) as the first-formed product, thus suggesting a one step, [[inverting]] mechanism <cite>Kolenova2010</cite>.

== Catalytic Residues ==
The catalytic residues have not yet been identified in a member of this family.

== Three-dimensional structures ==
No 3D structure has been solved for this family at present, although crystallization of a ''Streptomyces pristinaespiralis'' homolog has been reported <cite>Fujimoto2011</cite>.

== Family Firsts ==
;First stereochemistry determination: Release of the β-anomer of 4-methyl-D-glucuronic acid by both the ''Schizophyllum commune'' and ''Pichia stipitis'' enzymes using <sup>1</sup>H NMR <cite>Kolenova2010</cite>.
;First [[general acid]] residue identification: Not yet identified.
;First [[general base]] residue identification: Not yet identified.
;First 3-D structure: Crystallization of the ''Streptomyces pristinaespiralis'' family member has been reported <cite>Fujimoto2011</cite>.

== References ==
<biblio>
#Khandke1989 pmid=2802623
#Tenkanen2000 pmid=10725538
#Ryabova2009 pmid=19344716
#Kolenova2010 pmid=20804758
#Fujimoto2011 Fujimoto Z, Ichinose H, Biely P, Kaneko S. ''Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 α-glucuronidase from Streptomyces pristinaespiralis.'' Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):68-71. //''Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out:'' [http://dx.doi.org/10.1107/S1744309110043721 DOI:10.1107/S1744309110043721] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21206027 PMID: 21206027]
#Chong2011 Chong SL, Battaglia E, Coutinho PM, Henrissat B, Tenkanen M, de Vries RP. ''The α-glucuronidase Agu1 from Schizophyllum commune is a member of a novel glycoside hydrolase family (GH115).'' Appl Microbiol Biotechnol. 2011 May;90(4):1323-1332. //''Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out:'' [http://dx.doi.org/10.1007/s00253-011-3157-y DOI:10.1007/s00253-011-3157-y] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21442271 PMID: 21442271]
</biblio>

[[Category:Glycoside Hydrolase Families|GH115]]

File:FIGURE ChiA ChiB.jpg

2012-06-21T20:57:02Z

Karen Eddy: Karen Eddy uploaded a new version of "File:FIGURE ChiA ChiB.jpg"

Glycoside Hydrolase Family 35

2012-06-14T22:11:26Z

Karen Eddy:

{{CuratorApproved}}
* [[Author]]s: ^^^Anna Kulminskaya^^^, ^^^Mirko Maksimainen^^^, ^^^Juha Rouvinen^^^
* [[Responsible Curator]]: ^^^Anna Kulminskaya^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH35'''
|-
|'''Clan'''
|GH-A
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH35.html
|}
</div>


== Substrate specificities ==
The majority of [[glycoside hydrolases]] of GH35 are β-galactosidases (EC [{{EClink}}3.2.1.23 3.2.1.23]). GH35 enzymes have been isolated from microorganisms such as fungi, bacteria and yeasts, as well as higher organisms such as plants, animals, and human cells. These β-galactosidases catalyse the hydrolysis of terminal non-reducing β-D-galactose residues in, for example, lactose (1,4-O-β-D-galactopyranosyl-D-glucose), oligosaccharides, glycolipids, and glycoproteins. Various GH35 β-galactosidases demonstrate specificity towards β-1,3-, β-1,6- or β-1,4-galactosidic linkages <cite>Zinin2002, Gamauf2007, Tanthanuch2008</cite>, and are often most active under acidic conditions <cite>Zhang1994, vanCasteren2000, Wang2009</cite>. As with many other CAZy families <cite>GeislerLee2006, Henrissat2001, Tuskan2006</cite>, GH35 members tend to be represented by multi-gene families in plants <cite>Ahn2007, Smith2000, Lazan2004, Ross1994, Tanthanuch2008</cite>. Moreover, plant GH35 β-galactosidases have be divided into two classes: members of the first are capable of hydrolyzing pectic β-1,4-galactans, while those of the second can specifically cleave β-1,3- and β-1,6-galactosyl linkages of arabinogalactan proteins <cite>Kotake2005</cite>.

In addition to β-galactosidases, GH35 also contains a limited number of archeal [[exo]]-β-glucosaminidases (EC [{{EClink}}3.2.1.165 3.2.1.165]) <cite>Tanaka2003 Liu2006</cite>. Such enzymes hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from non-reducing termini.

