S00231
type: Enzyme
rlcp: p1250
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/3.1.8.1
csa: 1ez2
macie: M0159
uniprot: P0A433
uniprot: P0A434
kegg enzyme: aryldialkylphosphatase
kegg enzyme: organophosphate hydrolase
kegg enzyme: paraoxonase
kegg enzyme: A-esterase
kegg enzyme: aryltriphosphatase
kegg enzyme: organophosphate esterase
kegg enzyme: esterase B1
kegg enzyme: esterase E4
kegg enzyme: paraoxon esterase
kegg enzyme: pirimiphos-methyloxon esterase
kegg pathway: gamma-Hexachlorocyclohexane degradation
kegg cofactor: Zinc
kegg substrate: Aryl dialkyl phosphate
kegg substrate: H2O
kegg product: Dialkyl phosphate
kegg product: Phenol
pdb: 1dpmA
pdb: 1dpmB
pdb: 1eywA
pdb: 1ez2A
pdb: 1ez2B
pdb: 1hzyA
pdb: 1hzyB
pdb: 1i03A
pdb: 1i03B
pdb: 1i0bA
pdb: 1i0bB
pdb: 1i0dA
pdb: 1i0dB
pdb: 1jgmA
pdb: 1jgmB
pdb: 1p6bA
pdb: 1p6bB
pdb: 1p6cA
pdb: 1p6cB
pdb: 1pscA
pdb: 1pscB
pdb: 1ptaA
active site residues resources: Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase.
active site residues resources: Structural determinants of the substrate and stereochemical specificity of phosphotriesterase.
active site residues resources: 1psc
active site residues resources: 1p6b
references: Chemical and kinetic evidence for an essential histidine in the phosphotriesterase from Pseudomonas diminuta.
references: Structural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR spectroscopy.
references: Characterization of the zinc binding site of bacterial phosphotriesterase.
references: Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents.
references: Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis.
references: Utilization of copper as a paramagnetic probe for the binuclear metal center of phosphotriesterase.
references: Histidine-254 is essential for the inactivation of phosphotriesterase with the alkynyl phosphate esters and diethyl pyrocarbonate.
references: Three-dimensional structure of the binuclear metal center of phosphotriesterase.
references: Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase.
references: Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate.
references: Mechanism-based inhibitors for the inactivation of the bacterial phosphotriesterase.
references: Perturbations to the active site of phosphotriesterase.
references: Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase.
references: A combinatorial library for the binuclear metal center of bacterial phosphotriesterase.
references: Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family.
references: Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase.
references: Phosphotriesterase: an enzyme in search of its natural substrate.
references: Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX.
references: The binding of substrate analogs to phosphotriesterase.
references: High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta.
references: Structural determinants of the substrate and stereochemical specificity of phosphotriesterase.
references: Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.
references: Mobility of the active site bound paraoxon and sarin in zinc-phosphotriesterase by molecular dynamics simulation and quantum chemical calculation.
references: Ab initio structure of the active site of phosphotriesterase.
references: Successful molecular dynamics simulation of two zinc complexes bridged by a hydroxide in phosphotriesterase using the cationic dummy atom method.
references: Enzymatic synthesis of chiral organophosphothioates from prochiral precursors.
references: Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site.
references: Coordination number of zinc ions in the phosphotriesterase active site by molecular dynamics and quantum mechanics.
references: Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.
comment: This enzyme is activated in vitro by the addition of carbon dioxide, which carbamates the sidechain of Lys169, according to the literature [12]. This modified lysine residue is essential to bridge the two metal cofactors. Although early work (literature [1] & [4]) suggested that a general base to activate a water molecule, the water can be activated by the metal cofactor without any general base, according to the more recent literature ([8], [9], [10], [14]). In any case, the metal cofactors play the following roles (see [9]): (a) They can decrease pKa of th bound wate, increasing its nucleophilicity. (b) They can polarize the P=O bond (or P=S bond), and thereby facilitate the approach of the attacking hydroxyl ion, by increasing the electrophilic character of the phosphoryl core. (c) They can neutralize the development of the negative charge on the leaving group. The most recent literature [20] and structural information suggested that the catalytic reaction of this enzyme proceeds via SN2-like mechanism as follows: (1) Phosphoryl-oxygen bond is polarized by its interaction with zinc-2. (2) A water or hydroxide ion bridging the two zinc ions is activated by the two zinc ions (particulary zinc-1) and Asp301 (as a general base). (3) The activated water makes a nucleophilic attack on the phosphorus atom, releasing the leaving phenol group.

