Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity

FEBS Open Bio

Volumn 3, Issue , 2013, Pages 473-478

  Jensen, Chantel N ^a   Ali, Sohail T ^b   Allen, Michael J ^b   Grogan, Gideon ^a  

^a UNIVERSITY OF YORK   (United Kingdom)

^b PLYMOUTH MARINE LABORATORY   (United Kingdom)

Author keywords

Baeyer Villiger monoxygenase; Biocatalyst; Flavoprotein monoxygenase; NADPH; Sulfoxide

Indexed keywords

ASPARAGINE; METHYLENETETRAHYDROFOLATE REDUCTASE (NADPH2); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNSPECIFIC MONOOXYGENASE;

ARTICLE; BINDING SITE; ENANTIOSELECTIVITY; ENZYME ENGINEERING; METHYLOPHAGA AMINISULFIDIVORANS; METHYLOTROPHIC BACTERIUM; MUTATION; NONHUMAN; PRIORITY JOURNAL; SULFOXIDATION;

METHYLOPHAGA; STENOTROPHOMONAS MALTOPHILIA;

EID: 84887529605     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2013.09.008     Document Type: Article

References (31)

1. van Berkel W.J.H., Kamerbeek N.M., Fraaije M.W. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 2006, 124:670-689.
2. Cashman J.R., Zhang J. Human flavin-containing monooxygenases. Annu. Rev. Pharmacol. Toxicol. 2006, 46:65-100.
3. Beam M., Bosserman M.A., Noinaj N., Wehenkel M., Rohr J. Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway. Biochemistry 2009, 48:4476-4487.
4. Seo M.-J., Zhu D., Endo S., Ikeda H., Cane D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 2011, 50:1739-1754.
5. Grogan G. Asymmetric enzymatic sulfoxidation. Comprehensive Chirality 2012, 295-328. Elsevier. E.M. Carreira, H. Yamamoto (Eds.).
6. Kamerbeek N.M., Fraaije M.W., Janssen D.B. Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases. Eur. J. Biochem. 2004, 271:2107-2116.
7. Dudek H., Torres Pazmiño D., Rodríguez C., de Gonzalo G., Gotor V., Fraaije M.W. Investigating the coenzyme specificity of phenylacetone monooxygenase from Thermobifida fusca. Appl. Microbiol. Biotechnol. 2010, 88:1135-1143.
8. Jensen C.N., Cartwright J., Ward J., Hart S., Turkenburg J.P., Ali S.T., Allen M.J., Grogan G. A flavoprotein monooxygenase that catalyses a Baeyer-Villiger reaction and thioether oxidation using NADH as the nicotinamide cofactor. Chembiochem 2012, 13:872-878.
9. Riebel A., de Gonzalo G., Fraaije M.W. Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHA1. J. Mol. Catal. B Enzym. 2013, 88:20-25.
10. Choi H.S., Kim J.K., Cho E.H., Kim Y.K., Kim J.I., Kim S.W. A novel flavin-containing monooxygenase from Methylophaga sp. strain SK1 and its indigo synthesis in Escherichia coli. Biochem. Biophys. Res. Commun. 2003, 306:930-936.
11. Rioz-Martinez A., Kopacz M., de Gonzalo G., Torres Pazmiño D.E., Gotor V., Fraaije M.W. Exploring the biocatalytic scope of a bacterial flavin-containing monooxygenase. Org. Biomol. Chem. 2011, 9:1337-1341.
12. Alfieri A., Malito E., Orru R., Fraaije M.W., Mattevi A. Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase. Proc. Natl. Acad. Sci. USA 2008, 105:6572-6577.
13. Cho H.J., Cho H.Y., Kim K.J., Kim M.H., Kim S.W., Kang B.S. Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism. J. Struct. Biol. 2011, 175:39-48.
14. Malito E., Alfieri A., Fraaije M.W., Mattevi A. Crystal structure of a Baeyer-Villiger monooxygenase. Proc. Natl. Acad. Sci. USA 2004, 101:13157-13162.
15. Mirza I.A., Yachnin B.J., Wang S., Grosse S., Bergeron H., Imura A., Iwaki H., Hasegawa Y., Lau P.C.K., Berghuis A.M. Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor. J. Am. Chem. Soc. 2009, 131:8848-8854.
16. Andreadeli A., Platis D., Tishkov V., Popov V., Labrou N.E. Structure-guided alteration of coenzyme specificity of formate dehydrogenase by saturation mutagenesis to enable efficient utilization of NADP+. FEBS J. 2008, 275:859-3869.
17. Hatrongjit R., Packdibamrung K. A novel NADP+-dependent formate dehydrogenase from Burkholderia stabilis 15516: screening, purification and characterization. Enzyme Microb. Technol. 2010, 46:557-561.
18. Reetz M.T., Daligault F., Brunner B., Hinrichs H., Deege A. Directed evolution of cyclohexanone monooxygenases: enantioselective biocatalysts for the oxidation of prochiral thioethers. Angew. Chem. Int. Ed. 2004, 43:4078-4081.
19. Torres Pazmiño D.E., Snajdrova R., Rial D.V., Mihovilovic M.D., Fraaije M.W. Altering the substrate specificity and enantioselectivity of phenylacetone monooxygenase by structure-inspired enzyme redesign. Adv. Synth. Catal. 2007, 349:1361-1368.
20. Orru R., Pazmiño D.E.T., Fraaije M.W., Mattevi A. Joint functions of protein residues and NADP(H) in oxygen activation by flavin-containing monooxygenase. J. Biol. Chem. 2010, 285:35021-35028.
21. McDonald C.A., Fagan R.L., Collard F., Monnier V.M., Palfey B.A. Oxygen reactivity in flavoenzymes: context matters. J. Am. Chem. Soc. 2011, 133:16809-16811.
22. Völker A., Kirschner A., Bornscheuer U.T., Altenbuchner J. Functional expression, purification and characterization of the recombinant Baeyer-Villiger monooxygenase MekA from Pseudomonas veronii MEK700. Appl. Microbiol. Biotechnol. 2008, 77:1251-1260.
23. Reetz M.T., Kahakeaw D., Lohmer R. Addressing the numbers problem in directed evolution. Chembiochem 2008, 9:1797-1804.
24. Hall M., Stueckler C., Kroutil W., Macheroux P., Faber K. Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 fromLycopersicon esculentum (Tomato): a striking change of stereoselectivity. Angew. Chem. Int. Ed. 2007, 46:3934-3937.
25. Kabsch W. XDS. Acta Crystallogr. Sect. D Biol. Crystallogr. 2010, 66:125-132.
26. Evans P. Scaling and assessment of data quality. Acta Crystallogr. Sect. D Biol. Crystallogr. 2006, 62:72-82.
27. Winter G. Xia2: an expert system for macromolecular crystallography data reduction. J. Appl. Crystallogr. 2010, 3:186-190.
28. Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
29. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D Biol. Crystallogr. 2004, 60:2126-2132.
30. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D Biol. Crystallogr. 1997, 53:240-255.
31. Laskowski R.A., Macarthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 1993, 26:283-291.