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Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase

Nature Structural Biology volume 2, pages 548–553 (1995)Cite this article

An Erratum to this article was published on 01 August 1995

Abstract

Mutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine aminotransferase 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.

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Authors and Affiliations

  1. Department of Structural Biology, Boizentrum, University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland

    Vladimir N. Malashkevich & Johan N. Jansonius

  2. Molecular and Cell Biology Department, University of California, Barker Hall, Berkeley, California, 94720, USA

    James J. Onuffer & Jack F. Kirsch

Authors
  1. Vladimir N. Malashkevich
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  2. James J. Onuffer
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  3. Jack F. Kirsch
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  4. Johan N. Jansonius
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Malashkevich, V., Onuffer, J., Kirsch, J. et al. Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nat Struct Mol Biol 2, 548–553 (1995). https://doi.org/10.1038/nsb0795-548

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