Dihydropteroate synthase

Dihydropteroate synthase
Tetrahydrofolate synthesis pathway
Identifiers
EC number	2.5.1.15
CAS number	9055-61-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles

Pterin binding enzyme
Identifiers
Symbol	Pterin_bind
Pfam	PF00809
InterPro	IPR000489
PROSITE	PDOC00630
SCOP	1ajz
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

Dihydropteroate synthetase is an enzyme classified under EC 2.5.1.15. It produces dihydropteroate in bacteria, but it is not expressed in most eukaryotes including humans. This makes it a useful target for sulfonamide antibiotics, which compete with the PABA precursor.

• (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate (PABA) $\rightleftharpoons$ diphosphate + dihydropteroate.

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 that allows these organisms to use dietary folates. Proteins containing this domain include dihydropteroate synthase (EC 2.5.1.15) as well as a group of methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulphur protein methyltransferase (MeTr) Q46389 that catalyses a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation.

Dihydropteroate synthase (EC 2.5.1.15) (DHPS) catalyses 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-step pathway leading from 6-hydroxymethyl-7,8-dihydropterin to 7,8-dihydrofolate. DHPS is the target of sulphonamides, which are substrate analogues that compete with para-aminobenzoic acid. Bacterial DHPS (gene sul or folP)^[1] is a protein of about 275 to 315 amino acid residues that 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].

References

1. ^ Crawford IP, Slock J, Stahly DP, Six EW, Han CY (1990). "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". J. Bacteriol. 172 (12): 7211–7226. PMID 2123867. 
2. ^ Volpe F, Dyer M, Scaife JG, Darby G, Stammers DK, Delves CJ (1992). "The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase". Gene 112 (2): 213–218. doi:10.1016/0378-1119(92)90378-3. PMID 1313386. 

External links

• MeSH Dihydropteroate+synthetase

This article includes text from the public domain Pfam and InterPro IPR000489

This enzyme-related article is a stub. You can help Wikipedia by expanding it.v · Categories: Enzyme stubs EC 2.5.1 Wikimedia Foundation. 2010. Игры ⚽ Нужен реферат? 2-Amino-4-hydroxy-6-pyrophosphoryl-methylpteridine Dihydropteroate synthase inhibitor Look at other dictionaries: Dihydropteroate synthase inhibitor — A dihydropteroate synthetase inhibitor is a drug that inhibits the action of dihydropteroate synthetase. Most are sulfonamides. Tetrahydrofolate synthesis pathway In bacteria, antibacterial sulfonamides act as competitive inhibitors of the enzyme …   Wikipedia Dihydrofolate synthase — Identifiers EC number 6.3.2.12 CAS number 37318 62 0 …   Wikipedia Sulfanilamide — Général Nom IUPAC 4 aminobenzenesulfonamide Synonymes …   Wikipédia en Français List of EC numbers (EC 2) — This list contains a list of EC numbers for the second group, EC 2, transferases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 2.1: Transferring One… …   Wikipedia Metabolism — Cell metabolism redirects here. For the journal, see Cell Metabolism. Structure of adenosine triphosphate, a central intermediate in energy metabolism Metabolism (from Greek: μεταβολή metabolē , change or Greek: μεταβολισμός metabolismos,… …   Wikipedia Dihydrofolate reductase — Ribbon diagram of human dihydrofolate reductase in complex with folate (blue). From PDB 1DRF …   Wikipedia Methionine adenosyltransferase — I, alpha Identifiers Symbol MAT1A Entrez 4143 HUGO …   Wikipedia Methylenetetrahydrofolate reductase — methylene tetrahydrofolate reductase [NAD(P)H] Ribbon diagram of the active site of E. coli MTHFR. The flavin cofactor (top) is shown interacting with the bound substrate NADH.[1] …   Wikipedia PCBD1 — Pterin 4 alpha carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor 1 alpha PDB rendering based on 1dch …   Wikipedia Pantothenate kinase — (PanK; CoaA) is the first enzyme in the Coenzyme A biosynthetic pathway. It phophorylates pantothenate (vitamin B5) to form 4 phosphopantothenate. Types Three distinct types of PanK has been identified PanK I (found in bacteria), PanK II (mainly… …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”