== Kinetics and Mechanism ==
Beta-galactosidases of GH35 catalyze the hydrolysis of terminal β-galactosyl residues via a [[classical Koshland retaining mechanism]], which leads to net retention of the β-anomeric configuration of the released galactose molecule. The stereochemistry of the reaction was first shown by NMR for the human β-galactosidase precursor <cite>Zhang1994</cite> and has been subsequently confirmed by other investigators for microbial and plant enzymes <cite>vanCasteren2000, Zinin2002</cite> .

== Catalytic Residues ==
The catalytic residues for family 35 were first predicted on the basis of hydrophobic cluster analysis of proteins of similar protein fold <cite>Henrissat1995</cite>. Experimentally, the glutamic acid residue 268 was first identified as the [[catalytic nucleophile]] in human lysosomal β-galactosidase precursor using a slow substrate, 2,4-dinitrophenyl 2-deoxy-2-fluoro-β-D-galactopyranoside, which allowed trapping of a covalent glycosyl-enzyme intermediate and subsequent peptide mapping <cite>McCarter1997</cite>. This approach was repeated for two bacterial β-galactosidases from ''Xanthomonas manihotis'' and ''Bacillus circulans'' <cite>Blanchard2001</cite>. The [[general acid/base]] residue was inferred to be Glu200 from structural studies of a ''Penicillium'' sp. β-galactosidase <cite>Rojas2004</cite>. Recent structural studies (''vide infra'') revealed two different conformations of the [[general acid/base]] residue in the β-galactosidase of ''Trichoderma reesei'' <cite> Maksimainen2010</cite>.

== Three-dimensional structures ==
The first 3D-structures of a GH35 enzyme, those of a β-galactosidase from ''Pencillium'' sp. (Psp-β-gal) in native (PDB [{{PDBlink}}1tg7 1tg7]) and product-complexed (PDB [{{PDBlink}}1xc6 1xc6]) forms, were reported in 2004 at 1.90 Å and 2.10 Å resolution, respectively <cite>Rojas2004</cite>. The structure of a β-galactosidase from ''Bacteriodes thetaiotamicron'' (Btm-β-gal) was subsequently reported by the New York Structural GenomiX Research Consortium in 2008 at 2.15 Å resolution (PDB [{{PDBlink}}3d3a 3d3a]). In 2010, an atomic (1.2 Å) resolution crystal structure of a ''Trichoderma reesei'' (''Hypocrea jecorina'') β-galactosidase (Tr-β-gal, PDB [{{PDBlink}}3og2 3og2]) was reported, together with complex structures with galactose, IPTG and PETG at 1.5, 1.75 and 1.4 Å resolutions, respectively (PDB codes [{{PDBlink}}3ogr 3ogr], [{{PDBlink}}3ogs 3ogs], and [{{PDBlink}}3ogv 3ogv], respectively) <cite>Maksimainen2010</cite>.

GH35 enzymes belong to Clan GH-A, and thus have an (α/β)<sub>8</sub> (TIM) barrel as the catalytic domain, in which two glutamic acid residues act as the general acid-base and nucleophilic catalysts. These residues are located in strands 4 and 7 of the barrel.

The comparison of the native structures of Psp-β-gal, Tr-β-gal and Btmβ-gal reveals two things ('''Figure 1'''): Firstly, Btm-β-gal consists of three distinct domains, whereas Psp-β-gal and Tr-β-gal consist of five and six domains, respectively. The second and third domains of Btm-β-gal are quite similar with the fourth and fifth domains of Psp-β-gal, and with the fifth and sixth domains of Tr-β-gal. Secondly, major structural differences between Psp-β-gal and Tr-β-gal are in the conformations of the loop regions. Although the crystal structures of Psp-β-gal and Tr-β-gal are similar, the interpretation of the structure of Tr-β-gal is somewhat different from that presented earlier for Psp-β-gal: Rojas et al. considered Psp-β-gal to be composed of five distinct structural domains. The overall structure is built around the first, TIM barrel, domain. Domain 2 is an all β-sheet domain containing an immunoglobulin-like subdomain, Domain 3 is based on a Greek-key β-sandwich, and Domains 4 and 5 are jelly rolls <cite>Rojas2004</cite>. In contrast, Maksimainen et al. concluded the domain 2 includes two different domains and thus the Tr-β-gal and Psp-β-gal structures both form six similar domains <cite>Maksimainen2010</cite>.

