Any feedback?
Literature summary for 1.1.1.405 extracted from
- Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of the reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus (2004), Biochemistry, 43, 11802-11812.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of TarI and TarJ individually from their respective genes using the T7 expression system | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide | - |
Haemophilus influenzae |  |
| 2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide | - |
Staphylococcus aureus | |
| D-ribitol 5-phosphate | - |
Haemophilus influenzae | |
| D-ribitol 5-phosphate | - |
Staphylococcus aureus | |
| NADP+ | competitive versus NADPH | Haemophilus influenzae | |
| NADP+ | competitive versus NADPH | Staphylococcus aureus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00674 | - |
NADPH | - |
Staphylococcus aureus | |
| 0.00706 | - |
NADPH | - |
Haemophilus influenzae | |
| 0.0285 | - |
ribulose 5-phosphate | - |
Staphylococcus aureus | |
| 0.106 | - |
ribulose 5-phosphate | - |
Haemophilus influenzae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 26000 | - |
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE | Staphylococcus aureus |
| 41000 | - |
2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE | Staphylococcus aureus |
| 53190 | - |
2 * 53190, calculation from amino acid composition | Haemophilus influenzae |
| 106400 | - |
amino acid composition | Haemophilus influenzae |
| 129000 | - |
calculation from gel filtration and sedimentation velocity data | Staphylococcus aureus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haemophilus influenzae | - |
- |
- |
| Staphylococcus aureus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Staphylococcus aureus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-ribulose 5-phosphate + NADPH + H+ | tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex. Release and free diffusion of the intermediate ribitol 5-phosphate without channelling between active sites, ordered bi-bi mechanism | Staphylococcus aureus | D-ribitol 5-phosphate + NADP+ | - |
? | |
| D-ribulose 5-phosphate + NADPH + H+ | the data suggest that NADPH binds first and ribulose 5-phosphate binds second. Bifunction enzyme catalyzing the reactions of EC 1.1.1.137 and EC 2.7.7.40, ordered bi-bi mechanism | Haemophilus influenzae | D-ribitol 5-phosphate + NADP+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | 2 * 26000 + 2 * 41000, tarI encodes an orthologue of the cytidylyltransferase domain of Bcs1 from Haemophilus influenzae and tarJ encodes an analogue of the reductase domain of Bcs1, TarI and TyrJ form a functional CDP-ribitol synthase complex, SDS-PAGE | Staphylococcus aureus |
| dimer | 2 * 53190, calculation from amino acid composition | Haemophilus influenzae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bcs1 | - |
Haemophilus influenzae |
| TarIJ | - |
Staphylococcus aureus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03 | 0.55 | NADPH | - |
Haemophilus influenzae | |
| 0.79 | - |
NADPH | - |
Staphylococcus aureus | |
| 6.08 | - |
NADPH | - |
Staphylococcus aureus | |
| 7.41 | - |
NADPH | - |
Haemophilus influenzae | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide | Ki(intercept) and Ki(slope)-values | Staphylococcus aureus | |
| additional information | - |
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide | Ki(intercept) and Ki(slope)-values | Haemophilus influenzae | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
