Marked enhancement of Acinetobacter sp. Organophosphorus hydrolase activity by a single residue substitution Ile211Ala

Bioresources and Bioprocessing

Volumn 2, Issue 1, 2015, Pages

  Chen, Jie ^a   Luo, Xiao Jing ^a   Chen, Qi ^a   Pan, Jiang ^a   Zhou, Jiahai ^b   Xu, Jian He ^a  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b SHANGHAI INSTITUTE OF ORGANIC CHEMISTRY   (China)

Author keywords

Crystal structure; Lactonase; Organophosphorus hydrolase; Semi rational design; Site directed mutagenesis

Indexed keywords

HYDROLASES;

ACINETOBACTER SP; CRYSTALS STRUCTURES; HYDROLASE ACTIVITIES; LACTONASE; METHYL PARATHION; ORGANOPHOSPHORUS-HYDROLASE; RATIONAL DESIGN; SEMI-RATIONAL DESIGN; SINGLE RESIDUE; SITE DIRECTED MUTAGENESIS;

CRYSTAL STRUCTURE;

EID: 85037058472     PISSN: None     EISSN: 21974365     Source Type: Journal    
DOI: 10.1186/s40643-015-0067-3     Document Type: Article

References (27)

1. Afriat L, Roodveldt C, Manco G, Tawfik DS (2006) The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry 45:13677–13686
2. Bar-Rogovsky H, Hugenmatter A, Tawfik DS (2013) The evolutionary origins of detoxifying enzymes: the mammalian serum paraoxonases (PONs) relate to bacterial homoserine lactonases. J Biol Chem 288:23914–23927
3. Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS (2012) Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1. J Mol Biol 418:181–196
4. Cheng TC, DeFrank JJ, Rastogi VK (1999) Alteromonas prolidase for organophosphorus G-agent decontamination. Chem Biol Interact 119:455–462
5. Dong YJ, Bartlam M, Sun L, Zhou YF, Zhang ZP, Zhang GG, Rao Z, Zhang XE (2005) Crystal structure of methyl parathion hydrolase from Pseudomonas sp. WBC-3. J Mol Biol 353:655–663
6. Du FL, Yu HL, Xu JH, Li CX (2014) Enhanced limonene production by optimizing the expression of limonene biosynthesis and MEP pathway genes in E. coli. Bioresour Bioprocess 1:10
7. Dumas DP, Caldwell SR, Wild JR, Raushel FM (1989) Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J Biol Chem 264:19659–19665
8. Elias M, Dupuy J, Merone L, Mandrich L, Porzio E, Moniot S, Rochu D, Lecomte C, Rossi M, Masson P, Manco G, Chabriere E (2008) Structural basis for natural lactonase and promiscuous phosphotriesterase activities. J Mol Biol 379:1017–1028
9. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60:2126–2132
10. Gotthard G, Hiblot J, Gonzalez D, Elias M, Chabriere E (2013) Structural and enzymatic characterization of the phosphotriesterase OPHC2 from pseudomonas pseudoalcaligenes. PLoS ONE 8:e77995
11. Hawwa R, Larsen SD, Ratia K, Mesecar AD (2009) Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans. J Mol Biol 393:36–57
12. Hong L, Zhang JJ, Zhang SJ, Zhang XE, Zhou NY (2005) Plasmid-borne catabolism of methyl parathion and p-nitrophenolin Pseudomonas sp. strain WBC-3. Biochem Biophys Res Commun 334:1107–1114
13. Khersonsky O, Tawfik DS (2005) Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44:6371–6382
14. Luo XJ, Kong XD, Zhao J, Zhou JH, Xu JH (2014) Switching a newly discovered lactonase into an efficient and thermostable phosphotriesterase by simple double mutations His250Ile/Ile263Trp. Biotechnol Bioeng 111:1920–1930
15. McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ (2007) Phaser crystallographic software. J Appl Crystallogr 40:658–674
16. Merone L, Mandrich L, Porzio E, Rossi M, Muller S, Reiter G, Worek F, Manco G (2010) Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase. Bioresour Technol 101:9204–9212
17. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240–255
18. Omburo GA, Kuo JM, Mullins LS, Raushel FM (1992) Characterization of the zinc binding site of bacterial phosphotriesterase. J Biol Chem 267:13278–13283
19. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307–326
20. Raushel FM (2002) Bacterial detoxification of organophosphate nerve agents. Curr Opin Microbiol 5:288–295
21. Roodveldt C, Tawfik DS (2005) Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily. Biochemistry 44:12728–12736
22. Sapozhnikova Y, Bawardi O, Schlenk D (2004) Pesticides and PCBs insediments and fish from the Salton Sea, California, USA. Chemosphere 55:797–809
23. Sapozhnikova Y, Zubcov N, Hungerford S, Roy LA, Boicencob N, Zubcovb E, Schlenka D (2005) Evaluation of pesticides and metals in fish of the Dniester River, Moldova. Chemosphere 60:196–205
24. Singh BK (2008) Organophosphorus-degrading bacteria: ecology and industrial applications. Nat Rev Microbiol 7:156–164
25. Singh BK, Walker A (2006) Microbial degradation of organophosphorus compounds. FEMS Microbiol Rev 30:428–471
26. Vyas NK, Nickitenko A, Rastogi VK, Shah SS, Quiocho FA (2010) Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase. Biochemistry 49:547–559
27. Zhang Y, An J, Ye W, Yang G, Qian ZG, Chen HF, Cui L, Feng Y (2012) Enhancing the promiscuous phosphotriesterase activity of a thermostable lactonase (GkaP) for the efficient degradation of organophosphate pesticides. Appl Environ Microbiol 78:6647–6655