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2.6.1.11 |
| Description |
Acetylornithine aminotransferase. |
| Alternative names |
acetylornithine 5-aminotransferase
N-acetylornithine-delta-transaminase |
| Catalyzed reaction |
N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. |
| Cofactor |
Pyridoxal-phosphate. |
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This E. coli enzyme exhibits also succinyldiaminopimelate aminotransferase activity (2.6.1.17), and shows similar specificity constants for N-acetylornithine and N-succinyldiaminopimelate. |
| Prosite |
PROSITE; PDOC00519; |
| Organisms |
-Bacteria -Archea -Plants -Fungi |
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Family |
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| Links |
Enzyme (activities) 2.6.1.11
BRENDA (activities) 2.6.1.11
KEGG (pathways) 2.6.1.11
PLPMDB (PLP mutants) 2.6.1.11
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| References |
Rajaram V, Prasad K, Ratna Prasuna P, Ramachandra N, Bharath SR, Savithri HS, Murthy MR. (2006) Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the biosynthetic N-acetylornithine aminotransferases from Salmonella typhimurium and Escherichia coli Acta Crystallogr Sect F Struct Biol Cryst Commun 62 980-3. Ledwidge, R.; Blanchard, J.S. (1999) The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis.
Biochemistry 38 3019-24.. Heimberg, H.; Boyen, A.; Crabeel, M.; Glansdorff, N. (1990) Escherichia coli and Saccharomyces cerevisiae acetylornithine aminotransferase: evolutionary relationship with ornithine aminotransferase Gene 90 69-78.. Articles on 2.6.1.11 |
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| last changed |
2007/09/20 18:44 |
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