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Literature summary extracted from
- Intermediates in the transformation of phosphonates to phosphate by bacteria (2011), Nature, 480, 570-573.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.7.8.37 | GST fusion proteins of PhnI and PhnL expressed in Escherichia coli BL21(DE3), His-tagged PhnG and PhnH expressed in Escherichia coli BL21(DE3) | Escherichia coli |
| 3.6.1.63 | expressed in Escherichia coli | Escherichia coli |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.7.8.37 | Mg2+ | - |
Escherichia coli |  |
| 3.6.1.63 | Mg2+ | - |
Escherichia coli | |
| 3.6.1.63 | Zn2+ | - |
Escherichia coli | |
| 4.7.1.1 | Iron | enzyme binds 2.2 equivalents of iron per monomer | Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.7.8.37 | Escherichia coli | - |
- |
- |
| 3.6.1.63 | Escherichia coli | - |
- |
- |
| 4.7.1.1 | Escherichia coli | - |
- |
- |
| 4.7.1.1 | Escherichia coli | P16688 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.7.8.37 | GST fusion proteins: GSTrap column, His-tagged proteins: HisTrap column | Escherichia coli |
| 3.6.1.63 | purified using gel filtration with a High Load Superdex 200 26/60 prep grade column followed by anion exchange chromatography | Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.6.1.63 | alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O = alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate | when the hydrolysis reaction of D-ribose-5-triphosphate catalyzed by PhnM is conducted in oxygen-18 labeled water, the oxygen-18 is found exclusively in D-ribose-5-phosphate and not in diphosphate. Therefore, water attacks the alpha-phosphoryl group of D-ribose-5-triphosphate rather than the beta-phosphoryl group | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.7.8.37 | ATP + H2O | - |
Escherichia coli | adenine + D-ribose-5-triphosphate | - |
? | |
| 2.7.8.37 | ATP + methylphosphonate | - |
Escherichia coli | adenine + alpha-D-ribose-1-methylphosphonate-5-triphosphate | - |
? | |
| 2.7.8.37 | GTP + H2O | - |
Escherichia coli | guanine + D-ribose-5-triphosphate | - |
? | |
| 3.6.1.63 | alpha-D-ribose 1-methylphosphonate 5-triphosphate + H2O | - |
Escherichia coli | alpha-D-ribose 1-methylphosphonate 5-phosphate + diphosphate | - |
? | |
| 3.6.1.63 | D-ribose 5-diphosphate + H2O | - |
Escherichia coli | D-ribose 5-phosphate + phosphate | - |
? | |
| 3.6.1.63 | D-ribose 5-triphosphate + H2O | - |
Escherichia coli | D-ribose 5-phosphate + phosphate | - |
? | |
| 4.7.1.1 | alpha-D-ribose 1-methylphosphonate 5-phosphate | the carbon-phosphorus bond of the substrate is cleaved via a radical-based reaction to alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate and methane in the presence of S-adenosyl-L-methionine. Enzyme additionally requires S-adenosyl-L-methionine | Escherichia coli | alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate + methane | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.7.8.37 | PhnI | in the presence of PhnG, PhnH and PhnL | Escherichia coli |
| 3.6.1.63 | phnM | - |
Escherichia coli |
| 4.7.1.1 | phnJ | - |
Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.63 | 8.5 | - |
assay at | Escherichia coli |
| 4.7.1.1 | 6.8 | - |
assay at | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.7.1.1 | S-adenosyl-L-methionine | - |
Escherichia coli | |
| 4.7.1.1 | [4Fe-4S]-center | enzyme shows a absorption band centered at 403 nm and has a reddish-brown colour. The absorption band disappears upon addition of 1 mM dithionite | Escherichia coli | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.7.1.1 | physiological function | deletion of the enzyme gene from Escherichia coli leads to the detection of alpha-D-ribose 1-methylphosphonate in the growth medium. alpha-D-Ribose 1-methylphosphonate is the ultimate substrate for the actual C-P lyase reaction | Escherichia coli |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.7.8.37 | 13 | - |
ATP | PhnI, nucleosidase activity, pH not specified in the publication, temperature not specified in the publication | Escherichia coli | |
| 2.7.8.37 | 83 | - |
GTP | PhnI, nucleosidase activity, pH not specified in the publication, temperature not specified in the publication | Escherichia coli | |
| 2.7.8.37 | 340 | - |
GTP | PhnI, PhnG, PhnH and PhnL, GST tags in situ removed, proteins begin to precipitate after removal of the GST tags, therefore kinetic constants are not definitive, pH not specified in the publication, temperature not specified in the publication | Escherichia coli | |
| 2.7.8.37 | 350 | - |
ATP | PhnI, PhnG, PhnH and PhnL, GST tags in situ removed, proteins begin to precipitate after removal of the GST tags, therefore kinetic constants are not definitive, pH not specified in the publication, temperature not specified in the publication | Escherichia coli | |
| 3.6.1.63 | 110 | - |
alpha-D-ribose 1-methylphosphonate 5-triphosphate | pH 8.5, temperature not specified in the publication | Escherichia coli | |
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