Location and sequence analysis of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase-encoding gene (bpdF) of the biphenyl/polychlorinated biphenyl degradation pathway in Rhodococcus sp M5

被引：17

作者：

Lau, PCK

Garnon, J

Labbe, D

Ying, W

机构：

[1] Biotechnology Research Institute, National Research Council of Canada, Montréal

[2] Biotechnology Research Institute, National Research Council of Canada, Montréal, Que. H4P 2R2

来源：

GENE | 1996年 / 171卷 / 01期

关键词：

biodegradation; PCB; aromatic metabolism; serine hydrolase; alpha/beta hydrolase-fold; nocardioform actinomycete; pseudomonads; Gram(+) bacteria; primordial serine codon;

D O I：

10.1016/0378-1119(96)00025-X

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

The 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate (HOPD) hydrolase-encoding gene (bpdF) in the biphenyl (BP)/polychlorinated biphenyl (PCB)-degrading bacterium, Rhodococcus sp. M5 (M5), was found to be located within a 4.5-kb HindIII-BamHI genomic DNA that was 5.4 kb downstream from the bpdC1C2BADE gene cluster. The deduced amino acid (aa) sequence of bpdF revealed that the hydrolase contains 297 aa (32 679 Da) that was verified by expression in the Escherichia coli T7 RNA polymerase/promoter system. Unlike previously known HOPD hydrolases, the aa sequence of BpdF appears unique. Interestingly, all HOPD hydrolases and related proteins from the phenol and toluene/ xylene degradation pathways, were found to have a bias in the codon usage in the catalytic Ser within the conserved VGNS(M/F)GG motif.

引用

页码：53 / 57

页数：5

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