Cloning and characterization of a thermostable H 2O-forming NADH oxidase from Lactobacillus rhamnosus

Enzyme and Microbial Technology

Volumn 50, Issue 4-5, 2012, Pages 255-262

  Zhang, Ye Wang ^a,b   Tiwari, Manish Kumar ^a   Gao, Hui ^a   Dhiman, Saurabh Sudha ^a   Jeya, Marimuthu ^a   Lee, Jung Kul ^a  

^a Konkuk University   (South Korea)

^b JIANGSU UNIVERSITY   (China)

Author keywords

Characterization; Cofactor regeneration; H 2O forming NADH oxidase; Lactobacillus rhamnosus; Thermal stability

Indexed keywords

AMINO ACID RESIDUES; COFACTOR REGENERATION; GEL-FILTRATION CHROMATOGRAPHY; HEAT INACTIVATION; HIGH ACTIVITY; HOMODIMERS; LACTOBACILLUS RHAMNOSUS; MOLECULAR DYNAMICS SIMULATIONS; NADH OXIDASE; OPEN READING FRAME; OPTIMAL ACTIVITY; SEQUENCE ANALYSIS; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS;

AMINO ACIDS; BACILLI; CHARACTERIZATION; CLONING; ELECTROPHORESIS; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENES; INDUSTRIAL APPLICATIONS; MOLECULAR DYNAMICS; SODIUM; SODIUM SULFATE; THERMODYNAMIC STABILITY;

ENZYME ACTIVITY;

AMINO ACID; DODECYL SULFATE SODIUM; HOMODIMER; METAL ION; POLYPEPTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; WATER;

ARTICLE; BACTERIAL GENE; CATALYSIS; CLONING; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME METABOLISM; ENZYME PURIFICATION; ENZYME STABILITY; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; GENE OVEREXPRESSION; GENETIC CODE; HEAT; LACTOBACILLUS RHAMNOSUS; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NONHUMAN; OPEN READING FRAME; PH; PHYSICAL CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

AMINO ACID SEQUENCE; BIOTECHNOLOGY; CLONING, MOLECULAR; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME STABILITY; ESCHERICHIA COLI; HOT TEMPERATURE; KINETICS; LACTOBACILLUS RHAMNOSUS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; NAD; NADH, NADPH OXIDOREDUCTASES; RECOMBINANT PROTEINS; SEQUENCE ANALYSIS, DNA; WATER;

ESCHERICHIA COLI; LACTOBACILLUS RHAMNOSUS;

EID: 84862830721     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.01.009     Document Type: Article

References (36)

