|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
|Bacillus subtilis :||ornithine acetyltransferase
|Saccharomyces cerevisiae :||acetylornithine acetyltransferase
In Pathway: L-arginine biosynthesis II (acetyl cycle)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: glutamate N-acetyltransferase
Enzyme Commission Synonyms: ornithine transacetylase, α-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, acetylglutamate synθse, acetylglutamate-acetylornithine transacetylase, acetylglutamic synθse, acetylglutamic-acetylornithine transacetylase, acetylornithinase, acetylornithine glutamate acetyltransferase, glutamate acetyltransferase, N-acetyl-L-glutamate synθse, N-acetylglutamate synthase, N-acetylglutamate synθse, ornithine acetyltransferase, 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -1.2482033 [Latendresse13]
Enzyme Commission Summary:
Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
Relationship Links: BRENDA:EC:22.214.171.124 , ENZYME:EC:126.96.36.199 , IUBMB-ExplorEnz:EC:188.8.131.52 , UniProt:RELATED-TO:P38434 , UniProt:RELATED-TO:P74122 , UniProt:RELATED-TO:Q04728 , UniProt:RELATED-TO:Q07908 , UniProt:RELATED-TO:Q57645
Staub66: Staub M, Denes G (1966). "Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I. Purification and properties of ornithine acetyltransferase." Biochim Biophys Acta 128(1);82-91. PMID: 5972370
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