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Difference between revisions of "Glycoside Hydrolase Family 81"

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== Substrate specificities ==
 
== Substrate specificities ==
 
GH81 family are endo-&beta;(1,3)-glucanases ([{{EClink}}3.2.1.39 EC 3.2.1.39]) with diverse physiological roles, such as plant biomass degradation, cell cycling, and enzymatic pathogen defense. They are mostly found in bacteria and fungi, particularly abundant in ''Saccharomyces'', and ''Streptomyces'' species. Activity has been demonstrated on laminarin <cite>Fontaine1997, McGrath2006, Martin-Cuadrado2008, Zhou2013, Pluvinage2017, Kumar2018</cite>, curdlan <cite>Fontaine1997, Martin-Cuadrado2008, Pluvinage2017, Kumar2018</cite>, and pachyman  <cite>McGrath2006, Pluvinage2017</cite>.
 
GH81 family are endo-&beta;(1,3)-glucanases ([{{EClink}}3.2.1.39 EC 3.2.1.39]) with diverse physiological roles, such as plant biomass degradation, cell cycling, and enzymatic pathogen defense. They are mostly found in bacteria and fungi, particularly abundant in ''Saccharomyces'', and ''Streptomyces'' species. Activity has been demonstrated on laminarin <cite>Fontaine1997, McGrath2006, Martin-Cuadrado2008, Zhou2013, Pluvinage2017, Kumar2018</cite>, curdlan <cite>Fontaine1997, Martin-Cuadrado2008, Pluvinage2017, Kumar2018</cite>, and pachyman  <cite>McGrath2006, Pluvinage2017</cite>.
 +
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
Content is to be added here.
+
GH81 enzymes follow an [[inverting]] mechanism, first shown by <sup>1</sup>H-NMR during the hydrolysis of laminarioligosaccharides <cite>Fliegmann2005</cite>, and laminarin <cite>McGrath2006</cite>, thus operating by a [[Glycoside_hydrolases#Inverting_glycoside_hydrolases|single-displacement mechanism]].
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
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#Pluvinage2017 pmid=28781080
 
#Pluvinage2017 pmid=28781080
 
#Kumar2018 pmid=29870811
 
#Kumar2018 pmid=29870811
 +
#Fliegmann2005 pmid=16297387
 +
 
</biblio>
 
</biblio>
  
 
[[Category:Glycoside Hydrolase Families|GH081]]
 
[[Category:Glycoside Hydrolase Families|GH081]]

Revision as of 12:56, 21 July 2020

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH81
Clan none
Mechanism inverting
Active site residues not known
CAZy DB link
https://www.cazy.org/GH81.html


Substrate specificities

GH81 family are endo-β(1,3)-glucanases (EC 3.2.1.39) with diverse physiological roles, such as plant biomass degradation, cell cycling, and enzymatic pathogen defense. They are mostly found in bacteria and fungi, particularly abundant in Saccharomyces, and Streptomyces species. Activity has been demonstrated on laminarin [1, 2, 3, 4, 5, 6], curdlan [1, 3, 5, 6], and pachyman [2, 5].

Kinetics and Mechanism

GH81 enzymes follow an inverting mechanism, first shown by 1H-NMR during the hydrolysis of laminarioligosaccharides [7], and laminarin [2], thus operating by a single-displacement mechanism.

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

Error fetching PMID 9030754:
Error fetching PMID 17115704:
Error fetching PMID 17933563:
Error fetching PMID 24100321:
Error fetching PMID 28781080:
Error fetching PMID 29870811:
Error fetching PMID 16297387:
  1. Error fetching PMID 9030754: [Fontaine1997]
  2. Error fetching PMID 17115704: [McGrath2006]
  3. Error fetching PMID 17933563: [Martin-Cuadrado2008]
  4. Error fetching PMID 24100321: [Zhou2013]
  5. Error fetching PMID 28781080: [Pluvinage2017]
  6. Error fetching PMID 29870811: [Kumar2018]
  7. Error fetching PMID 16297387: [Fliegmann2005]

All Medline abstracts: PubMed