The superimposition of the active sites of the GH35 β-galactosidases shows a remarkable similarity. In addition to the catalytic residues, the active sites of the GH35 β-galactosidases contain many identical residues ('''Figure 1B'''). Based on the galactose-bound crystallographic models of Psp-β-gal and Tr-β-gal, a single galactose molecule is bound to the active site of the GH35 enzyme in the chair conformation in the β-anomeric configuration.

Additionally, Maksimainen et al. have described conformational changes in two loop regions of the active site of Tr-β-gal, that implicates a conformational selection mechanism for the enzyme (Figure 2). Unlike the induced fit theory, which assumes that the initial interaction between a protein and its binding partner induces a conformational change in the protein through a stepwise process, the conformational selection theory is based on the assumption that the unbound protein exists as an ensemble of conformations in dynamic equilibrium. Interaction between a weakly populated, higher-energy conformation and a binding partner causes the equilibrium to move in favor of the selected conformation <cite>Tsai1999, Boehr2008</cite>. This can be seen in the structures of Tr-β-gal: the open and closed conformation are both favorable in the native structure and the closed conformation becomes more favorable in the complex structures. Furthermore, The acid/base catalyst Glu200 has two different conformations in the IPTG and PETG complex structures that clearly affects the p''K''<sub>a</sub> value of this residue and thus the catalytic mechanism of the enzyme <cite>Maksimainen2010</cite>.

=== Structure images ===

[[Image: GH35 comparison.png|thumb|left|750px|'''Figure 1. Comparison of the native structures of GH35 β-galactosidases.''' A. Global structures, B. Active sites. Psp-β-gal (PDB code [{{PDBlink}}1tg7 1tg7]), Tr-β-gal (PDB code [{{PDBlink}}3og2 3og2]) and Btm-β-gal (PDB code [{{PDBlink}}3d3a 3d3a]) are colored in green, brown and blue, respectively.]]

[[Image: Conformational selection.png|thumb|left|750px| '''Figure 2. Illustration of the conformational selection mechanism observed in Tr-β-gal <cite>Maksimainen2010</cite>.''']]

<br style="clear: both" />

== Family Firsts ==
;First stereochemistry determination:
[[Retaining]] stereochemical outcome for human β-galactosidase precursor by NMR <cite>Zhang1994</cite>

;First [[catalytic nucleophile]] identification:
Human β-galactosidase precursor by 2-fluorogalactose labeling <cite>McCarter1997</cite>.

;First [[general acid/base]] residue identification:
''Penicillium sp.'' β-galactosidase by structural identification <cite>Rojas2004</cite>.

;First 3-D structure:
''Penicillium sp.'' β-galactosidase <cite>Rojas2004</cite>.

== References ==
<biblio>
#Ahn2007 pmid=17466346
#Smith2000 pmid=10889266
#Lazan2004 pmid=15694277
#Ross1994 pmid=7991682
#Tanthanuch2008 pmid=18664295
#Tanka2003 pmid=12923090
#Liu2006 pmid=16912928
#Zhang1994 pmid=7998946
#Henrissat1995 pmid=7624375
#McCarter1997 pmid=8995274
#Rojas2004 pmid=15491613
#Blanchard2001 pmid=11423106
#Maksimainen2010 pmid=21130883
#GeislerLee2006 pmid=16415215
#Henrissat2001 pmid=11554480
#Tuskan2006 pmid=16973872
#Gamauf2007 pmid=17381511
#Zinin2002 pmid=11909597
#vanCasteren2000 pmid=11086688
#Wang2009 pmid=19453169
#Kotake2005 pmid=15980190
#Boehr2008 Boehr DD, Wright PE ''How do proteins interact?'' Science 2008, 320 1429-1430.
#Tsai1999 pmid=10468538
</biblio>

[[Category:Glycoside Hydrolase Families|GH035]]

User:Hisashi Ashida

2012-06-12T20:24:04Z

Karen Eddy:

[[Image:ashida.jpg|200px|right]]
Hisashi Ashida is a professor in the Department of Science and Technology on Food Safety, Faculty of Biology-Oriented Science and Technology, Kinki University. He graduated from Kyoto University in 1988, and received his Ph.D. degree of Agricultural Science from the same university in 2000 under the supervision of Prof. Kenji Yamamoto. He became a post-doctoral fellow at the Department of Biochemistry, Tulane University School of Medicine (Prof. Yu-Teh Li) from 2000 to 2001, and then at the Research Institute for Microbial Diseases, Osaka University (Prof. Taroh Kinoshita) from 2001 to 2004. He obtained the position of an assistant professor at Prof. Kinoshita’s laboratory in 2004. In 2006, he moved to the Graduate School of Biostudies, Kyoto University (Prof. Yamamoto), and promoted to an associate professor in 2008. He moved to Kinki University in 2012. His research interests are the metabolism of complex carbohydrates in animals and microbes. He discovered [[GH129]] <cite>Kiyohara2012a</cite>, and also contributed to the discoveries of [[GH98]] <cite>Anderson2005</cite> and [[GT76]] <cite>Kang2005</cite>.

----
<biblio>
#Kiyohara2012a pmid=22090027
#Anderson2005 pmid=15618227
#Kang2005 pmid=15623507

</biblio>

User:Shinya Fushinobu

2012-06-12T20:23:08Z

Karen Eddy:

[[Image:Fushinobu.jpg|200px|right]]

I am an Associate Professor at [http://enzyme13.bt.a.u-tokyo.ac.jp/index-e.html Laboratory of Enzymology] in Department of Biotechnology, [http://www.a.u-tokyo.ac.jp/english/index.html Graduate School of Agricultural and Life Sciences], [http://www.u-tokyo.ac.jp/index_e.html The University of Tokyo] located in Tokyo, Japan. Raised in [http://www.city.kure.hiroshima.jp/english/index.html Kure], Hiroshima, Japan. I obtained Ph.D degree in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo in 1999. My research interests concern structure and function of enzymes, mainly those of Carbohydrate-Active enZymes. My home page is [http://enzyme13.bt.a.u-tokyo.ac.jp/fushi/index-e.html here]. I contributed to three-dimensional structure determination of

*[[GH1]] ''Phanerochaete chrysosporium'' β-glucosidase 1B (BGL1B) <cite>Nijikken2007</cite>
*[[GH3]] ''Kluyveromyces marxianus'' β-glucosidase (''Km''BglI) <cite>Yoshida2010</cite>
*[[GH8]] ''Bacillus halodurans'' reducing-end xylose-releasing exo-oligoxylanase (Rex) <cite>Fushinobu2005</cite>
*[[GH10]] ''Clostridium stercorarium'' xylanase B (XynB) <cite>Nishimoto2007</cite>
*[[GH11]] ''Aspergillus kawachii'' xylanase C (XynC) <cite>Fushinobu1998</cite>
*[[GH29]] ''Bifidobacterium longum'' subsp. ''infantis'' 1,3-1,4-α-L-fucosidase (''Bi''AfcB) <cite>Sakurama2012</cite>
*[[GH42]] ''Thermus thermophilus'' β-galactosidase (A4-β-Gal) '''Family First''' <cite>Hidaka2002</cite>
*[[GH51]] ''Thermotoga maritima'' α-L-arabinofuranosidase (''Tm''-AFase) <cite>Im2012</cite>
*[[GH54]] ''Aspergillus kawachii'' α-L-arabinofuranosidase B (AkAbfB) '''Family First''' plus identification of CBM42 <cite>Miyanaga2004</cite>
*[[GH55]] ''Phanerochaete chrysosporium'' β-1,3-glucanase (Lam55A) '''Family First''' <cite>Ishida2009</cite>
*[[GH57]] ''Thermococcus litoralis'' 4-α-glucanotransferase (TLGT) '''Family First''' <cite>Imamura2003</cite>
*[[GH94]] ''Vibrio proteolyticus'' chitobiose phosphorylase (ChBP) '''Family First''' <cite>Hidaka2004</cite>
*[[GH94]] ''Cellvibrio gilvus'' cellobiose phosphorylase (CBP) <cite>Hidaka2006</cite>
*[[GH101]] ''Bifidobacterium longum'' endo-α-''N''-acetylgalactosaminidase (EngBF) <cite>Suzuki2009</cite>
*[[GH112]] ''Bifidobacterium longum'' galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) '''Family First''' <cite>Hidaka2009</cite>
*PL20 ''Trichoderma reesei'' endo-β-1,4-glucuronan lyase (TrGL) '''Family First''' <cite>Konno2009</cite>
*CBM28 in ''Clostridium josui'' Cel5A (''Cj''CBM28) <cite>Tsukimoto2010</cite>