1. Zhang W., O'Connor K., Wang D.I., Li Z. Bioreduction with efficient recycling of NADPH by coupled permeabilized microorganisms. Appl Environ Microbiol 2009, 75:687-694.
2. Wichmann R., Vasic-Racki D. Cofactor regeneration at the lab scale. Adv Biochem Eng Biotechnol 2005, 92:225-260.
3. Geueke B., Riebel B., Hummel W. NADH oxidase from Lactobacillus brevis: a new catalyst for the regeneration of NAD. Enzyme Microb Technol 2003, 32:205-211.
4. Riebel B.R., Gibbs P.R., Wellborn W.B., Bommarius A.S. Cofactor regeneration of NAD+ from NADH: novel water-forming NADH oxidases. Adv Synth Catal 2002, 344:1156-1168.
5. Ward D.E., Donnelly C.J., Mullendore M.E., van der Oost J., de Vos W.M., Crane E.J. The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress. Eur J Biochem 2001, 268:5816-5823.
6. Claiborne A., Yeh J.I., Mallett T.C., Luba J., Crane E.J., Charrier V., et al. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 1999, 38:15407-15416.
7. 2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309. Appl Microbiol Biotechnol 2008, 80:71-78.
8. 2O-forming NADH oxidase from Streptococcus faecalis. Eur J Biochem 1986, 156:149-155.
9. Higuchi M. Reduced nicotinamide adenine dinucleotide oxidase involvement in defense against oxygen toxicity of Streptococcus mutans. Oral Microbiol Immunol 1992, 7:309-314.
10. Yang X., Ma K. Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima. J Bacteriol 2007, 189:3312-3317.
11. Yang X., Ma K. Purification and characterization of an NADH oxidase from extremely thermophilic anaerobic bacterium Thermotoga hypogea. Arch Microbiol 2005, 183:331-337.
12. 2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria. Arch Microbiol 2004, 181:324-330.
13. Herles C., Braune A., Blaut M. Purification and characterization of an NADH oxidase from Eubacterium ramulus. Arch Microbiol 2002, 178:71-74.
14. Riebel B.R., Gibbs P.R., Wellborn W.B., Bommarius A.S. Cofactor regeneration of both NAD+ from NADH and NADP+ from NADPH:NADH oxidase from Lactobacillus sanfranciscensis. Adv Synth Catal 2003, 345:707-712.
15. Hummel W., Riebel B. Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis. Biotechnol Lett 2003, 25:51-54.
16. Case C.L., Rodriguez J.R., Mukhopadhyay B. Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii. Microbiology 2009, 155:69-79.
17. Toomey D., Mayhew S.G. Purification and characterisation of NADH oxidase from Thermus aquaticus YT1 and evidence that it functions in a peroxide-reduction system. Eur J Biochem 1998, 251:935-945.
18. 2-forming NADH oxidases from Archaeoglobus fulgidus. Eur J Biochem 2003, 270:2885-2894.
19. 2O. FEBS J 2008, 275:5355-5366.
20. Hirano J.-I., Miyamoto K., Ohta H. The green and effective oxidation of alcohols to carboxylic acids with molecular oxygen via biocatalytic reaction. Tetrahedron Lett 2008, 49:1217-1219.
21. 2-forming NADH oxidase is an alkyl hydroperoxide reductase protein. Free Radical Biol Med 2000, 28:108-120.
22. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
23. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 1996, 8:477-486.
24. Tiwari M., Lee J.K. Molecular modeling studies of l-arabinitol 4-dehydrogenase of Hypocrea jecorina: its binding interactions with substrate and cofactor. J Mol Graph Model 2010, 28:707-713.
25. Lopez de Felipe F., Hugenholtz J. Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis. Int Dairy J 2001, 11:37-44.
26. Koike K., Kobayashi T., Ito S., Saitoh M. Purification and characterization of NADH oxidase from a strain of Leuconostoc mesenteroides. J Biochem 1985, 97:1279-1288.
27. Ross R.P., Claiborne A. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1: comparison with NADH peroxidase and the flavoprotein disulfide reductases. J Mol Biol 1992, 227:658-671.
28. 2O-forming NADH oxidase from Streptococcus mutans. Biosci Biotechnol Biochem 1996, 60:39-43.
29. 2-forming NADH oxidase from Sporolactobacillus inulinus NRIC 1133T. J Ferment Bioeng 1996, 82:531-537.
30. 2 into two water molecules by the flavoenzyme. Biochemistry 2006, 45:9648-9659.
31. Mallett T.C., Claiborne A. Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change. Biochemistry 1998, 37:8790-8802.
32. Krauth-Siegel R.L., Arscott L.D., Schonleben-Janas A., Schirmer R.H., Williams C.H. Role of active site tyrosine residues in catalysis by human glutathione reductase. Biochemistry 1998, 37:13968-13977.
33. Jakoby W.B., Fredericks J. Erythritol dehydrogenase from Aerobacter aerogenes. Biochim Biophys Acta 1961, 48:26-32.
34. Yang V., Jeffries T. Purification and properties of xylitol dehydrogenase from the xylose-fermenting yeast Candida shehatae. Appl Biochem Biotechnol 1990, 26:197-206.
35. Takamizawa K., Uchida S., Hatsu M., Suzuki T., Kawai K. Development of a xylitol biosensor composed of xylitol dehydrogenase and diaphorase. Can J Microbiol 2000, 46:350-357.
36. Yablochkova E.N., Bolotnikova O.I., Mikhailova N.P., Nemova N.N., Ginak A.I. The activity of xylose reductase and xylitol dehydrogenase in yeasts. Microbiology 2003, 72:414-417.