Three-dimensional structure of microbial 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HPDA) hydrolase (BphD enzyme) from Rhodococcus sp. strain RHA1, in the PCB degradation pathway

被引:15
|
作者
Nandhagopal, N [1 ]
Senda, T [1 ]
Hatta, T [1 ]
Yamada, A [1 ]
Masai, E [1 ]
Fukuda, M [1 ]
Mitsui, Y [1 ]
机构
[1] OKAYAMA UNIV SCI, RES INST TECHNOL, OKAYAMA 703, JAPAN
关键词
BphD; crystal structure; hydrolase; PCB degradation; alpha beta hydrolase fold; protein structure;
D O I
10.2183/pjab.73.154
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The three-dimensional structure of an enzyme, 2-hydroxyl-6-oxo-6-phenylhexa-2,4-dienoic acid (HPDA) hydrolase (conventionally called BphD) from Rhodococcus sp. strain RHA1 has been solved by X-ray crystal structure analysis. This enzyme hydrolyzes one of the highly reactive intermediates, the meta cleavage product of the reaction catalyzed by 2,3-dihydroxybiphenyl dioxygenase, in the metabolic pathway degrading biphenyl compounds including the notorious environmental pollutant PCBs (polychlorinated biphenyls). By virtue of this and several other enzymes, the biphenyl compounds including PCBs are finally introduced into the tricarboxylic acid cycle. The BphD enzyme is an oligomeric enzyme made up of eight identical subunits each of 285 amino acid residues. The subunit consists of two domains, alpha/beta domain and alpha domain, between which the active site is located.
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页码:154 / 157
页数:4
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