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Literature summary for 5.1.99.8 extracted from
- Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase (2007), J. Mol. Biol., 368, 161-169.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with neopterin, an analog of dihydroneopterin, and with monapterin, to 1.7 A and 1.68 A resolution, respectively. Active site residues E22, K100, and Y54 function coordinately during catalysis | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| monapterin | - |
Staphylococcus aureus |  |
| neopterin | - |
Staphylococcus aureus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | P56740 | bifunctional epimerase and aldolase, EC 4.1.2.25 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 7,8-dihydroneopterin | - |
Staphylococcus aureus | 7,8-dihydromonapterin | - |
? | |
| additional information | enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, reaction of EC 4.1.2.25, and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin | Staphylococcus aureus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FolB | - |
Staphylococcus aureus |
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Release 2023.1 (January 2023)
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