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.140
catalytic domain: index.html

gamma-Hexachlorocyclohexane degradation
type: KeggPathway
references: KEGG:MAP00361

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Aryl dialkyl phosphate
type: KeggSubstrate
references: KEGG:C03254
compound type: aromatic ring (only carbon atom)
compound type: phosphate group/phosphate ion

H2O
type: KeggSubstrate
references: KEGG:C00001
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Dialkyl phosphate
type: KeggProduct
references: KEGG:C02534
compound type: phosphate group/phosphate ion

Phenol
type: KeggProduct
references: KEGG:C15584
compound type: aromatic ring (only carbon atom)
references: CHEBI:15882
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1dpmA
type: Pdb
references: 1dpm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dpm
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 902(carbamylated)
comment: LYS-FMT carbamylated Lys

1dpmB
type: Pdb
references: 1dpm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dpm
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 904(carbamylated)
comment: LYS-FMT carbamylated Lys

1eywA
type: Pdb
references: 1eyw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1eyw
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);KCX 169(Zinc-1 & Zinc-2)
modified residue: KCX 169(carbamylated)
comment: KCX carbamylated Lys

1ez2A
type: Pdb
references: 1ez2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ez2
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);KCX 169(Zinc-1 & Zinc-2)
modified residue: KCX 169(carbamylated)
comment: KCX carbamylated Lys

1ez2B
type: Pdb
references: 1ez2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ez2
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);KCX 169(Zinc-1 & Zinc-2)
modified residue: KCX 169(carbamylated)
comment: KCX carbamylated Lys

1hzyA
type: Pdb
references: 1hzy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hzy
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 369(carbamylated)
comment: LYS-FMT carbamylated Lys169

1hzyB
type: Pdb
references: 1hzy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hzy
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 369(carbamylated)
comment: LYS-FMT carbamylated Lys169

1i03A
type: Pdb
references: 1i03
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i03
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: CBX 369(carbamylated)
comment: LYS-CBX carbamylated Lys169

1i03B
type: Pdb
references: 1i03
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i03
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: CBX 369(carbamylated)
comment: LYS-CBX carbamylated Lys169

1i0bA
type: Pdb
references: 1i0b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0b
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 369(carbamylated)
comment: LYS-FMT carbamylated Lys169

1i0bB
type: Pdb
references: 1i0b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0b
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 369(carbamylated)
comment: LYS-FMT carbamylated Lys169

1i0dA
type: Pdb
references: 1i0d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0d
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 369(carbamylated)
comment: LYS-FMT carbamylated Lys169

1i0dB
type: Pdb
references: 1i0d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0d
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 369(carbamylated)
comment: LYS-FMT carbamylated Lys169

1jgmA
type: Pdb
references: 1jgm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jgm
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);KCX 169(Zinc-1 & Zinc-2)
modified residue: KCX 169(carbamylated)
comment: KCX carbamylated Lys

1jgmB
type: Pdb
references: 1jgm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jgm
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);KCX 169(Zinc-1 & Zinc-2)
modified residue: KCX 169(carbamylated)
comment: KCX carbamylated Lys

1p6bA
type: Pdb
references: 1p6b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p6b
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LCX 169(Zinc-1 & Zinc-2)
modified residue: LCX 169(carbamylated)
comment: LCX carbamylated Lys, mutant H254G, H257W, I303T

1p6bB
type: Pdb
references: 1p6b
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p6b
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LCX 169(Zinc-1 & Zinc-2)
modified residue: LCX 169(carbamylated)
comment: LCX carbamylated Lys, mutant H254G, H257W, I303T

1p6cA
type: Pdb
references: 1p6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p6c
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LCX 169(Zinc-1 & Zinc-2)
modified residue: LCX 169(carbamylated)
comment: LCX carbamylated Lys, mutant H254G, H257W, I303T

1p6cB
type: Pdb
references: 1p6c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1p6c
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LCX 169(Zinc-1 & Zinc-2)
modified residue: LCX 169(carbamylated)
comment: LCX carbamylated Lys, mutant H254G, H257W, I303T

1pscA
type: Pdb
references: 1psc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psc
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 901(carbamylated)
comment: LYS-FMT carbamylated Lys

1pscB
type: Pdb
references: 1psc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psc
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)
modified residue: FMT 902(carbamylated)
comment: LYS-FMT carbamylated Lys

1ptaA
type: Pdb
references: 1pta
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pta
catalytic residue: ASP 301
cofactor binding residue: HIS 55;HIS 57;ASP 301(Zinc-1);HIS 201;HIS 230(Zinc-2);LYS 169(Zinc-1 & Zinc-2)

Chemical and kinetic evidence for an essential histidine in the phosphotriesterase from Pseudomonas diminuta.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2174875
journal: J Biol Chem
volume: 265
pages: 21498-503
published year: 1990
authors:
  item: Dumas DP
  item: Raushel FM

Structural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8396425
journal: Biochemistry
volume: 32
pages: 9148-55
published year: 1993
authors:
  item: Omburo GA
  item: Mullins LS
  item: Raushel FM

