Graham I A, Smith L M, Brown J W, Leaver C J, Smith S M
Department of Botany, University of Edinburgh, Scotland, UK.
Plant Mol Biol. 1989 Dec;13(6):673-84. doi: 10.1007/BF00016022.
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% 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.
已确定了编码黄瓜乙醛酸循环体酶苹果酸合酶的全长cDNA克隆和基因组克隆的完整序列。这些序列使我们能够识别该基因5'端的假定调控区域、三个内含子以及3'端可能的可变聚腺苷酸化位点。推导的氨基酸序列预测出一种分子量为64,961的多肽，它与大肠杆菌的多肽具有48%的同一性。将黄瓜苹果酸合酶的序列与大肠杆菌以及其他乙醛酸循环体和过氧化物酶体酶的序列进行比较，结果表明保守的C末端三肽是那些导入微体的酶的共同特征。
