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Literature summary for 3.2.1.3 extracted from

  • Sevcik, J.; Hostinova, E.; Solovicova, A.; Gasperik, J.; Dauter, Z.; Wilson, K.S.
    Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain (2006), FEBS J., 273, 2161-2171.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain AH22, secretion of recombinant enzymes Saccharomycopsis fibuligera

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant nonglycosylated enzyme, 10 mg/ml protein in 50 mM acetate, pH 5.4, with 15% PEG 8000, X-ray diffraction structure determination and analysis at 1.1-1.6 A resolution, modelling Saccharomycopsis fibuligera

Protein Variants

Protein Variants Comment Organism
H447A site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure Saccharomycopsis fibuligera
H447A/D450A site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure Saccharomycopsis fibuligera
R15A site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure Saccharomycopsis fibuligera
T462A site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure Saccharomycopsis fibuligera

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular enzyme secretion Saccharomycopsis fibuligera
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + H2O Saccharomycopsis fibuligera
-
starch + beta-D-glucose
-
?
starch + H2O Saccharomycopsis fibuligera HUT 7212
-
starch + beta-D-glucose
-
?
starch + H2O Saccharomycopsis fibuligera IFO 0111
-
starch + beta-D-glucose
-
?

Organism

Organism UniProt Comment Textmining
Saccharomycopsis fibuligera P08017 Glu1 precursor
-
Saccharomycopsis fibuligera Q8TFE5 Glu-1.1 precursor
-
Saccharomycopsis fibuligera HUT 7212 P08017 Glu1 precursor
-
Saccharomycopsis fibuligera IFO 0111 Q8TFE5 Glu-1.1 precursor
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Saccharomycopsis fibuligera

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae strain AH22 medium by gel filtration and ion exchange chromatography to homogeneity Saccharomycopsis fibuligera

Reaction

Reaction Comment Organism Reaction ID
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site Saccharomycopsis fibuligera

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + H2O
-
Saccharomycopsis fibuligera starch + beta-D-glucose
-
?
starch + H2O
-
Saccharomycopsis fibuligera HUT 7212 starch + beta-D-glucose
-
?
starch + H2O
-
Saccharomycopsis fibuligera IFO 0111 starch + beta-D-glucose
-
?

Subunits

Subunits Comment Organism
More the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding Saccharomycopsis fibuligera

Synonyms

Synonyms Comment Organism
alpha-1,4-D-glucan glucohydrolase
-
Saccharomycopsis fibuligera
Glu-1.1
-
Saccharomycopsis fibuligera
Glu-A
-
Saccharomycopsis fibuligera
Glu1
-
Saccharomycopsis fibuligera
Glucan 1,4-alpha-glucosidase
-
Saccharomycopsis fibuligera
glucoamylase
-
Saccharomycopsis fibuligera

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Saccharomycopsis fibuligera

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6
-
assay at Saccharomycopsis fibuligera