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Literature summary extracted from

  • Newman, J.; Seabrook, S.; Surjadi, R.; Williams,C.C.; Lucent, D.; Wilding, M.; Scott, C.; Peat, T.S.
    Determination of the structure of the catabolic N-succinylornithine transaminase (AstC) from Escherichia coli (2013), PLoS One, 8, e58298.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.81 structure of apo and holo-Ast C and of the enzyme complexed with its physiological substrate, succinylornithine, to 2.2-2.75 A resolution. Docking studies support that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.81 0.284
-
 N2-succinyl-L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli
2.6.1.81 0.338
-
 N2-Acetyl-L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli
2.6.1.81 4.391
-
 L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.81 Escherichia coli A0A140N9B6
-
-
2.6.1.81 Escherichia coli BL21-DE3 A0A140N9B6
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.6.1.81 the holo-enzyme can be reconstituted by the addition of pyridoxal 5'-phosphate to the apo-protein. The reconstituted enzyme is more heat stable than the apo-protein Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.81 L-ornithine + 2-oxoglutarate
-
 Escherichia coli L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.81 L-ornithine + 2-oxoglutarate
-
 Escherichia coli BL21-DE3 L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.81 N2-acetyl-L-ornithine + 2-oxoglutarate
-
 Escherichia coli N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.81 N2-acetyl-L-ornithine + 2-oxoglutarate
-
 Escherichia coli BL21-DE3 N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.81 N2-succinyl-L-ornithine + 2-oxoglutarate
-
 Escherichia coli N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?
2.6.1.81 N2-succinyl-L-ornithine + 2-oxoglutarate
-
 Escherichia coli BL21-DE3 N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.81 AstC
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.6.1.81 43.5
-
 apo-protein Escherichia coli
2.6.1.81 46
-
 enzyme reconstituetd from apo-protein Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.81 3
-
 N2-succinyl-L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli
2.6.1.81 3.5
-
 L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli
2.6.1.81 4.7
-
 N2-Acetyl-L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.81 pyridoxal 5'-phosphate
-
 Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.6.1.81 0.8
-
 L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli
2.6.1.81 10.56
-
 N2-succinyl-L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli
2.6.1.81 13.9
-
 N2-Acetyl-L-ornithine pH 8.0, temperature not specified in the publication Escherichia coli