EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.15 | apo-structure and structure of the complex with pteroate, analysis, overview | Yersinia pestis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.15 | additional information | structural, computational and mutagenesis studies on the catalytic and resistance mechanisms of DHPS with sulfonamide antibiotics, overview | Bacillus anthracis | |
2.5.1.15 | additional information | structural, computational and mutagenesis studies on the catalytic and resistance mechanisms of DHPS with sulfonamide antibiotics, overview | Yersinia pestis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.15 | (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate | Yersinia pestis | - |
diphosphate + 7,8-dihydropteroate | - |
? | |
2.5.1.15 | (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate | Bacillus anthracis | - |
diphosphate + 7,8-dihydropteroate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.15 | Bacillus anthracis | - |
- |
- |
2.5.1.15 | Yersinia pestis | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.5.1.15 | (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 | |
2.5.1.15 | (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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.15 | (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate | - |
Yersinia pestis | diphosphate + 7,8-dihydropteroate | - |
? | |
2.5.1.15 | (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate | - |
Bacillus anthracis | diphosphate + 7,8-dihydropteroate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.15 | DHPS | - |
Yersinia pestis |
2.5.1.15 | DHPS | - |
Bacillus anthracis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.15 | evolution | dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes | Yersinia pestis |
2.5.1.15 | evolution | dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes | Bacillus anthracis |
2.5.1.15 | metabolism | dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes | Yersinia pestis |
2.5.1.15 | metabolism | dihydropteroate synthase is a key enzyme in the folate pathway of bacteria and primitive eukaryotes | Bacillus anthracis |