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Literature summary for 3.2.1.3 extracted from

  • Fang, T.Y.; Ford, C.
    Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum (1998), Protein Eng., 11, 383-388.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S411A 54-74% of the catalytic efficiency of the wild type enzyme. Increased pH-optimum by 0.8 units for both maltose and maltoheptaose hydrolysis while maintaining a high level of activity and catalytic efficiency. In hydrolysis of 28% DE 10 maltodextrin, the mutant enzyme has a pH optimum of 7 compared with 5.6 for wild-type enzyme, and has higher initial rates of glucose production than wild-type enzyme at all pH values tested above pH 6.6 Aspergillus awamori
S411C 54-74% of the catalytic efficiency of the wild type enzyme Aspergillus awamori
S411D 6-12% of the catalytic efficiency of the wild type enzyme Aspergillus awamori
S411G catalytic efficiency like that of wild type enzyme for isomaltose, maltose and maltoheptaose hydrolysis at pH 4.4 Aspergillus awamori
S411H 6-12% of the catalytic efficiency of the wild type enzyme Aspergillus awamori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
maltoheptaose mutant enzyme S411C Aspergillus awamori
0.083
-
maltoheptaose wild-type enzyme Aspergillus awamori
0.104
-
maltoheptaose mutant enzyme S411A Aspergillus awamori
0.132
-
maltoheptaose mutant enzyme S411G Aspergillus awamori
0.148
-
maltoheptaose mutant enzyme S411D Aspergillus awamori
0.53
-
maltose mutant enzyme S411C Aspergillus awamori
1.01
-
maltose wild-type enzyme Aspergillus awamori
1.26
-
maltose mutant enzyme S411A Aspergillus awamori
1.59
-
maltose mutant enzyme S411G Aspergillus awamori
3.58
-
maltose mutant enzyme S411D Aspergillus awamori
12.3
-
isomaltose mutant enzyme S411C Aspergillus awamori
23.5
-
isomaltose wild-type enzyme Aspergillus awamori
26.2
-
isomaltose wild-type enzyme Aspergillus awamori
27.9
-
isomaltose mutant enzyme S411A Aspergillus awamori

Organism

Organism UniProt Comment Textmining
Aspergillus awamori
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isomaltose + H2O
-
Aspergillus awamori glucose
-
?
maltoheptaose + H2O
-
Aspergillus awamori ?
-
?
maltose + H2O
-
Aspergillus awamori 2 glucose
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.22
-
isomaltose mutant enzyme S411C Aspergillus awamori
0.63
-
isomaltose mutant enzyme S411A Aspergillus awamori
0.72
-
isomaltose wild-type enzyme Aspergillus awamori
0.93
-
isomaltose mutant enzyme S411G Aspergillus awamori
4.36
-
maltose mutant enzyme S411D Aspergillus awamori
7.78
-
maltose mutant enzyme S411C Aspergillus awamori
14.5
-
maltose mutant enzyme S411G Aspergillus awamori
15.8
-
maltoheptaose mutant enzyme S411D Aspergillus awamori
18.9
-
maltose mutant enzyme S411A Aspergillus awamori
20.4
-
maltose wild-type enzyme Aspergillus awamori
33
-
maltoheptaose mutant enzyme S411C Aspergillus awamori
59.4
-
maltoheptaose mutant enzyme S411A Aspergillus awamori
72.3
-
maltoheptaose wild-type enzyme Aspergillus awamori
84
-
maltoheptaose mutant enzyme S411G Aspergillus awamori

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
hydrolysis of maltose, wild-type enzyme Aspergillus awamori
4.1
-
hydrolysis of maltose, mutant enzyme S411H Aspergillus awamori
4.2
-
hydrolysis of maltose, mutant enzyme S411G Aspergillus awamori
4.4
-
hydrolysis of maltose, mutant enzyme S411D Aspergillus awamori
4.7
-
hydrolysis of maltoheptaose, wild-type enzyme Aspergillus awamori
4.8
-
hydrolysis of maltose, mutant enzyme S411A and S411C Aspergillus awamori
5
-
hydrolysis of maltoheptaose, mutant enzyme S411G Aspergillus awamori
5.5
-
hydrolysis of maltoheptaose, mutant enzyme S411A Aspergillus awamori