PMID:7664122

Citation	Malashkevich, VN, Onuffer, JJ, Kirsch, JF and Jansonius, JN (1995) Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nat. Struct. Biol. 2:548-53
Abstract	Mutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine amino-transferase without loss of aspartate transaminase activity. X-ray crystallographic analysis of key inhibitor complexes of the hexamutant reveals the structural basis for this substrate selectivity. It appears that tyrosine aminotransferase achieves nearly equal affinities for a wide range of amino acids by an unusual conformational switch. An active-site arginine residue either shifts its position to electrostatically interact with charged substrates or moves aside to allow access of aromatic ligands.
Links	PubMed
Keywords	Arginine; Aspartate Aminotransferases/metabolism; Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Tyrosine Transaminase/metabolism
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.