----

<biblio>
#Nijikken2007 pmid=17376440
#Yoshida2010 pmid=20662765
#Fushinobu2005 pmid=15718242
#Nishimoto2007 pmid=17383976
#Fushinobu1998 pmid=9930661
#Hidaka2002 pmid=12215416
#Miyanaga2004 pmid=15292273
#Ishida2009 pmid=19193645
#Imamura2003 pmid=12618437
#Hidaka2004 pmid=15274915
#Hidaka2006 pmid=16646954
#Suzuki2009 pmid=19502354
#Hidaka2009 pmid=19124470
#Konno2009 pmid=19306878
#Tsukimoto2010 pmid=20159017
#Im2012 pmid=22313787
#Sakurama2012 pmid=22451675
</biblio>

[[Category:Contributors|Fushinobu, Shinya]]

Glycoside Hydrolase Family 84

2012-06-12T20:21:52Z

Karen Eddy:

{{CuratorApproved}}
* [[Author]]: ^^^Ian Greig^^^
* [[Responsible Curator]]: ^^^David Vocadlo^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH84'''
|-
|'''Clan'''
|none
|-
|'''Mechanism'''
|retaining
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |http://www.cazy.org/GH84.html
|}
</div>


== Substrate specificities ==

[[Glycoside hydrolases]] of GH84 include ''β''-''N''-acetylglucosaminidases but members have often also been annotated as ''β''-''N''-acetylhyaluronidases. This second annotation arises from the initial cloning of the enzyme and its early sequence analysis, which suggested sequence similarity to ''β''-''N''-acetylhyaluronidases <cite>Heckel98</cite>. Biochemical analysis of a GH84 enzyme annotated in as a hyaluronidase, however, revealed that it had no such activity <cite>Black2006</cite> and structural studies of other homologues have suggested the active site would be unable to process polymeric hyaluronan. Humans possess only one enzyme belonging to GH84, first defined by its unique biochemical properties including activity at neutral pH and selectivity for ''N''-acetylglucosamine residues. The human GH84 enzyme was labelled as HexC to distinguish it from the human [[GH20]] lysosomal enzymes HexA and HexB. HexC was first cloned from a meningoma library using autologous serum and defined as meningoma expressed antigen 5 (MGEA5) <cite>Heckel98</cite>. It was later cloned and biochemically characterized as ''O''-GlcNAcase, a nuclear and cytoplasmic enzyme targeting glycoprotein substrates modified by ''β''-linked GlcNAc residues linked to serine and threonine residues <cite>Gao01 Dong94</cite>. A truncated, nuclear-localized isoform of human ''O''-GlcNAcase lacking a putative C-terminal histone acetyl transferase domain retains similar kinetic properties (aside from a much lower activity) and inhibition patterns as the full-length cytosolic isoform and is consistent with hexosaminidase activity residing in the ''N''-terminal domain, which shares similarity with other GH84 enzymes <cite>DJV2009Trunc</cite>. In contrast to the ''β''-hexosaminidases of [[GH20]] a relaxed specificity for substitutions of the ''N''-acyl group is observed with residues significantly more bulky than the ''N''-acyl group being tolerated <cite>DJV2005</cite>.

== Kinetics and Mechanism ==
Members of GH84 are [[retaining]] enzymes that use a catalytic mechanism of [[neighboring group participation]], this originally being established through the use of free-energy relationship-based studies of human ''O''-GlcNAcase <cite>DJV2005</cite>. More recent studies of the human enzyme have investigated variations in rates of reaction (''V/K'') with both nucleophile and leaving group structures <cite>DJV2009</cite>. For substrates possessing the naturally-occurring acetyl nucleophile a pre-chemical step is rate-determining on ''V/K'' for leaving groups with a p''K''<sub>a</sub> below 11 (with the chemical step rate-determining for substrates with higher p''K''<sub>a</sub> values). Studies of substrates possessing fluoroacetyl nucleophiles highlighted that a dissociative (D<sub>N</sub>*A<sub>N</sub>) <cite>Guthrie89</cite> mechanism involving [[general acid]] catalysis operates for the hydrolysis of substrates possessing leaving groups with a p''K''<sub>a</sub> greater than approximately 7; a concerted (A<sub>N</sub>D<sub>N</sub>) <cite>Guthrie89</cite> mechanism, not employing general acid catalysis was found for substrates possessing leaving groups with lower p''K''<sub>a</sub> values (consistent with prior studies showing hydrolysis of 1-''S''-glucosaminides <cite>DJV2005Thio</cite>).

Numerous carbohydrate and carbohydrate like-scaffolds have been reported as potent inhibitors of GH84 enzymes. These include "NAG-thiazolines" <cite>DJV2005</cite>, PUGNAc (''O''-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-''N''-phenylcarbamate) <cite>Stubbs06</cite>, GlcNAcstatins <cite>Dorf2006 Vasella2006</cite>, 6-''epi''-valeinamines <cite>Stick2007</cite>, and 6-acetamido-6-deoxy-castanospermine <cite>Mac2010</cite>. The greater tolerance of the ''N''-acyl binding pockets of GH84 enzymes for bulky sidechains compared to those of [[GH20]] enzymes has enabled the development of inhibitors that are not only highly potent but also highly selective in their inhibition of human nucleocytoplasmic ''O''-GlcNAcase (GH84) over human lysosomal ''β''-hexosaminidases <cite>DJV2005 Whitworth2007 Dorf2010</cite>. Many of these families of inhibitors possess structural characteristics reminiscent of the [[oxocarbenium ion]]-like transition states of glycosyl group transfer and, as such may loosely be termed '[[transition state]] analogues'. An analysis of NAG-thiazoline- and PUGNAc-derived inhibitors of human ''O''-GlcNAcase has shown that only the NAG-thiazolines position the inhibitors and their ''N''-acyl side-chains within the hydrophobic binding pocket in a manner consistent with the species found along the reaction coordinate <cite>Whitworth2007</cite>. As such NAG-thiazoline inhibitors may be termed 'Bartlett-type' (free-energy relationship-based) <cite>Bartlett1997</cite> [[transition state]] analogues. Significantly streptozotocin, a widely used diabetogenic compound whose toxicity towards pancreatic β-cells was hypothesized to arise from its ability to act as an inhibitor of human ''O''-GlcNAcase, neither binds covalently to GH84 enzymes <cite>DJV2005 DvA2008 GJD2009</cite>, nor is a particularly potent inhibitor of human ''O''-GlcNAcase <cite>DJV2005 Kudlow2001 Sato1999</cite>.

== Catalytic Residues ==
Studies of two mutants of human ''O''-GlcNAcase established that adjacent aspartate residues, Asp174 and Asp175, act as critical components of the catalytic machinery of this enzyme <cite>DJV2006</cite>.

The mutant Asp175Ala displayed marked reductions in activity (''V'' and (''V/K'')) towards aryl ''N''-acetylglucosaminides possessing poor leaving groups with smaller reductions being observed for both ''O''-aryl and ''S''-aryl ''N''-acetylglucosaminides substrates possessing better leaving groups. Exogenous azide was found to partially rescue the activity of human ''O''-GlcNAcase towards 3,4-dinitrophenylglucosaminide. These results clearly identified Asp175 as the [[general acid]] catalyst.

The mutant Asp174Ala showed significantly decreased activity towards ''O''-aryl ''N''-acetylglucosaminides possessing either good or poor leaving groups and it was argued that this is consistent with its role as a residue responsible for the orientation and polarization of the ''N''-acyl nucleophile.

== Three-dimensional structures ==
The reported crystallization of ''Clostridium perfringens'' NagJ (''Cp''OGA) <cite>ABB2005</cite> was followed by solved structures for that enzyme <cite>DvA2006</cite> and ''Bacteroides thetaiotaomicron'' ''β''-glucosaminidase (''Bt''OGA) <cite>DvA2006</cite>. In common with the chitinases of family [[GH18]] and the ''exo''-acting ''β''-hexosaminidases of [[GH20]] the catalytic domain is a (''βα'')<sub>8</sub>-barrel structure. The structure of human ''O''-GlcNAcase has not been solved but both bacterial homologues are good models of both the active site and catalytic domain of human ''O''-GlcNAcase. More recently the structure of the GH84 ''β''-hexosaminidase from ''Oceanicola granulosus'' has been solved and shown to possess good sequence identity with the catalytic domain of the human enzyme <cite>DvA2010</cite>. Furthermore, the ''C''-terminal domain of this protein also displays notable sequence identity with the spacer domain, which separates the domains possessing ''O''-GlcNAcase and histone acetyltransferase activities) of the human enzyme.

[[Image:GH84conf.jpg|thumb|450px|'''Defining the conformational itinerary of a GH84 enzyme.''' Azepane (i) binds with a boat-like conformation to ''Bacteroides thetaiotaomicron'' ''β''-hexosaminidase (''Bt''OG). This binding mode is confirmed by the structure of a bound substrate (ii). Thiazoline (iii) binds to wild-type ''Bt''OG, 5-fluoro-oxazoline (iv) binds to the Asp243Asn mutant of ''Bt''OG, and oxazoline (v) binds to the Asp242Asn mutant of ''Bt''OG in the <sup>4</sup>C<sub>1</sub> conformation.]]

A series of crystallographic studies on ''Bacteroides thetaiotaomicron'' ''β''-hexosaminidase have used a variety of small molecules to define the conformational itinerary for this family of enzymes. Substrate distortion from the stable <sup>4</sup>C<sub>1</sub> conformation found in solution to a bound <sup>1,4</sup>B / <sup>1</sup>S<sub>3</sub> conformation was supported by the crystal structure of the wild-type enzyme in complex with 6-acetamido-6-deoxy-castanospermine <cite>Mac2010</cite> and the 7-membered ring-containing azepane <cite>Ble2009</cite>. This distortion was confirmed by the structure the wild-type enzyme in complex with the substrate 3,4-difluorophenyl 2-deoxy-2-difluoroacetamido-''β''-D-glucopyranoside <cite>GJD2010</cite>. Early studies of the wild-type ''Bt''OGA-bound thiazoline show that this intermediate is found in a <sup>4</sup>C<sub>1</sub>conformation <cite>DJV2005</cite>; subsequent studies have shown that oxazoline intermediates are bound in this conformation to ''Bt''OGA active site mutants <cite>GJD2010</cite>.

== Family Firsts ==
;First sterochemistry determination: <sup>1</sup>H-NMR studies of human ''O''-GlcNAcase established that it hydrolyzes the product with [[retaining|retention]] of anomeric stereochemistry to give the ''β''-configured hemiacetal product, which then anomerises in solution <cite>DJV2009</cite>.
;First [[catalytic nucleophile]] identification: This family of enzymes uses a mechanism of neighbouring group participation, in the the substrate ''N''-acetyl group acts as a nucleophile. This was first established through the use of free energy relationships studies <cite>DJV2005</cite>.
;First [[general acid/base]] residue identification: Studies of human ''O''-GlcNAcase mutant Asp175Ala identified reactivity patterns (free energy relationships, pH-activity profiles) consistent with the action of Asp175 as the catalytic [[general acid/base]] <cite>DJV2006</cite>.
;First 3-D structure: The structures of ''Bacteroides thetaiotaomicron'' ''O''-GlcNAcase <cite>GJD2006</cite> and ''Clostridium perfringens'' NagJ <cite>DvA2006</cite>.

== References ==
<biblio>
#Gao01 pmid=11148210
#Guthrie89 Guthrie RD, Jencks WP. ''IUPAC Recommendations for the Representation of Reaction Mechanisms'' Acc. Chem. Res. 1989; 22(10): 343-349.
#Heckel98 pmid=9811929
#Dong94 pmid=8034696
#Black2006 pmid=16822234
#ABB2005 pmid=16511172
#Ble2009 pmid=19331390
#DJV2009Trunc pmid=19423084
#DJV2005 pmid=15795231
#DJV2005Thio pmid=16332065
#DJV2009 pmid=19715310
#DJV2010 pmid=20067256
#DJV2006 pmid=16533067
#GJD2006 pmid=16565725
#GJD2009 pmid=19217614
#GJD2010 pmid=20067256
#DvA2006 pmid=16541109
#DvA2010 pmid=20863279
#DvA2008 pmid=18721751
#Whitworth2007 pmid=17227027
#Stubbs06 pmid=16493467
#Dorf2006 pmid=17177381
#Dorf2010 pmid=21095575
#Bartlett1997 pmid=11851452
#Vasella2006 pmid=17057847
#Stick2007 pmid=17728868
#Kudlow2001 pmid=11336633
#Sato1999 pmid=9917327
#Mac2010 pmid=20851343
</biblio>

[[Category:Glycoside Hydrolase Families|GH084]]