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Literature summary for 5.1.1.3 extracted from

  • Glaser, L.
    Glutamic acid racemase from Lactobacillus arabinosus (1960), J. Biol. Chem., 235, 2095-2098.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
hydroxylamine
-
Lactiplantibacillus plantarum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6
-
D-Glu
-
Lactiplantibacillus plantarum

Organism

Organism UniProt Comment Textmining
Lactiplantibacillus plantarum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Lactiplantibacillus plantarum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Lactiplantibacillus plantarum

Storage Stability

Storage Stability Organism
enzyme can be kept frozen at all stages of the purification for several weeks without loss of activity Lactiplantibacillus plantarum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glu
-
Lactiplantibacillus plantarum L-Glu
-
?
additional information enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu Lactiplantibacillus plantarum ?
-
?

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 6.5: 90% of the activity at pH 7.5, routinely assayed at pH 7.5, 8.5: 70% of the activity at pH 7.5 Lactiplantibacillus plantarum