Biotechnology and Bioprocess Engineering:BBE

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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Expression and Characterization of Escherichia coli Prolidase with Organophosphorus Compounds

  • Hong, Jin-Kyu (EM Industrial Corporation) ;
  • Park, Min-Sun (Department of chemistry, Texas A&M University) ;
  • Frank M. Raushel (Department of chemistry, Texas A&M University) ;
  • Khang, Yong-Ho (Department of Applied Microbiology, Yeungnam University)
  • Published : 2003.04.01
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Abstract

A relatively high homology between Escherichia coli prolidase and Alteromonas organophosphorous acid anhydrolase suggests that E. coli prolidase may have an activity to d egrade toxic organophosphorous compounds. To confirm this suggestion, we cloned and expressed a prolidase gene (pepQ) of E. coliBL2l. The recombinant E. coli prolidase that consisted of 443 amino acid residues exhibited activity and stereochemical selectivity against organopho sphorous compounds, although its activity was two to three orders of magnitude less than that of the other organophosphorous acid hydrolase isolated from Pseudomonas diminuta.

Keywords

References

  1. Appl. Environ. Microb. v.62 Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme Cheng,T.C.;S.P.Harvey;G.L.Chen
  2. Biotechnol. Bioeng. v.63 Detoxification of organophosphate nerve agents by immo-bilized Escherichia coli with surface-expressed organophosphorus hydrolase Mulchandani,A.;I.Kaneva;W.Chen https://doi.org/10.1002/(SICI)1097-0290(19990420)63:2<216::AID-BIT10>3.0.CO;2-0
  3. Biotechnol. Bioeng. v.70 Degradation of organophosphorous nerve agents by enzyme-polymer nanocomposites: efficient biocatalytic materials for personal protection and large-scale detoxification Gill,I.;A.Ballesteros https://doi.org/10.1002/1097-0290(20001120)70:4<400::AID-BIT5>3.0.CO;2-2
  4. Curr. Opin. Microbiol. v.5 Bacterial detoxification of organophosphate nerve agents Raushel,F.M. https://doi.org/10.1016/S1369-5274(02)00314-4
  5. Appl. Environ. Microbiol. v.51 Identification of a plasmid-borne parathion hydrolase gene from Flavobac-terium sp. by southern hybridization with opd from Pseudomonas diminuta Mulbry,W.;J.S.Karns;P.C.Kearney;J.O.Nelson;C.S.McDaniel;J.R.Wild
  6. Appl. Environ. Microbiol. v.44 Dissimilar plasmids isolated from Pseudomoans diminuta MG and a Flavobacterium sp.(ATCC 27551) contain identical opd genes Harper,I.I.;C.S.McDaniel;C.E.Miller;J.R.Wild
  7. Proc. Natl. Acad. Sci. USA v.91 Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold Bazan,J.F.;L.H.Weaver;S.L.Roderick;R.Huber;B.W.Matthews https://doi.org/10.1073/pnas.91.7.2473
  8. Proc. Natl. Acad. Sci. USA v.95 Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli Wilce,M.C.J.;C.S.Bond;N.E.Dixon;H.C.Freeman;J.M.Guss;P.E.Lilley;J.A.Wilce https://doi.org/10.1073/pnas.95.7.3472
  9. Bioorg. Med. Chem. v.9 Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase Li,W.S.;K.T.Lim;M.Chen-Goodspeed;M.A.Sogorb;F.M.Raushel https://doi.org/10.1016/S0968-0896(01)00113-4
  10. Bioorg. Chem. v.29 Stereochemical specificity of organophosphorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin Hill,C.M.;W.S.Li;T.C.Cheng;J.J.DeFrank;F.M.Raushel https://doi.org/10.1006/bioo.2000.1189
  11. Biochemistry v.40 Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues Chen-Goodspeed,M.;M.A.Sogorb;F.Wu;F.M.Raushel https://doi.org/10.1021/bi001549d
  12. Chem. Biol. Interact. v.119;120 Alteromonas prolidase for organophosphorus G-agent decontamination Cheng,T.C.;J.J.DeFrank;V.K.Rastogi
  13. Mol. Genet. Genomics v.267 Cloning of a prolidase gene from Aspergillus nidulans and characterisation of its product Jalving,R.;P.Bron;H.C.Kester;J.Visser;P.J.Schaap https://doi.org/10.1007/s00438-002-0655-8
  14. Microbiology v.145 Characterization of a prolidase from Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 with an unusual regulation of biosynthesis Morel,F.;J.Frot-Coutaz;D.Aubel;R.Portalier;D.Atlan https://doi.org/10.1099/13500872-145-2-437
  15. J. Bacteriol. v.180 Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase(prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus Ghosh,M.;A.M.Grunden;D.M.Dun;R.Weiss;M.W.W.Adams