3l24

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Template:STRUCTURE 3l24

Contents

Crystal Structure of the Nerve Agent Degrading Organophosphate Anhydrolase/Prolidase in Complex with Inhibitors

Template:ABSTRACT PUBMED 20000741

Function

[PEPQ_ALTSX] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position and a nonpolar amino acid at the N-terminal position. Also catalyzes the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds including insecticide paraoxon and nerve gases such as diisopropylfluorophosphate (DFP), O-isopropyl methylphosphonofluoridate (sarin), O-pinacolyl methylphosphonofluoridate (soman), and O-cyclohexyl methylphosphonofluoridate.[1] [2] [3] [4]

About this Structure

3l24 is a 3 chain structure with sequence from Alteromonas sp.. Full crystallographic information is available from OCA.

Reference

  • Vyas NK, Nickitenko A, Rastogi VK, Shah SS, Quiocho FA. Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase. Biochemistry. 2010 Jan 26;49(3):547-59. PMID:20000741 doi:10.1021/bi9011989
  1. Cheng TC, Harvey SP, Chen GL. Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme. Appl Environ Microbiol. 1996 May;62(5):1636-41. PMID:8633861
  2. DeFrank JJ, Cheng TC. Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate. J Bacteriol. 1991 Mar;173(6):1938-43. PMID:2001997
  3. Cheng T, Liu L, Wang B, Wu J, DeFrank JJ, Anderson DM, Rastogi VK, Hamilton AB. Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis. J Ind Microbiol Biotechnol. 1997 Jan;18(1):49-55. PMID:9079288
  4. Hill CM, Wu F, Cheng TC, DeFrank JJ, Raushel FM. Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters. Bioorg Med Chem Lett. 2000 Jun 5;10(11):1285-8. PMID:10866401

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