Literature summary for 2.6.1.81 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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]

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	A0A140N9B6	-	-
Escherichia coli BL21-DE3	A0A140N9B6	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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)

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

Synonyms

Synonyms	Comment	Organism
AstC	-	Escherichia coli

Temperature Stability [°C]

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

Turnover Number [1/s]

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

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Escherichia coli

kcat/KM [mM/s]

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