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Literature summary for 3.2.1.3 extracted from

  • Fierobe, H.P.
    Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering (1996), Biochemistry, 35, 8696-8704.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A246C the T50-value is enhanced by 4°C to 73°C. Compared to wild-type enzyme, the mutant is twice as active at 66°C but half as active at 45°C Aspergillus awamori
C320A barely improved thermostability or altered activity Aspergillus awamori
P307A/T310V/Y312M/N313G up to 15fold decreased turnover-number for alpha-1,4-linked substrates. Up to 9fold increase in Km-value for alpha-1,6-linked substrates Aspergillus awamori
V181T/N182Y/G183A 2fold increased Km-value for alpha-1,4-linked substrates: For alpha-1,6-linked substrates a 2fold increase in Km and a 3fold decrease in turnover-number Aspergillus awamori
V181T/N182Y/G183A/P307A/T310V/Y312M/A313G remarkably low Km-value for isomaltotriose through isomaltoheptaose and elevated turnover-number on isomaltose, resulting in an approximately 2fold improved catalytic effeciency Aspergillus awamori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-values for the wild type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G Aspergillus awamori

Organism

Organism UniProt Comment Textmining
Aspergillus awamori
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isomaltoheptaose + H2O
-
Aspergillus awamori ?
-
?
isomaltohexaose + H2O
-
Aspergillus awamori ?
-
?
isomaltopentaose + H2O
-
Aspergillus awamori ?
-
?
isomaltose + H2O
-
Aspergillus awamori glucose
-
?
isomaltotetraose + H2O
-
Aspergillus awamori ?
-
?
isomaltotriose + H2O
-
Aspergillus awamori ?
-
?
maltoheptaose + H2O
-
Aspergillus awamori ?
-
?
maltohexaose + H2O
-
Aspergillus awamori ?
-
?
maltopentaose + H2O
-
Aspergillus awamori ?
-
?
maltose + H2O
-
Aspergillus awamori 2 glucose
-
?
maltotetraose + H2O
-
Aspergillus awamori ?
-
?
maltotriose + H2O
-
Aspergillus awamori maltose + glucose
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover numbers for the wild-type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G Aspergillus awamori