EzCatDB: S00048
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00048
CATH domainDomain 11.50.10.10 : GlycosyltransferaseCatalytic domain
E.C.3.2.1.3

CATH domainRelated DB codes (homologues)
1.50.10.10 : GlycosyltransferaseS00531,S00845,D00167,D00500,M00192,T00245,T00246

Enzyme Name
UniProtKBKEGG

P08017
Protein nameGlucoamylase GLU1glucan 1,4-alpha-glucosidase
glucoamylase
amyloglucosidase
gamma-amylase
lysosomal alpha-glucosidase
acid maltase
exo-1,4-alpha-glucosidase
glucose amylase
gamma-1,4-glucan glucohydrolase
acid maltase
1,4-alpha-D-glucan glucohydrolase
SynonymsEC 3.2.1.3
Glucan 1,4-alpha-glucosidase
1,4-alpha-D-glucan glucohydrolase
PfamPF00723 (Glyco_hydro_15)
[Graphical view]
CAZyGH15 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP08017
Entry nameAMYG_SACFI
ActivityHydrolysis of terminal (1->4)-linked alpha-D- glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00718C00001C00718C00221
CompoundAmyloseH2OAmylosebeta-D-Glucose
TypepolysaccharideH2Opolysaccharidecarbohydrate
ChEBI
15377

15903
PubChem
962
22247451

64689
            
1ayxAUnbound UnboundAnalogue:TRS

Active-site residues
pdbCatalytic residues
         
1ayxATYR 63;GLU 210;GLU 456

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.862-864
[7]Fig.5, p.279-280

references
[1]
PubMed ID7937705
JournalProtein Eng
Year1994
Volume7
Pages749-60
AuthorsCoutinho PM, Reilly PJ
TitleStructural similarities in glucoamylase by hydrophobic cluster analysis.
[2]
PubMed ID8177888
JournalProtein Eng
Year1994
Volume7
Pages393-400
AuthorsCoutinho PM, Reilly PJ
TitleStructure-function relationships in the catalytic and starch binding domains of glucoamylase.
[3]
PubMed ID8713124
JournalBiochem Biophys Res Commun
Year1996
Volume224
Pages790-5
AuthorsSolovicova A, Gasperik J, Hostinova E
TitleHigh-yield production of Saccharomycopsis fibuligera glucoamylase in Escherichia coli, refolding, and comparison of the nonglycosylated and glycosylated enzyme forms.
[4]
PubMed ID9365988
JournalProteins
Year1997
Volume29
Pages334-47
AuthorsCoutinho PM, Reilly PJ
TitleGlucoamylase structural, functional, and evolutionary relationships.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID98437615
PubMed ID9757101
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages854-66
AuthorsSevcik J, Solovicova A, Hostinova E, Gasperik J, Wilson KS, Dauter Z
TitleStructure of glucoamylase from Saccharomycopsis fibuligera at 1.7 A resolution.
Related PDB1ayx
Related UniProtKBP08017
[6]
PubMed ID10491121
JournalEur J Biochem
Year1999
Volume264
Pages756-64
AuthorsSolovicova A, Christensen T, Hostinova E, Gasperik J, Sevcik J, Svensson B
TitleStructure-function relationships in glucoamylases encoded by variant Saccharomycopsis fibuligera genes.
[7]
PubMed ID11150611
JournalBiochim Biophys Acta
Year2000
Volume1543
Pages275-93
AuthorsSauer J, Sigurskjold BW, Christensen U, Frandsen TP, Mirgorodskaya E, Harrison M, Roepstorff P, Svensson B
TitleGlucoamylase: structure/function relationships, and protein engineering.
[8]
PubMed ID12623067
JournalArch Biochem Biophys
Year2003
Volume411
Pages189-95
AuthorsHostinova E, Solovicova A, Dvorsky R, Gasperik J
TitleMolecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain.
[9]
PubMed ID15963591
JournalJ Biotechnol
Year2005
Volume118
Pages167-76
AuthorsLatorre-Garcia L, Adam AC, Manzanares P, Polaina J
TitleImproving the amylolytic activity of Saccharomyces cerevisiae glucoamylase by the addition of a starch binding domain.

comments
This enzyme belongs to the glycosidase family-15, with an inverting mechanism.
According to the literature [5] & [7], the catalytic mechanism seems to be similar to that of beta-amylase (D00166 in EzCatDB). Glu210 and Glu456 act as a general acid and a general base, respectively.

createdupdated
2004-07-092009-03-16


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.