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 5' end of the gene, three introns, and possible alternative polyadenylation sites at the 3' end. The deduced amino acid sequence predicts a polypeptide of 64 961 molecular weight, which has 48 ~o 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.

Item Type:	Refereed Article
Keywords:	malate synthase, gene structure, glyoxylate cycle, glyoxysomes, Cucumis sativus
Research Division:	Biological Sciences
Research Group:	Plant Biology
Research Field:	Plant Physiology
Objective Division:	Expanding Knowledge
Objective Group:	Expanding Knowledge
Objective Field:	Expanding Knowledge in the Biological Sciences
UTAS Author:	Smith, SM (Professor Steven Smith)
ID Code:	101605
Year Published:	1989
Web of Science® Times Cited:	51
Deposited By:	Plant Science
Deposited On:	2015-06-26
Last Modified:	2015-09-24
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