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Difference between revisions of "Glycoside Hydrolase Family 145"

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* [[Author]]: [[User:Harry Brumer|Harry Brumer]]
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* [[Author]]: ^^^Alan Cartmell^^^
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* [[Responsible Curator]]: [[User:Bernard Henrissat|Bernard Henrissat]]
* [[Responsible Curator]]: ^^^Harry Gilbert^^^
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=== GH145 is a deleted family ===
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This family has been reclassified as [[Polysaccharide Lyase Family 42]]. Two members of the family from ''Bacteroides'' species were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure <cite>MunozMunoz2017</cite>.  Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to [[PL24]] and [[PL25]], was demonstrated in fungal <cite>Kondo2021</cite> and bacterial <cite>MunozMunoz2021</cite>  homologs.
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'''References'''
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<biblio>
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#MunozMunoz2017 pmid=28396425
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#MunozMunoz2021 pmid=34340552
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#Kondo2021 pmid=34303708
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</biblio>
 
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
<div style="float:right">
 
 
{| {{Prettytable}}  
 
{| {{Prettytable}}  
 
|-
 
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH145'''
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB links'''
 
|-
 
|-
|'''Clan'''   
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| colspan="2" |{{CAZyDBlink}}GH145.html
|GH-x
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|-
 
|-
|'''Mechanism'''
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| colspan="2" |{{CAZyDBlink}}PL42.html
|retaining/inverting
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|-
 
|'''Active site residues'''
 
|known/not known
 
|-
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
|-
 
| colspan="2" |{{CAZyDBlink}}GH145.html
 
 
|}
 
|}
</div>
 
 
<!-- This is the end of the table -->
 
<!-- This is the end of the table -->
 
 
== Substrate specificities ==
 
Content is to be added here.
 
 
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
 
== Kinetics and Mechanism ==
 
Content is to be added here.
 
 
== Catalytic Residues ==
 
Content is to be added here.
 
 
== Three-dimensional structures ==
 
Content is to be added here.
 
 
== Family Firsts ==
 
;First stereochemistry determination: Content is to be added here.
 
;First catalytic nucleophile identification: Content is to be added here.
 
;First general acid/base residue identification: Content is to be added here.
 
;First 3-D structure: Content is to be added here.
 
 
== References ==
 
<biblio>
 
#Cantarel2009 pmid=18838391
 
#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. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
 
</biblio>
 
  
 
[[Category:Glycoside Hydrolase Families|GH145]]
 
[[Category:Glycoside Hydrolase Families|GH145]]

Latest revision as of 14:15, 18 December 2021


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This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.

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This family has been deleted from the CAZy classification. A specific explanation may be found below.

GH145 is a deleted family

This family has been reclassified as Polysaccharide Lyase Family 42. Two members of the family from Bacteroides species were originally shown to have hydrolase activity catalyzed by a semi-conserved active site on the posterior side of the beta-propeller structure [1]. Subsequently, lyase activity on alpha-L-Rha-1,4-alpha-D-GlcA via a well-conserved active site on the anterior surface, with strong similarity to PL24 and PL25, was demonstrated in fungal [2] and bacterial [3] homologs.

References

  1. Munoz-Munoz J, Cartmell A, Terrapon N, Henrissat B, and Gilbert HJ. (2017). Unusual active site location and catalytic apparatus in a glycoside hydrolase family. Proc Natl Acad Sci U S A. 2017;114(19):4936-4941. DOI:10.1073/pnas.1701130114 | PubMed ID:28396425 [MunozMunoz2017]
  2. Kondo T, Kichijo M, Maruta A, Nakaya M, Takenaka S, Arakawa T, Fushinobu S, and Sakamoto T. (2021). Structural and functional analysis of gum arabic l-rhamnose-α-1,4-d-glucuronate lyase establishes a novel polysaccharide lyase family. J Biol Chem. 2021;297(3):101001. DOI:10.1016/j.jbc.2021.101001 | PubMed ID:34303708 [Kondo2021]
  3. Munoz-Munoz J, Ndeh D, Fernandez-Julia P, Walton G, Henrissat B, and Gilbert HJ. (2021). Sulfation of Arabinogalactan Proteins Confers Privileged Nutrient Status to Bacteroides plebeius. mBio. 2021;12(4):e0136821. DOI:10.1128/mBio.01368-21 | PubMed ID:34340552 [MunozMunoz2021]

All Medline abstracts: PubMed

CAZy DB links
http://www.cazy.org/GH145.html
http://www.cazy.org/PL42.html