PIRSF001031

Glucan 1,4-alpha-glucosidase with starch-binding domain

PIRSF entry
Member databasePIRSF
PIRSF typefamily
Short nameGlu-a-glcsd_SBD

Description

Glucan 1,4-alpha-glucosidase (glucoamylase; ) catalyses the release of glucose from the non-reducing ends of starch and related polysaccharides. Smaller molecular forms of the enzyme, G2, arise by proteolytic cleavage(s) of the carboxyl end of the large form, G1. Only G1 adsorbs and digests raw starch, but both forms are equally active towards soluble poly- and oligosaccharides
[1]
. The majority of these enzymes are multidomain proteins consisting of a catalytic domain connected to a starch-binding domain (SBD) by an O-glycosylated linker region. Glu179 and Glu400 of the Aspergillus niger sequence is involved in the general acid catalysis of the enzyme. Conserved tryptophan residues are involved in interactions of the glucoamylases with substrates and inhibitors
[2]
.

References

1.Characterization of a glucoamylase G2 from Aspergillus niger. Svensson B, Larsen K, Gunnarsson A. Eur. J. Biochem. 154, 497-502, (1986). View articlePMID: 3081341

2.Structure, function and protein engineering of starch-degrading enzymes. Gottschalk TE, Fierobe HP, Mirgorodskaya E, Clarke AJ, Tull D, Sigurskjold BW, Christensen T, Payre N, Frandsen TP, Juge N, McGuire KA, Cottaz S, Roepstorff P, Driguez H, Williamson G, Svensson B. Biochem. Soc. Trans. 26, 198-204, (1998). View articlePMID: 9649747

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.