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Literature summary extracted from

  • Diven, W.F.
    Studies on amino acid racemase. II. Purification and properties of the glutamate racemase from Lactobacillus fermenti (1969), Biochim. Biophys. Acta, 191, 702-706.
    View publication on PubMed

General Stability

EC Number General Stability Organism
5.1.1.3 stabilized in presence of mercaptoethanol and other sulfhydryl containing compounds Limosilactobacillus fermentum

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.3 3-hydroxypropyl FAD
-
 Limosilactobacillus fermentum
5.1.1.3 4-Hydroxypropyl FAD
-
 Limosilactobacillus fermentum
5.1.1.3 FAD
-
 Limosilactobacillus fermentum
5.1.1.3 FMN
-
 Limosilactobacillus fermentum
5.1.1.3 hydroxylamine
-
 Limosilactobacillus fermentum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 additional information
-
 additional information
-
 Limosilactobacillus fermentum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.3 23000
-
 gel filtration Limosilactobacillus fermentum

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Limosilactobacillus fermentum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3
-
 Limosilactobacillus fermentum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.1.3 7.7
-
-
 Limosilactobacillus fermentum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.3 D-Glu
-
 Limosilactobacillus fermentum L-Glu
-
 ?