Affiliation:
1. Department of Molecular Genetics and Microbiology, Burroughs Wellcome Co., Research Triangle Park, North Carolina 27709.
Abstract
The Escherichia coli gene coding for dihydropteroate synthase (DHPS) has been cloned and sequenced. The protein has 282 amino acids and a compositional molecular mass of 30,314 daltons. Increased expression of the enzyme was realized by using a T7 expression system. The enzyme was purified and crystallized. A temperature-sensitive mutant was isolated and found to express a DHPS with a lower specific activity and lower affinities for para-aminobenzoic acid and sulfathiazole. The allele had a point mutation that changed a phenylalanine codon to a leucine codon, and the mutation was in a codon that is conserved among published DHPS sequences.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
96 articles.
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