Klein B, Pawlowski K, Höricke-Grandpierre C, Schell J, Töpfer R
Max-Planck-Institut für Züchtungsforschung, Köln, FRG.
Mol Gen Genet. 1992 May;233(1-2):122-8. doi: 10.1007/BF00587569.
A cDNA encoding beta-ketoacyl-ACP reductase (EC 1.1.1.100), an integral part of the fatty acid synthase type II, was cloned from Cuphea lanceolata. This cDNA of 1276 bp codes for a polypeptide of 320 amino acids with 63 N-terminal residues presumably representing a transit peptide and 257 residues corresponding to the mature protein of 27 kDa. The encoded protein shows strong homology with the amino-terminal sequence and two tryptic peptides from avocado mesocarp beta-ketoacyl-ACP reductase, and its total amino acid composition is highly similar to those of the beta-ketoacyl-ACP reductases of avocado and spinach. Amino acid sequence homologies to polyketide synthase, beta-ketoreductases and short-chain alcohol dehydrogenases are discussed. An engineered fusion protein lacking most of the transit peptide, which was produced in Escherichia coli, was isolated and proved to possess beta-ketoacyl-ACP reductase activity. Hybridization studies revealed that in C. lanceolata beta-ketoacyl-ACP reductase is encoded by a small family of at least two genes and that members of this family are expressed in roots, leaves, flowers and seeds.
从柳叶菜（Cuphea lanceolata）中克隆出一个编码β-酮脂酰-ACP还原酶（EC 1.1.1.100）的cDNA，该酶是II型脂肪酸合酶的一个组成部分。这个1276 bp的cDNA编码一个由320个氨基酸组成的多肽，其中63个N端残基可能代表转运肽，257个残基对应于27 kDa的成熟蛋白。编码的蛋白质与鳄梨中果皮β-酮脂酰-ACP还原酶的氨基端序列和两个胰蛋白酶肽段具有很强的同源性，其总氨基酸组成与鳄梨和菠菜的β-酮脂酰-ACP还原酶高度相似。文中讨论了其与聚酮合酶、β-酮还原酶和短链醇脱氢酶的氨基酸序列同源性。在大肠杆菌中产生的一种缺少大部分转运肽的工程融合蛋白被分离出来，并被证明具有β-酮脂酰-ACP还原酶活性。杂交研究表明，在柳叶菜中，β-酮脂酰-ACP还原酶由一个至少包含两个基因的小家族编码，该家族成员在根、叶、花和种子中均有表达。
