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Literature summary extracted from

  • Vyas, N.K.; Nickitenko, A.; Rastogi, V.K.; Shah, S.S.; Quiocho, F.A.
    Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase (2010), Biochemistry, 49, 547-559.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.8.2 purified OPAA, in acetate buffer equilibrated in a reservoir solution containing a much greater concentration of acetate, 270 mM ammonium acetate and 60 mM sodium acetate, pH 4.6, X-ray structure determination and analysis at 2.7 A resolution for the enzyme with bound inhibitor N,N'-diisopropyldiamidophosphate, and at 2.3 A resolution for the native enzyme Alteromonas sp.
3.4.13.9 purified enzyme, hanging drop method, mixing of 0.002 ml of protein solution containing 10 mg/ml protein in 1 mM 2-mercaptoethanol, 0.1 mM MnCl2, and 10 mM Tris-HCl, pH 7.2, with 0.002 ml of reservoir solution containing 16% PEG 4000, 20 mM MnCl2, 1 mM 2-mercaptoethanol, 270 mM ammonium acetate, and 60 mM sodium acetate, pH 4.6, at 20°C, 2-4 days, X-ray diffraction structure determination and analysis Alteromonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.8.2 N,N'-diisopropyldiamidofluorophosphate i.e. mipafox or DDFP. the inhibitor's hydrolysis product, N,N'-diisopropyldiamidophosphate, is present in the cocrystal structure and bound by coordinating the binuclear metals and forming hydrogen bonds and nonpolar interactions with active site residues. An unusual common feature of the binding of the two ligands is the involvement of only one oxygen atom of the glycolate carboxylate and the product DDP tetrahedral phosphate in bridging the two Mn2+ ions, binding structure analysis, detailed overview Alteromonas sp.
3.4.13.9 N,N'-diisopropyldiamidofluorophosphate i.e. DDFP or mipafox Alteromonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.8.2 Mn2+ the active site harbors the binuclear Mn2+ ions, three glycolate oxygens of the enzyme coordinate the two Mn2+ atoms. All the oxygens of the carboxylate side chains coordinate the Mn2+ ions in the more favorable syn configuration, binding structure analysis, detailed overview Alteromonas sp.
3.4.13.9 Mn2+ the enzyme harbors binuclear Mn2+ ions within the active site Alteromonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.8.2 58000
-
 x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain Alteromonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Alteromonas sp. Q44238
-
-
3.1.8.2 Alteromonas sp. JD6.5 Q44238
-
-
3.4.13.9 Alteromonas sp.
-
-
-
3.4.13.9 Alteromonas sp. JD6.5
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Alteromonas sp. diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Alteromonas sp. JD6.5 diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Alteromonas sp. O-isopropylmethylphosphate + fluoride
-
 ?
3.1.8.2 O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Alteromonas sp. JD6.5 O-isopropylmethylphosphate + fluoride
-
 ?
3.1.8.2 O-pinacolyl methylphosphonofluoridate + H2O i.e. soman Alteromonas sp. O-pinacolyl methylphosphate + fluoride
-
 ?
3.1.8.2 O-pinacolyl methylphosphonofluoridate + H2O i.e. soman Alteromonas sp. JD6.5 O-pinacolyl methylphosphate + fluoride
-
 ?
3.4.13.9 additional information the bifunctional enzyme is active on the nerve agent organophosphate substrate diisopropyl fluorophosphate, DFP, producing N,N'-diisopropyldiamidophosphate, binding structure modelling, overview Alteromonas sp. ?
-
 ?
3.4.13.9 additional information the bifunctional enzyme is active on the nerve agent organophosphate substrate diisopropyl fluorophosphate, DFP, producing N,N'-diisopropyldiamidophosphate, binding structure modelling, overview Alteromonas sp. JD6.5 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.8.2 ? x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain Alteromonas sp.
3.4.13.9 More The OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions Alteromonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.1.8.2 OPAA
-
 Alteromonas sp.
3.1.8.2 organophosphate anhydrolase/prolidase
-
 Alteromonas sp.
3.4.13.9 OPAA
-
 Alteromonas sp.
3.4.13.9 organophosphate acid anhydrolase
-
 Alteromonas sp.
3.4.13.9 organophosphate anhydrolase/prolidase
-
 Alteromonas sp.
3.4.13.9 prolidase
-
 Alteromonas sp.

General Information

EC Number General Information Comment Organism
3.1.8.2 additional information the OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions. The native enzyme structure reveals the presence of a well-defined nonproteinaceous density in the active site, which might be due to a bound glycolate, which is isosteric with a glycine product. All three glycolate oxygens coordinate the two Mn2+ atoms Alteromonas sp.