CAZypedia celebrates the life of Senior Curator Emeritus Harry Gilbert, a true giant in the field, who passed away in September 2025.


CAZypedia needs your help!

We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article. Totally new to the CAZy classification? Read this first.

Difference between revisions of "Glycoside Hydrolase Family 77"

From CAZypedia
Jump to navigation Jump to search
Line 29: Line 29:
  
 
== Substrate specificities ==
 
== Substrate specificities ==
[[Glycoside hydrolase]] family 77 is the member of the α-amylase clan [[GH-H]] <cite>Cantarel2009</cite>, together with [[GH13]] and [[GH70]] <cite>MacGregor2001</cite>. The family contains only one enzyme specificity - the amylomaltase (EC [{{EClink}}2.4.1.25 2.4.1.25]), that is known as disproportionating enzyme (D-enzyme) in plants <cite>Takaha1993</cite> or 4-α-glucanotransferase in bacteria <cite>Terada1999</cite> and archaeons <cite>Kaper2005</cite>.
+
[[Glycoside hydrolase]] family 77 is the member of the α-amylase clan [[GH-H]] <cite>Cantarel2009</cite>, together with [[GH13]] and [[GH70]] <cite>MacGregor2001</cite>. The family contains only one enzyme specificity - the amylomaltase (EC [{{EClink}}2.4.1.25 2.4.1.25]), that is known as disproportionating enzyme (D-enzyme) in plants <cite>Takaha1993</cite> or 4-α-glucanotransferase in bacteria <cite>Terada1999</cite> and archaeons <cite>Kaper2005</cite>. As of April 2010, it has more than 700 members <cite>Cantarel2009</cite> with more than 650 from Bacteria, ~10 from Archaea and a few tens from Eukarya (plants and green algae).
  
  

Revision as of 00:40, 16 April 2010

Under construction icon-blue-48px.png

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 GH77
Clan GH-H
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH77.html


Substrate specificities

Glycoside hydrolase family 77 is the member of the α-amylase clan GH-H [1], together with GH13 and GH70 [2]. The family contains only one enzyme specificity - the amylomaltase (EC 2.4.1.25), that is known as disproportionating enzyme (D-enzyme) in plants [3] or 4-α-glucanotransferase in bacteria [4] and archaeons [5]. As of April 2010, it has more than 700 members [1] with more than 650 from Bacteria, ~10 from Archaea and a few tens from Eukarya (plants and green algae).


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
Cite some reference here, with a short (1-2 sentence) explanation.
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation.
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation.
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation.

References

Error fetching PMID 11257505:
Error fetching PMID 7678257:
Error fetching PMID 10049841:
Error fetching PMID 16151092:
  1. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 | PubMed ID:18838391 [Cantarel2009]
  2. Error fetching PMID 11257505: [MacGregor2001]
  3. Error fetching PMID 7678257: [Takaha1993]
  4. Error fetching PMID 10049841: [Terada1999]
  5. Error fetching PMID 16151092: [Kaper2005]

All Medline abstracts: PubMed