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Literature summary for 5.1.1.13 extracted from

  • Lamont, H.C.; Staudenbauer, W.L.; Strominger, J.L.
    Partial purification and characterization of an aspartate racemase from Streptococcus faecalis (1972), J. Biol. Chem., 247, 5103-5106.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information removal of some divalent cation by EDTA gives slight increase in activity Enterococcus faecalis
pyridoxal phosphate racemase contains bound pyridoxal phosphate Enterococcus faecalis

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoate)
-
Enterococcus faecalis
Mn2+
-
Enterococcus faecalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
25
-
L-Asp
-
Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis
-
strain ATCC 9790, strain IAM 10065, no activity in strain IAM 10067
-

Purification (Commentary)

Purification (Comment) Organism
-
Enterococcus faecalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala at half the rate of Asp Enterococcus faecalis D-Ala
-
?
L-Asp
-
Enterococcus faecalis D-Asp
-
?
additional information no racemase activity with Glu Enterococcus faecalis ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
thermal stability shows a bimodal dependence on pH, with minimum stability at pH 7.5, and remarkably stability at pH 6 and pH 8-9. 10 min, pH 8, 66% loss of activity Enterococcus faecalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 9
-
Enterococcus faecalis

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 thermal stability shows a bimodal dependence on pH, with minimum stability at pH 7.5, and remarkably stability at pH 6 and pH 8-9. 10 min, pH 8, 66% loss of activity Enterococcus faecalis