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Literature summary for 5.1.1.3 extracted from

  • Yagasaki, M.; Iwata, K.; Ishino, S.; Azuma, M.; Ozaki, A.
    Cloning, purification, and properties of a cofactor-independent glutamate racemase from Lactobacillus brevis ATCC 8287 (1995), Biosci. Biotechnol. Biochem., 59, 610-614.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information cofactor-independent enzyme Levilactobacillus brevis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Levilactobacillus brevis

Inhibitors

Inhibitors Comment Organism Structure
additional information insensitive to carbonyl reagents such as hydroxylamine, phenylhydrazine, or NaBH4 Levilactobacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.94
-
D-Glu
-
Levilactobacillus brevis
6.39
-
L-Glu
-
Levilactobacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
1 * 29000, SDS-PAGE Levilactobacillus brevis
29430
-
calculation from nucleotide sequence Levilactobacillus brevis

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Levilactobacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
216
-
-
Levilactobacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glu
-
Levilactobacillus brevis L-Glu
-
?

Subunits

Subunits Comment Organism
monomer 1 * 29000, SDS-PAGE Levilactobacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Levilactobacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Levilactobacillus brevis