Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | DHPS_2 |
Description
All organisms require reduced folate cofactors for the synthesis of a variety
of metabolites. Most microorganisms must synthesize folate de novo because
they lack the active transport system of higher vertebrate cells which allows
these organisms to use dietary folates. Enzymes that are involved in the
biosynthesis of folates are therefore the target of a variety of antimicrobial
agents such as trimethoprim or sulfonamides.
Dihydropteroate synthase (EC 2.5.1.15) (DHPS) catalyzes the condensation of
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate to para-aminobenzoic acid
to form 7,8-dihydropteroate. This is the second step in the three steps
pathway leading from 6-hydroxymethyl-7,8-dihydropterin to 7,8-dihydrofolate.
DHPS is the target of sulfonamides which are substrates analog that compete
with para-aminobenzoic acid.
Bacterial DHPS (gene sul or folP)
[1] is a protein of about 275 to 315 amino
acid residues which is either chromosomally encoded or found on various
antibiotic resistance plasmids. In the lower eukaryote Pneumocystis carinii,
DHPS is the C-terminal domain of a multifunctional folate synthesis enzyme
(gene fas) [2].
We developed two signature patterns for DHPS, the first signature is located
in the N-terminal section of these enzymes, while the second signature is
located in the central section.
References
1.An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene. Slock J, Stahly DP, Han CY, Six EW, Crawford IP. J. Bacteriol. 172, 7211-26, (1990). View articlePMID: 2123867