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PROSITE documentation PDOC00646 [for PROSITE entry PS00820]

Glucoamylase active site region signature





Description

Glucoamylase (GA) (EC 3.2.1.3) is an enzyme that catalyzes the release of D-glucose from the non-reducing ends of starch and other oligo- or polysaccharides. Extensive studies of fungal GA have shown [1,E1] that three closely clustered acidic residues play a role in the catalytic mechanism of GA. The region that includes these residues is also conserved in a recently sequenced bacterial GA [2]. We used this region as a signature pattern.

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Note:

These proteins belong to family 15 in the classification of glycosyl hydrolases [3,E1].

Note:

A GA from Schwanniomyces occidentalis is not a member of this family but belongs to family 31 (see <PDOC00120>).

Last update:

July 1998 / Text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

GLUCOAMYLASE, PS00820; Glucoamylase active site region signature  (PATTERN)


References

1AuthorsSierks M.R. Ford C. Reilly P.J. Svensson B.
TitleCatalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.
SourceProtein Eng. 3:193-198(1990).
PubMed ID1970434

2AuthorsOhnishi H. Kitamura H. Minowa T. Sakai H. Ohta T.
TitleMolecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme.
SourceEur. J. Biochem. 207:413-418(1992).
PubMed ID1633799

3AuthorsHenrissat B.
TitleA classification of glycosyl hydrolases based on amino acid sequence similarities.
SourceBiochem. J. 280:309-316(1991).
PubMed ID1747104

E1Sourcehttp://www.cazy.org/fam/GH15.html



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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