Glycoside Hydrolase Families - Revision history

Spencer Williams: updated list of NAD-dependent hydrolysis families

2023-12-17T21:23:34Z

updated list of NAD-dependent hydrolysis families

Harry Brumer at 19:24, 4 July 2023

2023-07-04T19:24:55Z

Harry Brumer: Undo revision 16418 by Mslwebmin (talk)

2021-12-14T01:30:53Z

Undo revision 16418 by Mslwebmin (talk)

Harry Brumer at 22:49, 13 December 2021

2021-12-13T22:49:46Z

Harry Brumer: Fixed DPL columns output with alternate syntax due to issue with latest version of MediaWiki

2021-12-13T18:26:05Z

Fixed DPL columns output with alternate syntax due to issue with latest version of MediaWiki

Harry Brumer: Fixed DPL columns output with alternate syntax due to issue with latest version of MediaWiki

2021-12-13T18:19:28Z

Fixed DPL columns output with alternate syntax due to issue with latest version of MediaWiki

Mslwebmin at 09:00, 11 December 2021

2021-12-11T09:00:31Z

Harry Brumer at 17:22, 1 June 2021

2021-06-01T17:22:53Z

Harry Brumer: /* Unassigned pages */

2020-06-02T17:51:14Z

Unassigned pages

Harry Brumer: Fixed broken link to Sorting the Diverse - new DOI link added

2020-04-19T01:11:35Z

Fixed broken link to Sorting the Diverse - new DOI link added

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 * [[Alpha-glucan lyases]] are found within family [[GH31]] and degrade &alpha;-(1-4)-linked glucans (''e.g.'' starch) and oligosaccharides via an elimination mechanism that yields an enol (unsaturated) product that tautomerises to its keto form, 1,5-anhydro fructose.
-* [[NAD-dependent hydrolysis|NAD-dependent glycoside hydrolases]] of families [[GH4]] and [[GH109]] use nicotinamide adenine dinucleotide as redox cofactor to activate the sugar ring for glycosidic bond cleavage by elimination.
+* [[NAD-dependent hydrolysis|NAD-dependent glycoside hydrolases]] of families [[GH4]], [[GH109]], [[GH177]], [[GH179]] and [[GH188]] use nicotinamide adenine dinucleotide as redox cofactor to activate the sugar ring for glycosidic bond cleavage by elimination.
 == Curator Approved ==

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 #Davies1995 pmid=8535779
 #Henrissat1997 pmid=9345621
-#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].
+#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 DOI:10.1042/BIO03004026].
 #VocadloDavies2008 pmid=18558099
 #YipWithers2006 pmid=16495121
 </biblio>

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 == Overview ==
-The term [[glycoside hydrolase|glycoside hydrolase (GH)]] (''alternatively, [[glycoside hydrolase|glycosidase]]'') formally refers to enzymes that catalyze the hydrolytic cleavage of the glycosidic bond to give the carbohydrate hemiacetal.  Detailed explanations of the distinct catalytic mechanisms employed by these enzymes can be found on the [[glycoside hydrolase]] lexicon page.  Since the seminal [[sequence-based classification]] of GHs into families, it has subsequently been observed that some of these families also group non-hydrolytic enzymes and proteins, due to sequence and structural similarity <ref>Henrissat1989 Henrissat1991 Henrissat1993 Henrissat1996 Henrissat1997 DaviesSinnott2008 Davies1995 VocadloDavies2008 YipWithers2006</ref>.  In many cases, these alternative activities bear some degree of mechanistic similarity (''e.g.'', conserved catalytic residues or enzyme intermediates) to the eponymous enzymes:
+The term [[glycoside hydrolase|glycoside hydrolase (GH)]] (''alternatively, [[glycoside hydrolase|glycosidase]]'') formally refers to enzymes that catalyze the hydrolytic cleavage of the glycosidic bond to give the carbohydrate hemiacetal.  Detailed explanations of the distinct catalytic mechanisms employed by these enzymes can be found on the [[glycoside hydrolase]] lexicon page.  Since the seminal [[sequence-based classification]] of GHs into families, it has subsequently been observed that some of these families also group non-hydrolytic enzymes and proteins, due to sequence and structural similarity <cite>Henrissat1989 Henrissat1991 Henrissat1993 Henrissat1996 Henrissat1997 DaviesSinnott2008 Davies1995 VocadloDavies2008 YipWithers2006</cite>.  In many cases, these alternative activities bear some degree of mechanistic similarity (''e.g.'', conserved catalytic residues or enzyme intermediates) to the eponymous enzymes:
 * [[Transglycosylases]] are mechanistically related to [[retaining]] [[glycoside hydrolases]], with the exception that a sugar (or another nucleophile), rather than water, acts as the acceptor substrate to yield glycosidic bond exchange.

