This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2oat
From Proteopedia
| Line 23: | Line 23: | ||
[[Category: pyridoxal phosphate]] | [[Category: pyridoxal phosphate]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:35:54 2007'' |
Revision as of 15:31, 30 October 2007
|
ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE
Overview
Ornithine aminotransferase (l-ornithine:2-oxoacid delta-aminotransferase;, EC 2.6.1.13), a pyridoxal-5'-phosphate-dependent mitochondrial enzyme, controls the l-ornithine level in tissues by catalyzing the transfer of, the delta-amino group of l-ornithine to 2-oxoglutarate, producing, l-glutamate- gamma-semialdehyde and l-glutamate. (2S, 5S)-5-Fluoromethylornithine is the only inhibitor exclusively specific for, ornithine aminotransferase known to date. Both in vitro and in vivo, it, blocks the enzyme by a suicide reaction leading to a covalent adduct with, the cofactor. The crystal structure of the enzyme-inhibitor complex was, solved at a resolution of 1.95 A. No significant conformational changes, compared with the native enzyme structure were observed. The structure, reveals the ... [(full description)]
About this Structure
2OAT is a [Single protein] structure of sequence from [Homo sapiens] with PFM as [ligand]. Active as [Ornithine aminotransferase], with EC number [2.6.1.13]. Structure known Active Sites: FMA, FMB and FMC. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine., Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN, J Mol Biol. 1999 Jan 8;285(1):297-309. PMID:9878407
Page seeded by OCA on Tue Oct 30 17:35:54 2007
