Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100.

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Dallas WS,Gowen JE,Ray PH,Cox MJ,Dev IK

doi

10.1128/jb.174.18.5961-5970.1992

keywords:

subject

Has Abstract

pub_date

1992-09-01 00:00:00

pages

5961-70

issue

18

eissn

0021-9193

issn

1098-5530

journal_volume

174

pub_type

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