Characterization of the zinc binding site of bacterial phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1320014
journal: J Biol Chem
volume: 267
pages: 13278-83
published year: 1992
authors:
  item: Omburo GA
  item: Kuo JM
  item: Mullins LS
  item: Raushel FM

Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 95092756
references: http://www.ncbi.nlm.nih.gov/pubmed/7999757
journal: Biochemistry
volume: 33
pages: 15001-7
published year: 1994
authors:
  item: Benning MM
  item: Kuo JM
  item: Raushel FM
  item: Holden HM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P16648

Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis.
type: BibliographicResource
comment: ACTIVE SITE.
medline id: 94206935
references: http://www.ncbi.nlm.nih.gov/pubmed/8155644
journal: Biochemistry
volume: 33
pages: 4265-72
published year: 1994
authors:
  item: Kuo JM
  item: Raushel FM
references: P16648

Utilization of copper as a paramagnetic probe for the binuclear metal center of phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7864632
journal: Arch Biochem Biophys
volume: 316
pages: 765-72
published year: 1995
authors:
  item: Chae MY
  item: Omburo GA
  item: Lindahl PA
  item: Raushel FM

Histidine-254 is essential for the inactivation of phosphotriesterase with the alkynyl phosphate esters and diethyl pyrocarbonate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7827033
journal: Biochemistry
volume: 34
pages: 750-4
published year: 1995
authors:
  item: Banzon JA
  item: Kuo JM
  item: Fischer DR
  item: Stang PJ
  item: Raushel FM

Three-dimensional structure of the binuclear metal center of phosphotriesterase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 95315185
references: http://www.ncbi.nlm.nih.gov/pubmed/7794910
journal: Biochemistry
volume: 34
pages: 7973-8
published year: 1995
authors:
  item: Benning MM
  item: Kuo JM
  item: Raushel FM
  item: Holden HM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P16648

Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8718883
journal: Biochemistry
volume: 35
pages: 10904-12
published year: 1996
authors:
  item: Hong SB
  item: Raushel FM

Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
medline id: 96214508
references: http://www.ncbi.nlm.nih.gov/pubmed/8634243
journal: Biochemistry
volume: 35
pages: 6020-5
published year: 1996
authors:
  item: Vanhooke JL
  item: Benning MM
  item: Raushel FM
  item: Holden HM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P16648

Mechanism-based inhibitors for the inactivation of the bacterial phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9220990
journal: Biochemistry
volume: 36
pages: 9022-8
published year: 1997
authors:
  item: Hong SB
  item: Mullins LS
  item: Shim H
  item: Raushel FM

Perturbations to the active site of phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9047295
journal: Biochemistry
volume: 36
pages: 1982-8
published year: 1997
authors:
  item: Kuo JM
  item: Chae MY
  item: Raushel FM

Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9325279
journal: J Biol Chem
volume: 272
pages: 25596-601
published year: 1997
authors:
  item: Watkins LM
  item: Mahoney HJ
  item: McCulloch JK
  item: Raushel FM

A combinatorial library for the binuclear metal center of bacterial phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9408951
journal: Proteins
volume: 29
pages: 553-61
published year: 1997
authors:
  item: Watkins LM
  item: Kuo JM
  item: Chen-Goodspeed M
  item: Raushel FM

Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9548740
journal: Biochemistry
volume: 37
pages: 5096-106
published year: 1998
authors:
  item: Buchbinder JL
  item: Stephenson RC
  item: Dresser MJ
  item: Pitera JW
  item: Scanlan TS
  item: Fletterick RJ

Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9651332
journal: J Biol Chem
volume: 273
pages: 17445-50
published year: 1998
authors:
  item: Shim H
  item: Hong SB
  item: Raushel FM

Phosphotriesterase: an enzyme in search of its natural substrate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10800593
journal: Adv Enzymol Relat Areas Mol Biol
volume: 74
pages: 51-93
published year: 2000
authors:
  item: Raushel FM
  item: Holden HM

Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11118318
journal: Biochem Biophys Res Commun
volume: 279
pages: 516-9
published year: 2000
authors:
  item: Gopal S
  item: Rastogi V
  item: Ashman W
  item: Mulbry W

The binding of substrate analogs to phosphotriesterase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10871616
journal: J Biol Chem
volume: 275
pages: 30556-60
published year: 2000
authors:
  item: Benning MM
  item: Hong SB
  item: Raushel FM
  item: Holden HM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11258882
journal: Biochemistry
volume: 40
pages: 2712-22
published year: 2001
authors:
  item: Benning MM
  item: Shim H
  item: Raushel FM
  item: Holden HM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural determinants of the substrate and stereochemical specificity of phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11170459
journal: Biochemistry
volume: 40
pages: 1325-31
published year: 2001
authors:
  item: Chen-Goodspeed M
  item: Sogorb MA
  item: Wu F
  item: Hong SB
  item: Raushel FM

Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11170460
journal: Biochemistry
volume: 40
pages: 1332-9
published year: 2001
authors:
  item: Chen-Goodspeed M
  item: Sogorb MA
  item: Wu F
  item: Raushel FM

Mobility of the active site bound paraoxon and sarin in zinc-phosphotriesterase by molecular dynamics simulation and quantum chemical calculation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11456615
journal: J Am Chem Soc
volume: 123
pages: 817-26
published year: 2001
authors:
  item: Koca J
  item: Zhan CG
  item: Rittenhouse RC
  item: Ornstein RL

Ab initio structure of the active site of phosphotriesterase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11206385
journal: J Chem Inf Comput Sci
volume: 41
pages: 8-17
published year: 2001
authors:
  item: Krauss M

Successful molecular dynamics simulation of two zinc complexes bridged by a hydroxide in phosphotriesterase using the cationic dummy atom method.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11599021
journal: Proteins
volume: 45
pages: 183-9
published year: 2001
authors:
  item: Pang YP

Enzymatic synthesis of chiral organophosphothioates from prochiral precursors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11929226
journal: J Am Chem Soc
volume: 124
pages: 3498-9
published year: 2002
authors:
  item: Li WS
  item: Li Y
  item: Hill CM
  item: Lum KT
  item: Raushel FM

Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/15369336
journal: J Am Chem Soc
volume: 125
pages: 8990-1
published year: 2003
authors:
  item: Hill CM
  item: Li WS
  item: Thoden JB
  item: Holden HM
  item: Raushel FM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Coordination number of zinc ions in the phosphotriesterase active site by molecular dynamics and quantum mechanics.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12548728
journal: J Comput Chem
volume: 24
pages: 368-78
published year: 2003
authors:
  item: Koca J
  item: Zhan CG
  item: Rittenhouse RC
  item: Ornstein RL

Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15018612
journal: Biochem J
volume: 380
pages: 627-33
published year: 2004
authors:
  item: Rochu D
  item: Viguie N
  item: Renault F
  item: Crouzier D
  item: Froment MT
  item: Masson P

OPA anhydrase
type: KeggEnzyme

organophosphorus hydrolase
type: KeggEnzyme

phosphotriesterase
type: KeggEnzyme

paraoxon hydrolase
type: KeggEnzyme

OPH
type: KeggEnzyme

organophosphorus acid anhydrase
type: KeggEnzyme

Analogue
compound: Aryl dialkyl phosphate
pdb: 1dpmA
ligand het code: EBP_900

Analogue
compound: Aryl dialkyl phosphate
pdb: 1dpmB
ligand het code: EBP_902

Analogue
compound: Aryl dialkyl phosphate
pdb: 1eywA
ligand het code: TEN

Analogue
compound: Aryl dialkyl phosphate
pdb: 1ez2A
ligand het code: DII

Analogue
compound: Aryl dialkyl phosphate
pdb: 1ez2B
ligand het code: DII

Analogue
compound: Aryl dialkyl phosphate
pdb: 1p6cA
ligand het code: DII

Analogue
compound: Aryl dialkyl phosphate
pdb: 1p6cB
ligand het code: DII

Analogue
compound: Zinc
pdb: 1i03A
ligand het code: 2x_CD

Analogue
compound: Zinc
pdb: 1i03B
ligand het code: 2x_CD

Analogue
compound: Zinc
pdb: 1i0bA
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1i0bB
ligand het code: 2x_MN

Analogue
compound: Zinc
pdb: 1i0dA
ligand het code: _ZN, _CD

Analogue
compound: Zinc
pdb: 1i0dB
ligand het code: _ZN, _CD

Analogue
compound: Zinc
pdb: 1jgmA
ligand het code: 2x_CD

Analogue
compound: Zinc
pdb: 1jgmB
ligand het code: 2x_CD

Analogue
compound: Zinc
pdb: 1pscA
ligand het code: 2x_CD

Analogue
compound: Zinc
pdb: 1pscB
ligand het code: 2x_CD

Analogue
compound: Dialkyl phosphate
pdb: 1p6bB
ligand het code: EFS

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.6, p.21502

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.9154

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.15005

ReferenceForCatalyticMechanism
reference index: 8
reference section: p.7978

ReferenceForCatalyticMechanism
reference index: 9
reference section: Fig.3, p.10908-10911

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.6, p.6024-6025

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.1982

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.6, p.17450

ReferenceForCatalyticMechanism
reference index: 17
reference section: Scheme 12,p.87-88

ReferenceForCatalyticMechanism
reference index: 20
reference section: p.2722