Lau P C, Garnon J, Labbé D, Wang Y
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec, Canada.
Gene. 1996 May 24;171(1):53-7. doi: 10.1016/0378-1119(96)00025-x.
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 (32679 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.
在联苯（BP）/多氯联苯（PCB）降解菌红球菌属M5（M5）中，编码2-羟基-6-氧代-6-苯基己-2,4-二烯酸酯（HOPD）水解酶的基因（bpdF）位于一段4.5 kb的HindIII - BamHI基因组DNA内，该DNA位于bpdC1C2BADE基因簇下游5.4 kb处。bpdF推导的氨基酸（aa）序列显示，该水解酶含有297个氨基酸（32679 Da），这通过在大肠杆菌T7 RNA聚合酶/启动子系统中的表达得到了验证。与先前已知的HOPD水解酶不同，BpdF的氨基酸序列显得独特。有趣的是，在苯酚和甲苯/二甲苯降解途径中，所有HOPD水解酶及相关蛋白在保守的VGNS(M/F)GG基序内催化丝氨酸的密码子使用上都存在偏向性。
