|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
In Pathway: arginine degradation II (AST pathway)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: arginine N-succinyltransferase
Enzyme Commission Synonyms: arginine succinyltransferase, AstA, arginine and ornithine N2-succinyltransferase, AOST, AST, succinyl-CoA:L-arginine 2-N-succinyltransferase
Enzyme Commission Summary:
Also acts on L-ornithine. This is the first enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [Vander88]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 188.8.131.52 (arginine N-succinyltransferase), EC 184.108.40.206 (N-succinylarginine dihydrolase), EC 220.127.116.11 (succinylornithine transaminase), EC 18.104.22.168 (succinylglutamate-semialdehyde dehydrogenase) and EC 22.214.171.124 (succinylglutamate desuccinylase) [Vander85, Cunin86].
Itoh97: Itoh Y (1997). "Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa." J Bacteriol 179(23);7280-90. PMID: 9393691
Tricot94: Tricot C, Vander Wauven C, Wattiez R, Falmagne P, Stalon V (1994). "Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine." Eur J Biochem 224(3);853-61. PMID: 7523119
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