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Literature summary for 2.7.1.25 extracted from
- Adenosine-5-phosphosulfate kinase from Escherichia coli K12. Purification, characterization, and identification of a phosphorylated enzyme intermediate (1989), J. Biol. Chem., 264, 15012-15021.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| adenosine 5'-phosphosulfate | - |
Escherichia coli |  |
| ADP | free form, reverse reaction, weak | Escherichia coli | |
| ATP | free form, weak inhibition; MgATP2-: product inhibition, reverse reaction | Escherichia coli | |
| Cd2+ | in excess | Escherichia coli | |
| Co2+ | in excess, activating below | Escherichia coli | |
| EDTA | - |
Escherichia coli | |
| Mn2+ | in excess, activating below | Escherichia coli | |
| additional information | not inhibited by Mg2+ | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic study | Escherichia coli | |
| 0.00025 | - |
adenosine 5'-phosphosulfate | pH 8.0, 25°C | Escherichia coli | |
| 0.01 | - |
ATP | pH 8.0, 25°C | Escherichia coli | |
| 0.13 | - |
ADP | pH 8.0, 25°C | Escherichia coli | |
| 0.13 | - |
ADP | ADP in form of MgADP- | Escherichia coli | |
| 0.37 | - |
3'-phosphoadenosine 5'-phosphosulfate | pH 8.0, 25°C | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | 0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively | Escherichia coli | |
| Co2+ | 0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, inhibitory in excess | Escherichia coli | |
| Mg2+ | 0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, maximal activation of reverse reaction at concentrations that equals the ADP concentration at 0.03 and 0.07 mM | Escherichia coli | |
| Mn2+ | 0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively, inhibitory in excess | Escherichia coli | |
| additional information | no monovalent cations required, stereochemistry of divalent metal ion coordination | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 21000 | - |
2 * 21000, phosphorylated enzyme, SDS-PAGE | Escherichia coli |
| 21000 | - |
4 * 21000, dephosphorylated enzyme, SDS-PAGE | Escherichia coli |
| 40000 | - |
phosphorylated enzyme, gel filtration | Escherichia coli |
| 80000 | - |
dephosphorylated enzyme, gel filtration | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
overproducing K12 strain, JM83/pTL3/pGP1-2 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate, phenyl-Sepharose, Q-Sepharose, Sephacryl S-300, hydroxylapatite, pentyl- agarose, aminohexyl agarose, ATP-agarose | Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate | mechanism | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 153 | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + 3'-phosphoadenylyl sulfate | - |
Escherichia coli | ATP + adenylyl sulfate | - |
r | |
| ATP + adenosine 5-phosphosulfate | no substrates are AMP, forward reaction, and 2'-phosphoadenosine 5'-phosphosulfate, reverse reaction | Escherichia coli | ADP + 3'-phosphoadenosine 5'-phosphosulfate | i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate | r | |
| ATP + adenosine 5-phosphosulfate | i.e. adenylylsulfate or APS | Escherichia coli | ADP + 3'-phosphoadenosine 5'-phosphosulfate | i.e. 3'-phosphoadenylylsulfate or PAPS, via a phosphorylated enzyme intermediate | r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 21000, phosphorylated enzyme, SDS-PAGE | Escherichia coli |
| dimer | native protein undergoes dimer-tetramer interconversions depending on experimental conditions and phosphorylation state | Escherichia coli |
| tetramer | native protein undergoes dimer-tetramer interconversions depending on experimental conditions and phosphorylation state | Escherichia coli |
| tetramer | 4 * 21000, dephosphorylated enzyme, SDS-PAGE | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 50 | - |
adenosine 5-phosphosulfate | pH 8.0, 30°C | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Escherichia coli |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0004 | - |
adenosine 5'-phosphosulfate | pH 8.0, 25°C | Escherichia coli | |
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