Cheng T, Liu L, Wang B, Wu J, DeFrank J J, Anderson D M, Rastogi V K, Hamilton A B
US Army Edgewood Research, Development, and Engineering Center, Aberdeen Proving Ground, MD 21010, USA.
J Ind Microbiol Biotechnol. 1997 Jan;18(1):49-55. doi: 10.1038/sj.jim.2900358.
Organophosphorus acid anhydrolases (OPAA) catalyzing the hydrolysis of a variety of toxic organophosphorus cholinesterase inhibitors offer potential for decontamination of G-type nerve agents and pesticides. The gene (opa) encoding an OPAA was cloned from the chromosomal DNA of Alteromonas haloplanktis ATCC 23821. The nucleotide sequence of the 1.7 -kb DNA fragment contained the opa gene (1.3 kb) and its flanking region. We report structural and functional similarity of OPAAs from A. haloplanktis and Alteromonas sp JD6.5 with the enzyme prolidase that hydrolyzes dipeptides with a prolyl residue in the carboxyl-terminal position. These results corroborate the earlier conclusion that the OPAA is a type of X-Pro dipeptidase, and that X-Pro could be the native substrate for such an enzyme in Alteromonas cells.
催化多种有毒有机磷胆碱酯酶抑制剂水解的有机磷酸酐酶（OPAA）为G型神经毒剂和杀虫剂的净化提供了可能。从嗜盐栖热袍菌ATCC 23821的染色体DNA中克隆了编码OPAA的基因（opa）。1.7kb DNA片段的核苷酸序列包含opa基因（1.3kb）及其侧翼区域。我们报道了嗜盐栖热袍菌和JD6.5交替单胞菌的OPAA与脯氨酰二肽酶在结构和功能上的相似性，脯氨酰二肽酶可水解在羧基末端位置带有脯氨酰残基的二肽。这些结果证实了早期的结论，即OPAA是一种X-脯氨酰二肽酶，并且X-脯氨酰可能是交替单胞菌细胞中这种酶的天然底物。
