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Difference between revisions of "Glycoside Hydrolase Family 91"

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* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
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=== GH91 is a deleted family ===
 
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Entries in GH91 were transferred to [[Polysaccharide Lyase Family 19]] due to recommendations of the NC-IUBMB; polysaccharide cleavage occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis.
 
  
 
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{| {{Prettytable}}  
 
{| {{Prettytable}}  
 
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|-
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB links'''
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|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH91'''
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|-
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|'''Clan'''   
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|-
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|'''Mechanism'''
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|'''Active site residues'''
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| colspan="2" |http://www.cazy.org/fam/GH91.html
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
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| colspan="2" |http://www.cazy.org/fam/PL19.html
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| colspan="2" |{{CAZyDBlink}}GH91.html
 
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{{CuratorApproved}}
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== History of reclassification ==
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Entries in [[Glycoside Hydrolase Family 91]] were reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction.  Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]).
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The family was ''placed back'' to [[Glycoside Hydrolase Family 91]] on 20 April 2010 due to direct analogy with the lytic transglycosidases of [[GH23]], [[GH102]], [[GH103]], and [[GH104]] and in particular the observation of a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) in this family <cite>Sakurai1997 Saito2003</cite>.
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== Substrate specificities ==
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Content is to be added here.
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== Kinetics and Mechanism ==
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Content is to be added here.
 +
 
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== Catalytic Residues ==
 +
Content is to be added here.
 +
 
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== Three-dimensional structures ==
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Content is to be added here.
 +
 
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== Family Firsts ==
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;First stereochemistry determination: .
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;First catalytic nucleophile identification: .
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;First general acid/base residue identification: .
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;First 3-D structure: .
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== References ==
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<biblio>
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#Sakurai1997 H. Sakurai, A. Yokota, Y. Sumita, Y. Mori, H. Matsui and F. Tomita, Metabolism of DFA III by Arthrobacter sp. H65-7: purification and properties of a DFA III hydrolysis enzyme (DFA IIIase). Biosci. Biotechnol. Biochem. 61 (1997), pp. 989–993. [http://dx.doi.org/10.1271/bbb.61.989 DOI: 10.1271/bbb.61.989]
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#Saito2003 pmid=16233453
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</biblio>
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[[Category:Glycoside Hydrolase Families|GH091]]
 
[[Category:Glycoside Hydrolase Families|GH091]]
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[[Category:Deleted families]]
 

Latest revision as of 07:01, 23 October 2012

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CAZypedia needs your help: This page is currently lacking a Responsible Curator and one or more Authors. If you are an expert on this family and would like to help us improve CAZypedia by getting involved with writing and maintaining this page, please contact the Primary Curator.

Undergraduate students, (post)graduate students, post-doctoral researchers, research associates, and professors are all welcomed to contribute!

  • If you are interested in contributing to CAZypedia, please see the 10th anniversary publication [1] and this page for an overview of the content and mission of our community-driven resource. Future authors of CAZypedia can include the CAZypedia article [1] and cite individual pages in their curricula vitae to reflect their contribution.
  • Until this CAZypedia page is completed, current information on the composition of this family is available via the corresponding page of the CAZy database [2]:
    https://www.cazy.org/GH91.html

References

  1. CAZypedia Consortium (2018). Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes. Glycobiology. 2018;28(1):3-8. DOI:10.1093/glycob/cwx089 | PubMed ID:29040563 [CAZypedia2018]
  2. Drula E, Garron ML, Dogan S, Lombard V, Henrissat B, and Terrapon N. (2022). The carbohydrate-active enzyme database: functions and literature. Nucleic Acids Res. 2022;50(D1):D571-D577. DOI:10.1093/nar/gkab1045 | PubMed ID:34850161 [CAZyDB2022]

All Medline abstracts: PubMed

Glycoside Hydrolase Family GH91
Clan
Mechanism
Active site residues
CAZy DB link
https://www.cazy.org/GH91.html

History of reclassification

Entries in Glycoside Hydrolase Family 91 were reclassified to Polysaccharide Lyase Family 19 on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction. Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC 4.2.2.17 and EC 4.2.2.18).

The family was placed back to Glycoside Hydrolase Family 91 on 20 April 2010 due to direct analogy with the lytic transglycosidases of GH23, GH102, GH103, and GH104 and in particular the observation of a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) in this family [3, 4].

Substrate specificities

Content is to be added here.

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
.
First catalytic nucleophile identification
.
First general acid/base residue identification
.
First 3-D structure
.

References

  1. H. Sakurai, A. Yokota, Y. Sumita, Y. Mori, H. Matsui and F. Tomita, Metabolism of DFA III by Arthrobacter sp. H65-7: purification and properties of a DFA III hydrolysis enzyme (DFA IIIase). Biosci. Biotechnol. Biochem. 61 (1997), pp. 989–993. DOI: 10.1271/bbb.61.989

    [Sakurai1997]
  2. Saito K, Sumita Y, Nagasaka Y, Tomita F, and Yokota A. (2003). Molecular cloning of the gene encoding the di-D-Fructofuranose 1,2':2,3' dianhydride hydrolysis enzyme (DFA IIIase) from Arthrobacter sp. H65-7. J Biosci Bioeng. 2003;95(5):538-40. DOI:10.1016/s1389-1723(03)80058-0 | PubMed ID:16233453 [Saito2003]
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