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 |allowcachedresults=no
 }}
 </div>
 == Unassigned pages ==
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 |allowcachedresults=no
 }}
 </div>
 == Deleted families ==
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 |allowcachedresults=no
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 </div>

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 |category=Glycoside Hydrolase Families
 |category=Under construction
 |resultsheader=\nThere are currently %PAGES% Glycoside Hydrolase Family pages [[:Category:Under construction|under construction]] in ''CAZypedia''.\n
 |noresultsheader=\nThere are currently no pages in this category.\n
 |ordermethod=sortkey
 |order=ascending
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 }}
 == Unassigned pages ==
 <blockquote class="toccolours" style="float:none; padding: 10px 15px 10px 15px; display:table;">
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 |category=Glycoside Hydrolase Families
 |category=Unassigned pages
 |resultsheader=\nThere are currently %PAGES% Glycoside Hydrolase Family pages in ''CAZypedia'' that have not been assigned to a [[Responsible Curator]].\n
 |noresultsheader=\nThere are currently no pages in this category.\n
 |ordermethod=sortkey
 |order=ascending
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 }}
 == Deleted families ==
 <blockquote class="toccolours" style="float:none; padding: 10px 15px 10px 15px; display:table;">
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 |category=Glycoside Hydrolase Families
 |category=Deleted families
 |resultsheader=\nThere are currently %PAGES% pages in ''CAZypedia'' that describe Glycoside Hydrolase families deleted from the CAZy DB.\n
 |noresultsheader=\nThere are currently no pages in this category.\n
 |ordermethod=sortkey
 |order=ascending
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 |allowcachedresults=no
 }}
 == References ==

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 == Overview ==
-The term [[glycoside hydrolase|glycoside hydrolase (GH)]] (''alternatively, [[glycoside hydrolase|glycosidase]]'') formally refers to enzymes that catalyze the hydrolytic cleavage of the glycosidic bond to give the carbohydrate hemiacetal.  Detailed explanations of the distinct catalytic mechanisms employed by these enzymes can be found on the [[glycoside hydrolase]] lexicon page.  Since the seminal [[sequence-based classification]] of GHs into families, it has subsequently been observed that some of these families also group non-hydrolytic enzymes and proteins, due to sequence and structural similarity <cite>Henrissat1991 Henrissat1993 Henrissat1996 Henrissat1997 DaviesSinnott2008 Davies1995 VocadloDavies2008 YipWithers2006</cite>.  In many cases, these alternative activities bear some degree of mechanistic similarity (''e.g.'', conserved catalytic residues or enzyme intermediates) to the eponymous enzymes:
+The term [[glycoside hydrolase|glycoside hydrolase (GH)]] (''alternatively, [[glycoside hydrolase|glycosidase]]'') formally refers to enzymes that catalyze the hydrolytic cleavage of the glycosidic bond to give the carbohydrate hemiacetal.  Detailed explanations of the distinct catalytic mechanisms employed by these enzymes can be found on the [[glycoside hydrolase]] lexicon page.  Since the seminal [[sequence-based classification]] of GHs into families, it has subsequently been observed that some of these families also group non-hydrolytic enzymes and proteins, due to sequence and structural similarity <cite>Henrissat1989 Henrissat1991 Henrissat1993 Henrissat1996 Henrissat1997 DaviesSinnott2008 Davies1995 VocadloDavies2008 YipWithers2006</cite>.  In many cases, these alternative activities bear some degree of mechanistic similarity (''e.g.'', conserved catalytic residues or enzyme intermediates) to the eponymous enzymes:
 * [[Transglycosylases]] are mechanistically related to [[retaining]] [[glycoside hydrolases]], with the exception that a sugar (or another nucleophile), rather than water, acts as the acceptor substrate to yield glycosidic bond exchange.
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 == References ==
 <biblio>
 #Henrissat1991 pmid=1747104
 #Henrissat1993 pmid=8352747
 #Henrissat1996 pmid=8687420

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 == Unassigned pages ==
 <blockquote class="toccolours" style="float:none; padding: 10px 15px 10px 15px; display:table;">
-[[File:Blank user-200px.png|left|40px]]The following [[:Category:Unassigned pages|Unassigned pages]] are currently lacking a [[Responsible Curator]] and one or more [[Author]]s. If you are an expert on any of these families and would like to help us improve ''CAZypedia'' by getting involved with the production and maintenance of the corresponding page(s), please contact a member of the [[Board of Curators]].
+[[File:Blank user-200px.png|left|40px]]The following [[:Category:Unassigned pages|Unassigned pages]] are currently lacking a [[Responsible Curator]] and one or more [[Author]]s. If you are an expert on any of these families and would like to help us improve ''CAZypedia'' by getting involved with the production and maintenance of the corresponding page(s), please contact a member of the [[Board of Curators]]. ''Undergraduate students, (post)graduate students, post-doctoral researchers, research associates, and professors are all welcomed to contribute!''
 </blockquote>
 {{#dpl: