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AbstractThe gene coding for folylpoly-()-glutamate synthetase (FPGS)-dihydrofolate synthetase (DHFS) of Neisseria gonorrhoeae (Ngo) has been cloned by functional complementation of an Escherichia coli folC mutant (SF4). The sequence encodes a 224-residue protein of 46.4kDa. It shows 46% identity to the E. coli FPGS-DHFS and 29% identity to the FPGS of Lactobacillus casei. Sequence comparisons between...
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