Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.3 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

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.3 glycoprotein
-
 Saccharomycopsis fibuligera

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.3 (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
a

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.2.1.3 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 40
-
 assay at Saccharomycopsis fibuligera

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 5.6
-
 assay at Saccharomycopsis fibuligera