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Literature summary extracted from

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.3 hydroxylamine
-
 Lactiplantibacillus plantarum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 3.6
-
 D-Glu
-
 Lactiplantibacillus plantarum

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Lactiplantibacillus plantarum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3
-
 Lactiplantibacillus plantarum

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 additional information
-
-
 Lactiplantibacillus plantarum

Storage Stability

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

Substrates and Products (Substrate)

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

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.3 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