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The malate synthase gene of cucumber
Authors:Ian A. Graham  Laura M. Smith  John W. S. Brown  Christopher J. Leaver  Steven M. Smith
Affiliation:(1) Department of Botany, The Kings Buildings, University of Edinburgh, Mayfield Road, EH9 3JH Edinburgh, Scotland, UK;(2) Present address: Department of Biochemistry, University of Leeds, LS2 9JT Leeds, England, UK;(3) Present address: Department of Biological Sciences, The University, DD1 4HN Dundee, Scotland, UK
Abstract:The complete sequences of a full-length cDNA clone and a genomic clone encoding the Cucumis sativus glyoxysomal enzyme malate synthase, have been determined. The sequences have enabled us to identify putative control regions at the 5prime end of the gene, three introns, and possible alternative polyadenylation sites at the 3prime end. The deduced amino acid sequence predicts a polypeptide of 64961 molecular weight, which has 48% identity with that of Escherichia coli. Comparison of the sequence of malate synthase from cucumber with that from E. coli and with other glyoxysomal and peroxisomal enzymes, shows that a conserved C-terminal tripeptide is a common feature of those enzymes imported into microbodies.
Keywords:malate synthase  gene structure  glyoxylate cycle  glyoxysomes  Cucumis sativus
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