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Literature summary for 3.1.8.2 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
Search for more literature for 3.1.8.2

Crystallization (Commentary)

Crystallization (Comment) Organism
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.

Inhibitors

Inhibitors Comment Organism Structure
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.

Metals/Ions

Metals/Ions Comment Organism Structure
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.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

Organism UniProt Comment Textmining
Alteromonas sp. Q44238
-
-
Alteromonas sp. JD6.5 Q44238
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diisopropyl fluorophosphate + H2O
-
 Alteromonas sp. diisopropyl phosphate + fluoride
-
 ?
diisopropyl fluorophosphate + H2O
-
 Alteromonas sp. JD6.5 diisopropyl phosphate + fluoride
-
 ?
O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Alteromonas sp. O-isopropylmethylphosphate + fluoride
-
 ?
O-isopropylmethylphosphonofluoridate + H2O i.e. sarin Alteromonas sp. JD6.5 O-isopropylmethylphosphate + fluoride
-
 ?
O-pinacolyl methylphosphonofluoridate + H2O i.e. soman Alteromonas sp. O-pinacolyl methylphosphate + fluoride
-
 ?
O-pinacolyl methylphosphonofluoridate + H2O i.e. soman Alteromonas sp. JD6.5 O-pinacolyl methylphosphate + fluoride
-
 ?

Subunits

Subunits Comment Organism
? 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.

Synonyms

Synonyms Comment Organism
OPAA
-
 Alteromonas sp.
organophosphate anhydrolase/prolidase
-
 Alteromonas sp.

General Information

General Information Comment Organism
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.