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Literature summary for 5.1.1.3 extracted from

  • Glavas, S.; Tanner, M.E.
    Active site residues of glutamate racemase (2001), Biochemistry, 40, 6199-6204.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D10N 1015fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.9fold increase in Km-value for L-glutamate compared to wild-type enzyme. 1079fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 4.6fold increase in Km-value for D-glutamate compared to wild-type enzyme Limosilactobacillus fermentum
D36N 3.4fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 106fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 158fold increase in Km-value for D-glutamate compared to wild-type enzyme Limosilactobacillus fermentum
E152Q 1.8fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.1fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 13.5fold increase in Km-value for D-glutamate compared to wild-type enzyme Limosilactobacillus fermentum
H186N 1533fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.4fold increase in Km-value for L-glutamate compared to wild-type enzyme. 731fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 17.3fold increase in Km-value for D-glutamate compared to wild-type enzyme Limosilactobacillus fermentum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.26
-
D-glutamate pH 8, 30°C, wild-type enzyme Limosilactobacillus fermentum
0.33
-
L-glutamate pH 8, 30°C, wild-type enzyme Limosilactobacillus fermentum
1.1
-
L-glutamate pH 8, 30°C, mutant enzyme H186N Limosilactobacillus fermentum
1.2
-
D-glutamate pH 8, 30°C, mutant enzyme D10N Limosilactobacillus fermentum
1.3
-
L-glutamate pH 8, 30°C, mutant enzyme D10N Limosilactobacillus fermentum
3.5
-
D-glutamate pH 8, 30°C, mutant enzyme H152Q Limosilactobacillus fermentum
4.5
-
D-glutamate pH 8, 30°C, mutant enzyme H186N Limosilactobacillus fermentum
5.8
-
L-glutamate pH 8, 30°C, mutant enzyme H152Q Limosilactobacillus fermentum
35
-
L-glutamate pH 8, 30°C, mutant enzyme D36N Limosilactobacillus fermentum
41
-
D-glutamate pH 8, 30°C, mutant enzyme D36N Limosilactobacillus fermentum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate Limosilactobacillus fermentum
-
D-glutamate
-
r

Organism

Organism UniProt Comment Textmining
Limosilactobacillus fermentum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-glutamate = D-glutamate the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate Limosilactobacillus fermentum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
Limosilactobacillus fermentum D-glutamate
-
r
L-glutamate the enzyme provides bacteria with a source of D-glutamate for use in peptidoglycan biosynthesis Limosilactobacillus fermentum D-glutamate
-
?
additional information the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate Limosilactobacillus fermentum ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.045
-
L-glutamate pH 8, 30°C, mutant enzyme H186N Limosilactobacillus fermentum
0.063
-
D-glutamate pH 8, 30°C, mutant enzyme D10N Limosilactobacillus fermentum
0.068
-
L-glutamate pH 8, 30°C, mutant enzyme D10N Limosilactobacillus fermentum
0.093
-
D-glutamate pH 8, 30°C, mutant enzyme H186N Limosilactobacillus fermentum
20
-
L-glutamate pH 8, 30°C, mutant enzyme D36N Limosilactobacillus fermentum
22
-
D-glutamate pH 8, 30°C, mutant enzyme D36N and H152Q Limosilactobacillus fermentum
38
-
L-glutamate pH 8, 30°C, mutant enzyme H152Q Limosilactobacillus fermentum
68
-
D-glutamate pH 8, 30°C, wild-type enzyme Limosilactobacillus fermentum
69
-
L-glutamate pH 8, 30°C, wild-type enzyme Limosilactobacillus fermentum