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J Bacteriol. 1993 May; 175(9): 2743-2749

research-article

A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate reductase, and a third polypeptide of unknown function.

A Pisabarro, M Malumbres, L M Mateos, J A Oguiza and J F Martín

Department of Ecology, Genetics and Microbiology, Faculty of Biology, University of León, Spain.

ABSTRACT

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.

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J Bacteriol. 1993 May; 175(9): 2743-2749