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Literature summary for 5.4.99.1 extracted from

  • Xia, L.; Ballou, D.P.; Marsh, E.N.
    Role of arg100 in the active site of adenosylcobalamin-dependent glutamate mutase (2004), Biochemistry, 43, 3238-3245.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R100K cob(II)alamin accumulates to a concentration similar to that of the wild-type enzyme, homolysis of the coenzyme is slower by an order of magnitude, compared to wild-type enzyme, glutamate binding is significantly weakened. Mutant does not exhibit the very large deuterium isotope effects that are observed for homolysis of the coenzyme when the wild-type enzyme is reacted with deuterated substrates. Km-value for glutamate is reduced 121fold compared to wild-type enzyme, KM-value for glutamate is increased 17fold compared to wild-type enzyme Clostridium cochlearium
R100M no cob(II)alamin detected in UV-visible spectrum. Km-value for glutamate is reduced 276fold compared to wild-type enzyme, KM-value for glutamate is increased 13fold compared to wild-type enzyme Clostridium cochlearium
R100Y no cob(II)alamin detected in UV-visible spectrum. Km-value for glutamate is reduced 322fold compared to wild-type enzyme, KM-value for glutamate is increased 17fold compared to wild-type enzyme Clostridium cochlearium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.58
-
L-glutamate 25°C, wild-type enzyme Clostridium cochlearium
7.6
-
L-glutamate 25°C, mutant enzyme R100Y Clostridium cochlearium
10
-
L-glutamate 25°C, mutant enzyme R100K Clostridium cochlearium
13
-
L-glutamate 25°C, mutant enzyme R100M 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
0.0181
-
L-glutamate 25°C, mutant enzyme R100Y Clostridium cochlearium
0.0211
-
L-glutamate 25°C, mutant enzyme R100M Clostridium cochlearium
0.048
-
L-glutamate 25°C, mutant enzyme R100K Clostridium cochlearium
5.8
-
L-glutamate 25°C, wild-type enzyme Clostridium cochlearium

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin Km-value for wild-type enzyme is 0.005 mM. No cob(II)alamin detected in UV-visible spectrum of mutant enzymes R100M and R100Y. In mutant enzyme R100K cob(II)alamin accumulates to a concentration similar to that of the wild-type enzyme, homolysis of the coenzyme is slower by an order of magnitude, compared to wild-type enzyme. Mutant does not exhibit the very large deuterium isotope effects that are observed for homolysis of the coenzyme when the wild-type enzyme is reacted with deuterated substrates Clostridium cochlearium