2byl: Difference between revisions
No edit summary |
No edit summary |
||
| Line 30: | Line 30: | ||
[[Category: transit peptide]] | [[Category: transit peptide]] | ||
''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 16:52:20 2007'' | ||
Revision as of 17:47, 30 October 2007
|
STRUCTURE OF ORNITHINE AMINOTRANSFERASE TRIPLE MUTANT Y85I Y55A G320F
OverviewOverview
Ornithine aminotransferase and 4-aminobutyrate aminotransferase are, related pyridoxal phosphate-dependent enzymes having different substrate, specificities. The atomic structures of these enzymes have shown (i) that, active site differences are limited to the steric positions occupied by, two tyrosine residues in ornithine aminotransferase and (ii) that, uniquely among related, structurally characterized aminotransferases, the, conserved arginine that binds the alpha-carboxylate of alpha-amino acids, interacts tightly with a glutamate residue. To determine the contribution, of these residues to the specificities of the enzymes, we analyzed, site-directed mutants of ornithine aminotransferase by rapid reaction, kinetics, x-ray crystallography, and 13C NMR spectroscopy. Mutation of one, ... [(full description)]
About this StructureAbout this Structure
2BYL is a [Single protein] structure of sequence from [Homo sapiens] with PLP as [ligand]. Active as [Ornithine aminotransferase], with EC number [2.6.1.13]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Determinants of substrate specificity in omega-aminotransferases., Markova M, Peneff C, Hewlins MJ, Schirmer T, John RA, J Biol Chem. 2005 Oct 28;280(43):36409-16. Epub 2005 Aug 11. PMID:16096275
Page seeded by OCA on Tue Oct 30 16:52:20 2007