Sankar P, Lee J H, Shanmugam K T
Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.
J Bacteriol. 1988 Dec;170(12):5440-5. doi: 10.1128/jb.170.12.5440-5445.1988.
Synthesis of formate dehydrogenase coupled to formate hydrogenlyase activity in Escherichia coli was found to require the product of the fhlA gene. Transcription of fdhF, the gene coding for the 80-kilodalton (kDa) selenopeptide of formate dehydrogenase, was not detected in an fhlA genetic background. Mutations in the fhlA gene also abolished production of the hydrogenase activity associated with formate hydrogenlyase activity. The fhlA gene resides next to the hydB gene at 59 min in the E. coli chromosome, and the two genes are transcribed in opposite directions. The fhlA gene codes for a 78-kDa protein. A neighboring gene, fdv, codes for an 82-kDa protein, and the physiological role of this gene product is unknown, although a role in H2 metabolism can be detected.
在大肠杆菌中,与甲酸氢裂解酶活性偶联的甲酸脱氢酶的合成被发现需要fhlA基因的产物。在fhlA基因背景中未检测到fdhF(编码80千道尔顿(kDa)甲酸脱氢酶硒肽的基因)的转录。fhlA基因中的突变也消除了与甲酸氢裂解酶活性相关的氢化酶活性的产生。fhlA基因位于大肠杆菌染色体59分钟处的hydB基因旁边,这两个基因以相反方向转录。fhlA基因编码一种78-kDa的蛋白质。一个相邻基因fdv编码一种82-kDa的蛋白质,尽管可以检测到该基因产物在H2代谢中的作用,但其生理作用尚不清楚。