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Literature summary for 5.4.99.1 extracted from

  • Madhavapeddi, P.; Marsh, E.N.
    The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase (2001), Chem. Biol., 8, 1143-1149.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E171A turnover number for glutamate is reduced 27.6fold, KM-value is increased 1.1fold, Km-value for adenosylcobalamin is reduced 1.23fold Clostridium cochlearium
E171D turnover number for glutamate is reduced 1.8fold, KM-value is reduced 1.54fold, Km-value for adenosylcobalamin is reduced 2.7fold Clostridium cochlearium
E171N turnover number for glutamate is reduced 232fold, KM-value is increased by 1.8fold, Km-value for adenosylcobalamin is reduced 1.4fold Clostridium cochlearium
E171Q turnover number for glutamate is reduced 53fold, KM-value is reduced 2.4fold, Km-value for adenosylcobalamin is reduced 2fold, mutant enzyme is independent of pH Clostridium cochlearium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.24
-
L-glutamate 23°C, mutant enzyme E171Q Clostridium cochlearium
0.38
-
L-glutamate 23°C, mutant enzyme E171D Clostridium cochlearium
0.58
-
L-glutamate 23°C, wild-type enzyme Clostridium cochlearium
0.65
-
L-glutamate 23°C, mutant enzyme E171A Clostridium cochlearium
1.07
-
L-glutamate 23°C, mutant enzyme E171N Clostridium cochlearium

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
Clostridium cochlearium L-threo-3-methylaspartate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.025
-
L-glutamate 23°C, mutant enzyme E171N Clostridium cochlearium
0.11
-
L-glutamate 23°C, mutant enzyme E171Q Clostridium cochlearium
0.21
-
L-glutamate 23°C, mutant enzyme E171A Clostridium cochlearium
3 6 L-glutamate 23°C, mutant enzyme E171D Clostridium cochlearium
3.19
-
L-glutamate 23°C, mutant enzyme E171D Clostridium cochlearium
5.8
-
L-glutamate 23°C, wild-type enzyme Clostridium cochlearium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Clostridium cochlearium

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.7 pH 6.5: about 50% of maximal activity, pH 8.7: about 80% of maximal activity Clostridium cochlearium

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin enzyme is dependent on, KM for wild-type enzyme is 0.0055 mM Clostridium cochlearium