2byl

From Proteopedia
Revision as of 13:55, 30 October 2007 by OCA (talk | contribs)
Jump to navigation Jump to search
File:2byl.gif


2byl, resolution 2.15Å

Drag the structure with the mouse to rotate

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 13:00:32 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA