| Autor: |
Dallas, W S, Gowen, J E, Ray, P H, Cox, M J, Dev, I K |
| Zdroj: |
Journal of Bacteriology; September 1992, Vol. 174 Issue: 18 p5961-5970, 10p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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