Zywno-van Ginkel S, Dooley T P, Suling W J, Barrow W W
Southern Research Institute, Birmingham, AL 35205, USA.
FEMS Microbiol Lett. 1997 Nov 1;156(1):69-78. doi: 10.1111/j.1574-6968.1997.tb12707.x.
Dihydrofolate reductase is an essential bacterial enzyme necessary for the maintenance of intracellular folate pools in a biochemically active reduced state. In this report, the Mycobacterium avium folA gene was identified by functional genetic complementation, sequenced, and expressed for the first time. It has an open reading frame of 543 bp with a G + C content of 73%. The translated polypeptide sequence shows 58% identity to the consensus sequence of the conserved regions from eight other bacterial dihydrofolate reductases. Recombinant M. avium dihydrofolate reductase was expressed actively in Escherichia coli, and SDS-PAGE analysis revealed a 20 kDa species, agreeable with that predicted from the polypeptide sequence:
二氢叶酸还原酶是一种必需的细菌酶，对于维持细胞内叶酸池处于生化活性还原状态至关重要。在本报告中，通过功能基因互补鉴定了鸟分枝杆菌folA基因，首次对其进行测序并表达。它有一个543 bp的开放阅读框，G + C含量为73%。翻译后的多肽序列与其他八种细菌二氢叶酸还原酶保守区域的共有序列有58%的同一性。重组鸟分枝杆菌二氢叶酸还原酶在大肠杆菌中得到了有效表达，SDS-PAGE分析显示有一个20 kDa的条带，与从多肽序列预测的结果一致：
