Literature summary for 5.1.1.13 extracted from

Long, Z.; Lee, J.A.; Okamoto, T.; Sekine, M.; Nimura, N.; Imai, K.; Yohda, M.; Maruyama, T.; Sumi, M.; Kamo, N.; Yamagishi, A.; Oshima, T.; Homma, H.
Occurrence of D-amino acids and a pyridoxal 5'-phosphate-dependent aspartate racemase in the acidothermophilic archaeon, Thermoplasma acidophilum (2001), Biochem. Biophys. Res. Commun., 281, 317-321.

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Inhibitors

Inhibitors	Comment	Organism	Structure
hydroxylamine	inclusion of hydroxylamine (1.0 mM and 10 mM) in the assay results in complete loss in the activity at 45°C, and also at 70°C where higher levels of activity are observed than at 45°C	Thermoplasma acidophilum
N-ethylmaleimide	-	Thermoplasma acidophilum

Organism

Organism	UniProt	Comment	Textmining
Thermoplasma acidophilum	-	-	-
Thermoplasma acidophilum HO-62	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1160	-	70°C, pH not specified in the publication	Thermoplasma acidophilum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate	the enzyme is highly selective for aspartate. No detectable racemase activity against Glu, Ala, Lys, Phe, or Ser in the assays incubated at 45°C. Even at 70°C, the racemase activity using Ala as a substrate is low	Thermoplasma acidophilum	D-aspartate	-	r
L-aspartate	the enzyme is highly selective for aspartate. No detectable racemase activity against Glu, Ala, Lys, Phe, or Ser in the assays incubated at 45°C. Even at 70°C, the racemase activity using Ala as a substrate is low	Thermoplasma acidophilum HO-62	D-aspartate	-	r

Synonyms

Synonyms	Comment	Organism
Asp racemase	-	Thermoplasma acidophilum

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	dependent on. Enzyme activity is very low in the absence of pyridoxal 5'-phosphate	Thermoplasma acidophilum

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Release 2023.1 (January 2023)