Pisabarro A, Malumbres M, Mateos L M, Oguiza J A, Martín J F
Department of Ecology, Genetics and Microbiology, Faculty of Biology, University of León, Spain.
J Bacteriol. 1993 May;175(9):2743-9. doi: 10.1128/jb.175.9.2743-2749.1993.
The dapA and dapB genes, encoding, respectively, dihydrodipicolinate synthase and dihydrodipicolinate reductase, the two first enzymes of the lysine branch of the aspartic amino acid family, were cloned from the DNA of the amino acid-producing bacterium Brevibacterium lactofermentum. The two genes were clustered in a 3.5-kb Sau3AI-BamHI fragment but were separated by an open reading frame of 750 nucleotides. The protein encoded by this open reading frame had little similarity to any protein in the data banks, and its function remains unknown. The three genes were translated in Escherichia coli, giving the corresponding polypeptides.
分别编码二氢吡啶二羧酸合酶和二氢吡啶二羧酸还原酶(天冬氨酸氨基酸家族赖氨酸分支的头两种酶)的dapA和dapB基因,是从产氨基酸细菌乳酸发酵短杆菌的DNA中克隆出来的。这两个基因聚集在一个3.5kb的Sau3AI - BamHI片段中,但被一个750个核苷酸的开放阅读框隔开。这个开放阅读框编码的蛋白质与数据库中的任何蛋白质几乎没有相似性,其功能仍然未知。这三个基因在大肠杆菌中进行了翻译,产生了相应的多肽。