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Literature summary for 2.5.1.15 extracted from

  • Yun, M.; Wu, Y.; Li, Z.; Zhao, Y.; Waddell, M.; Ferreira, A.; Lee, R.; Bashford, D.; White, S.
    Catalysis and sulfa drug resistance in dihydropteroate synthase (2012), Science, 335, 1110-1114.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.15

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-structure and structure of the complex with pteroate, analysis, overview Yersinia pestis

Inhibitors

Inhibitors Comment Organism Structure
additional information structural, computational and mutagenesis studies on the catalytic and resistance mechanisms of DHPS with sulfonamide antibiotics, overview Bacillus anthracis
additional information structural, computational and mutagenesis studies on the catalytic and resistance mechanisms of DHPS with sulfonamide antibiotics, overview Yersinia pestis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate Yersinia pestis
-
 diphosphate + 7,8-dihydropteroate
-
 ?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate Bacillus anthracis
-
 diphosphate + 7,8-dihydropteroate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
-
-
Yersinia pestis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + 7,8-dihydropteroate SN1 reaction mechanism via formation of a novel cationic pterin intermediate, quantum chemical modelling of the initial step, overview. Two conserved loops generate a substructure during catalysis that creates a specific binding pocket for 4-aminobenzoic acid, one of the two DHPS substrates. The carboxylate moiety of 4-aminobenzoic acid is accommodated by Ser221 and the helix dipole of helix alphaLoop7 Yersinia pestis
a
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + 7,8-dihydropteroate SN1 reaction mechanism via formation of a novel cationic pterin intermediate, quantum chemical modelling of the initial step, overview. Two conserved loops generate a substructure during catalysis that creates a specific binding pocket for 4-aminobenzoic acid, one of the two DHPS substrates. The carboxylate moiety of 4-aminobenzoic acid is accommodated by Ser221 and the helix dipole of helix alphaLoop7 Bacillus anthracis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
-
 Yersinia pestis diphosphate + 7,8-dihydropteroate
-
 ?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
-
 Bacillus anthracis diphosphate + 7,8-dihydropteroate
-
 ?

Synonyms

Synonyms Comment Organism
DHPS
-
 Yersinia pestis
DHPS
-
 Bacillus anthracis

General Information

General Information Comment Organism
evolution dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes Yersinia pestis
evolution dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes Bacillus anthracis
metabolism dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes Yersinia pestis
metabolism dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes Bacillus anthracis