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Glycoside Hydrolase Family 31

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Glycoside Hydrolase Family GH31
Clan GH-D
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH31.html

Substrate specificities

CAZy Family GH31 is one of the two major families, along with GH13, that contain α-glucosidases. These enzymes play important roles in primary metabolism (e.g. human sucrase/isomaltase, a target for diabetic drugs such as miglitol), in catabolism (e.g. human lysosomal α-glucosidase) and in glycoprotein processing (e.g. ER glucosidase II). In addition to α-glucosidases, GH31 also contains α-xylosidases, isomaltosyltransferases, maltase/glucoamylases and the mechanistically interesting, non-hydrolytic α-glucan lyases. These enzymes can be found in a wide range of organisms including archaea, bacteria, plants and animals. Interestingly the two mammalian digestive enzymes are both duplicated genes, each with dual specificities.

Kinetics and Mechanism

Catalytic Residues

Three-dimensional structures

Family Firsts

First sterochemistry determination
Cite some reference here, with a short explanation [1].
First catalytic nucleophile identification
First general acid/base residue identification
First 3-D structure

References

  1. Ernst HA, Lo Leggio L, Willemoës M, Leonard G, Blum P, and Larsen S. (2006). Structure of the Sulfolobus solfataricus alpha-glucosidase: implications for domain conservation and substrate recognition in GH31. J Mol Biol. 2006;358(4):1106-24. DOI:10.1016/j.jmb.2006.02.056 | PubMed ID:16580018 [1]