Cloned (Comment) | Organism |
---|---|
recombinant expression of N-terminally His6-tagged enzyme | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | architecture of active pocket of enzyme mPHP coordinates with two metal ions | Mycobacterium tuberculosis | |
Zn2+ | activates, required | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
diethyl-paraoxon + H2O | Mycobacterium tuberculosis | - |
diethyl phosphate + 4-nitrophenol | - |
? | |
diethyl-paraoxon + H2O | Mycobacterium tuberculosis H37Rv | - |
diethyl phosphate + 4-nitrophenol | - |
? | |
diethyl-paraoxon + H2O | Mycobacterium tuberculosis ATCC 25618 | - |
diethyl phosphate + 4-nitrophenol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WHN9 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WHN9 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WHN9 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His6-tagged enzyme | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
diethyl-paraoxon + H2O | - |
Mycobacterium tuberculosis | diethyl phosphate + 4-nitrophenol | - |
? | |
diethyl-paraoxon + H2O | - |
Mycobacterium tuberculosis H37Rv | diethyl phosphate + 4-nitrophenol | - |
? | |
diethyl-paraoxon + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | diethyl phosphate + 4-nitrophenol | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 |
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 | Comment | Organism |
---|---|---|
mPHP | - |
Mycobacterium tuberculosis |
phosphotriesterase | - |
Mycobacterium tuberculosis |
phosphotriesterase homology protein | UniProt | Mycobacterium tuberculosis |
PHP | - |
Mycobacterium tuberculosis |
PTE | - |
Mycobacterium tuberculosis |
Rv0230c | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
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 |
additional information | the architecture of active pocket of enzyme mPHP coordinates with two metal ions, substrate binding structure, structre comparisons, overview | Mycobacterium tuberculosis |