一种来自戈登氏菌属的邻苯二甲酸单-2-乙基己酯水解酶，该酶能够异化邻苯二甲酸二-2-乙基己酯。
A mono-2-ethylhexyl phthalate hydrolase from a Gordonia sp. that is able to dissimilate di-2-ethylhexyl phthalate.
作者信息
Nishioka Tuguhiro, Iwata Makoto, Imaoka Takuya, Mutoh Maiko, Egashira Yoshihiro, Nishiyama Takashi, Shin Takashi, Fujii Takao
机构信息
Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto 860-0082, Japan.
出版信息
Appl Environ Microbiol. 2006 Apr;72(4):2394-9. doi: 10.1128/AEM.72.4.2394-2399.2006.
Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The K(m) and V(max) values for mono-2-ethylhexyl phthalate were 26.9 +/- 4.3 microM and 18.1 +/- 0.9 micromol/min . mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% homology with those of meta-cleavage hydrolases which are serine hydrolases but exhibited no significant homology with the sequences of serine esterases. The pentapeptide motif GXSXG, which is conserved in serine hydrolases, was present in the sequence. The enzymatic properties and features of the primary structure suggested that this enzyme is a novel enzyme belonging to an independent group of serine hydrolases.
戈登氏菌属菌株P8219是从被机油污染的土壤中分离出来的，能够分解邻苯二甲酸二（2-乙基己基）酯。从该菌株的细胞提取物中纯化出了邻苯二甲酸单（2-乙基己基）酯水解酶。这种酶是一种分子量为32,164道尔顿的同二聚体蛋白，它能有效水解单邻苯二甲酸酯，如邻苯二甲酸单乙酯、单丁酯、单己酯和邻苯二甲酸单（2-乙基己基）酯。邻苯二甲酸单（2-乙基己基）酯的K(m)和V(max)值分别为26.9±4.3微摩尔和18.1±0.9微摩尔/分钟·毫克蛋白。该酶推导的氨基酸序列与作为丝氨酸水解酶的间位裂解水解酶的序列同源性低于30%，但与丝氨酸酯酶的序列没有显著同源性。丝氨酸水解酶中保守的五肽基序GXSXG存在于该序列中。酶学性质和一级结构特征表明，这种酶是一种属于丝氨酸水解酶独立组的新型酶。
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