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Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid

By P.T. Erskine, L. Coates, R. Newbold, A.A. Brindley, F. Stauffer, G.D.E Beaven, R. Gill, A. Coker, S.P. Wood, M.J. Warren, P.M. Shoolingin-Jordan, R. Neier and J.B. Cooper

Abstract

The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A ° . The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA)

Topics: QD, QH301
Year: 2005
OAI identifier: oai:eprints.soton.ac.uk:24094
Provided by: e-Prints Soton
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