Literature summary for 3.1.8.1 extracted from

Zhang, L.; Wang, H.; Liu, X.; Zhou, W.; Rao, Z.
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)

Cloned (Comment)	Organism
recombinant expression of N-terminally His6-tagged enzyme	Mycobacterium tuberculosis

Crystallization (Commentary)

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

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 [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Mycobacterium tuberculosis

Metals/Ions

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
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

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WHN9	-	-
Mycobacterium tuberculosis ATCC 25618	P9WHN9	-	-
Mycobacterium tuberculosis H37Rv	P9WHN9	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His6-tagged enzyme	Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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

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

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 [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Mycobacterium tuberculosis

General Information

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