PMID:1522070
| Citation |
Dallas, WS, Gowen, JE, Ray, PH, Cox, MJ and Dev, IK (1992) Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100. J. Bacteriol. 174:5961-70 |
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| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA Mutational Analysis; Dihydropteroate Synthase/biosynthesis; Dihydropteroate Synthase/genetics; Dihydropteroate Synthase/isolation & purification; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Gene Library; Genetic Complementation Test; Molecular Sequence Data; Mutagenesis; Nucleic Acid Conformation; RNA, Messenger; Recombinant Proteins/biosynthesis; Sequence Homology, Nucleic Acid |
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