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Literature summary extracted from
- The crystal structure of the phosphotriesterase from M. tuberculosis, another member of phosphotriesterase-like lactonase family (2019), Biochem. Biophys. Res. Commun., 510, 224-229 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.8.1 | recombinant expression of N-terminally His6-tagged enzyme | Mycobacterium tuberculosis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.8.1 | purified recombinant N-terminally His6-tagged enzyme with bound Zn2+, X-ray diffraction structure determination and analysis at 2.3 A resolution, the first residue of the N-terminal (Met1) and the last residue of the C-terminal (Gln326) are missing due to the lack of density. Molecular replacement, the structure of phosphotriesterase from Sulfolobus solfataricus (SsoPox), PDB ID 2VC5, is used as the search model | Mycobacterium tuberculosis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.8.1 | additional information | - |
additional information | Michaelis-Menten kinetics | Mycobacterium tuberculosis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.8.1 | additional information | architecture of active pocket of enzyme mPHP coordinates with two metal ions | Mycobacterium tuberculosis | |
| 3.1.8.1 | Zn2+ | activates, required | Mycobacterium tuberculosis |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.8.1 | diethyl-paraoxon + H2O | Mycobacterium tuberculosis | - |
diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.1 | diethyl-paraoxon + H2O | Mycobacterium tuberculosis H37Rv | - |
diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.1 | diethyl-paraoxon + H2O | Mycobacterium tuberculosis ATCC 25618 | - |
diethyl phosphate + 4-nitrophenol | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.8.1 | Mycobacterium tuberculosis | P9WHN9 | - |
- |
| 3.1.8.1 | Mycobacterium tuberculosis ATCC 25618 | P9WHN9 | - |
- |
| 3.1.8.1 | Mycobacterium tuberculosis H37Rv | P9WHN9 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.8.1 | recombinant N-terminally His6-tagged enzyme | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.8.1 | diethyl-paraoxon + H2O | - |
Mycobacterium tuberculosis | diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.1 | diethyl-paraoxon + H2O | - |
Mycobacterium tuberculosis H37Rv | diethyl phosphate + 4-nitrophenol | - |
? | |
| 3.1.8.1 | diethyl-paraoxon + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | diethyl phosphate + 4-nitrophenol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.8.1 | dimer | enzyme mPHP is a dimer with a typical distorted (beta/alpha)8 barrel structure like other structures of PLL family and PTE family | Mycobacterium tuberculosis |
| 3.1.8.1 | More | the monomeric mPHP is a distorted (beta/alpha)8 barrel. The eight beta-strands (beta3-beta10) form the inner barrel wall which surrounds the substrate binding pocket. The eight alpha-helices are roughly parallel to each other and form a twist barrel outside the inner beta barrel, secondary structure analysis, structure comparisons, overview | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.8.1 | mPHP | - |
Mycobacterium tuberculosis |
| 3.1.8.1 | phosphotriesterase | - |
Mycobacterium tuberculosis |
| 3.1.8.1 | phosphotriesterase homology protein | UniProt | Mycobacterium tuberculosis |
| 3.1.8.1 | PHP | - |
Mycobacterium tuberculosis |
| 3.1.8.1 | PTE | - |
Mycobacterium tuberculosis |
| 3.1.8.1 | Rv0230c | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.8.1 | 25 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.8.1 | 8 | - |
assay at | Mycobacterium tuberculosis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.8.1 | evolution | the enzyme is a member of phosphotriesterase-like lactonase family. The phosphotriesterase activities of phosphotriesterases (PTEs) are considered to derive from the lactonase-activities during the evolution, and phosphotriesterase-like lactonase family (PLL), is the closest protein family to PTE family based on protein-protein blast results. But members of PLL family exhibit higher lactonase activities than the phosphotriesterase activities, while the best substrates for PTEs are phosphotriesters. Enzyme mPHP is a dimer with a typical distorted (beta/alpha)8 barrel structure like other structures of PLL family and PTE family | Mycobacterium tuberculosis |
| 3.1.8.1 | additional information | the architecture of active pocket of enzyme mPHP coordinates with two metal ions, substrate binding structure, structre comparisons, overview | Mycobacterium tuberculosis |
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