Chao Y F, Weng S F, Lin J W
Institute of Molecular Biology, National Chung Hsing University, Taichung, Taiwan, ROC.
Gene. 1993 Apr 15;126(1):155-6. doi: 10.1016/0378-1119(93)90606-4.
The nucleotide sequence of luxD (EMBL accession No. X65611), encoding acyltransferase (ACT), of the lux operon from Photobacterium leiognathi PL741 was determined, and the amino acid (aa) sequence was deduced. ACT is a component of the fatty acid reductase complex, which is responsible for converting fatty acid to aldehyde that serves as the substrate in the luciferase-catalyzed bioluminescent reactions. The protein has a calculated M(r) of 34,384 and comprises 305 aa residues. Alignment and comparison of the ACT of P. leiognathi with that of Vibrio fischeri ATCC7744, V. harveyi B392 and Xenorhabdus luminescens Hm shows that there is 66%, 59% and 61% aa identity, respectively.
测定了来自利氏发光杆菌PL741的lux操纵子中编码酰基转移酶(ACT)的luxD(EMBL登录号:X65611)的核苷酸序列,并推导了氨基酸(aa)序列。ACT是脂肪酸还原酶复合物的一个组成部分,该复合物负责将脂肪酸转化为醛,醛作为荧光素酶催化的生物发光反应中的底物。该蛋白质的计算分子量(M(r))为34384,由305个氨基酸残基组成。将利氏发光杆菌的ACT与费氏弧菌ATCC7744、哈氏弧菌B392和发光异小杆线虫Hm的ACT进行比对和比较,结果显示氨基酸同一性分别为66%、59%和61%。