Dyer W E, Weaver L M, Zhao J M, Kuhn D N, Weller S C, Herrmann K M
Department of Horticulture, Purdue University, West Lafayette, Indiana 47907.
J Biol Chem. 1990 Jan 25;265(3):1608-14.
A cDNA encoding potato (Solanum tuberosum L.) 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, the first enzyme of the shikimate pathway, was cloned into phage lambda gt11. The clone represents the first cDNA for this enzyme from any eukaryotic source. The nucleotide sequence of the cDNA was determined, and its identity was confirmed through partial amino acid sequence analysis of the encoded enzyme. The cDNA contains a 1527-base pair open reading frame that encodes a polypeptide with a calculated molecular weight of 56,153. The amino terminus of the deduced polypeptide resembles a chloroplast transit sequence. Amino acid sequence identities between the mature potato enzyme and the homologous isoenzymes from Escherichia coli are only about 22%. The potato cDNA hybridized to various plant mRNAs that are all about 2 kilobases in size.
编码马铃薯(Solanum tuberosum L.)3-脱氧-D-阿拉伯庚酮糖酸-7-磷酸合酶(莽草酸途径的首个酶)的cDNA被克隆到噬菌体λgt11中。该克隆代表了来自任何真核生物来源的该酶的首个cDNA。测定了该cDNA的核苷酸序列,并通过对所编码酶的部分氨基酸序列分析证实了其身份。该cDNA包含一个1527个碱基对的开放阅读框,编码一个计算分子量为56,153的多肽。推导多肽的氨基末端类似于叶绿体转运序列。成熟马铃薯酶与来自大肠杆菌的同源同工酶之间的氨基酸序列同一性仅约为22%。马铃薯cDNA与各种大小均约为2千碱基的植物mRNA杂交。