A bifunctional enzyme from Rhodococcus erythropolis exhibiting secondary alcohol dehydrogenase-catalase activities

Applied Microbiology and Biotechnology

Volumn 98, Issue 22, 2014, Pages 9249-9258

  Martinez Rojas, Enriqueta ^a   Kurt, Tutku ^b   Schmidt, Udo ^b   Meyer, Vera ^b   Garbe, Leif Alexander ^a,b  

^a Central Laboratory   (Germany)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Catalase; R. erythropolis; Secondary alcohol dehydrogenase; Lactols; Lactones

Indexed keywords

ESCHERICHIA COLI; ESTERS; MASS SPECTROMETRY; PURIFICATION; SUBSTRATES;

CATALASE; FINE AND BULK CHEMICALS; LACTOLS; MASS SPECTROMETRIC IDENTIFICATION; NICOTINAMIDE ADENINE DINUCLEOTIDES; R. ERYTHROPOLIS; RHODOCOCCUS ERYTHROPOLIS; SECONDARY ALCOHOL DEHYDROGENASE;

ENZYMES;

ALCOHOL DEHYDROGENASE; CATALASE; COENZYME; ISOPROPANOL DEHYDROGENASE (NADP); LACTONE; NICOTINAMIDE ADENINE DINUCLEOTIDE;

CHEMISTRY; COENZYME; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; MOLECULAR CLONING; OXIDATION REDUCTION REACTION; RHODOCOCCUS; TEMPERATURE;

ALCOHOL OXIDOREDUCTASES; CATALASE; CLONING, MOLECULAR; COENZYMES; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION; LACTONES; MASS SPECTROMETRY; NAD; OXIDATION-REDUCTION; RHODOCOCCUS; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84920249583     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5808-2     Document Type: Article

References (33)

1. Abokitse K, Hummel W (2003) Cloning, sequence analysis and heterologous expression of the gene encoding a (s)-specific alcohol dehydrogenase from Rhodococcus erythropolis DSM 43297. Appl Microbiol Biotechnol 62:380–386
2. Barbey C, Crépin A, Cirou A, Budin-Verneuil A, Orange N, Feuillolev M, Faure D, Dessaux Y, Burini JF, Latour X (2012) Catabolic pathway of gamma-caprolactone in the biocontrol agent Rhodococcus erythropolis. J Proteome Res 11:206–2016
3. Bradford MM (1976) A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
4. Bryant FO, Wiegel J, Ljungdahl LG (1988) Purification and properties of primary and secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus. Appl Environ Microbiol 54:460–465
5. Chelikani P, Fita I, Loewen PC (2004) Review: diversity of structure and properties among catalases. Cell Mol Life Sci 61:192–208
6. Da Carvalho CCCR, Da Fonseca MMR (2005) The remarkable Rhodococcus erythropolis. Appl Microbiol Biotechnol 67:715–726
7. Eisenthal R, Cornish-Bowden (1974) The direct linear plot: a new graphical procedure for estimating enzyme kinetic parameter. Biochem J 193:715–720
8. Fuhrmann H, Dobeleit G, Belleir S, Gück T (2002) Cholesterol oxidase and resistance of Rhodococcus equi to peroxidative stress in vitro in the presence of cholesterol. J Vet Med B 49:310–311
9. Gabriel O (1971) Analytical disc gel electrophoresis. In: Jakoby WB (ed) Methods in enzymology. Academic Press, New York
10. Garbe LA, Morgenthal K, Kuscher K, Tressl R (2008) Metabolism of deuterated erythro-dihydroxy fatty acids in Saccharomyces cerevisiae. Enantioselective formation and characterization of hydroxylactones. Helv Chim Acta 91:993–1007
11. Haroune N, Combourieu B, Besse P, Sancelme M, Reemtsma T, Kloeper A, Biab A, Knapp JS, Baumberg S, Delort AM (2002) Benzothiazole degradation by Rhodococcus pyrodinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity. Appl Environ Microbiol 68:6114–6120
12. Hauck R, Adrian L, Wendler P, Amidjojo M, Hegemann W, Görisch H (2001) Transformation of 2,2′-dichlorodiisopropyl ether in mixed and pure culture. Appl Microbiol Biotechnol 56:491–495
13. Hou CT, Patel R, Bernabe N, Marczak I (1981) Stereospecificity and other properties of a novel secondary-alcohol-specific alcohol dehydrogenase. E J Biochem 119:359–364
14. Hughes MA, Macfadden JM, Townsed CA (2005) New alpha-methylene-γ-butyrolactones with antimycobacterial properties. Bioorg Med Chem Lett 15:3857–3859
15. Jeon YJ, Fong JCN, Riyanti EL, Neilan BA, Rogers PL, Svenson CJ (2007) Heterologous expression of the alcohol dehydrogenase (adhI) gene from Geobacillus thermoglucosidasius strain M10EXG. J Biotechnol 135:127–133
16. Kataoka M, Ishige T, Urano N, Nakamura Y, Sakuradani E, Fukui S, Kita S, Sakamoto K, Shimizu S (2008) Cloning and expression of the L-1amino-2-propanol dehydrogenase gene of Rhodococcus erythropolis, and its application to double chiral compound production. Appl Microbiol Biotechnol 80:597–604
17. Koclar AG, Coruh N, Bolukbasi U, Ogel ZB (2012) Oxidation of phenolic compounds by the bifunctional catalase-phenol oxidase (CATPO) from Scytalidium thermophilum. Appl Microbiol Biotechnol 97:661–6672
18. Koo OK, Jeong DW, Lee JM, Kim JM, Lee JH, Chang HC, Hwan JK, Lee HJ (2005) Cloning and characterization of the bifunctional alcohol/acetaldehyde dehydrogenase gene (adhE) in Leuconostoc mesenteroides isolated from kimchi. Biotechnol Lett 27:505–510
19. Kreit J, Elalamib A (2002) Substrate characterization of a NAD-dependent secondary alcohol dehydrogenase from Rhodococcus sp. GK1 (CIP 105335). J Mol Catal B: Enzym 19:253–259
20. Kujo C, Ohshima T (1998) Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase form the Archaeon Pyrobacterium islandicum and effects of denaturants and organic solvents. Appl Environ Microbiol 64:2152–2157
21. Kulys J, Kriauciunas K, Vidziunaite R (2003) Biphasic character of fungal catalases inhibition with hydroxylamine in presence of hydrogen peroxide. J Mol Catal B: Enzym 26:79–85
22. Ludwig B, Akundi A, Kendall K (1995) A long-chain secondary alcohol dehydrogenase from Rhodococcus erythropolis ATCC 4277. Appl Environ Microbiol 61:3729–3733
23. Moreno-Horn M, Garbe LA, Tressl R, Görisch H (2005) Transient accumulation of γ-butyrolactone during degradation of bis(4-chloro-n-butyl) ether by diethylether grown Rhodococcus sp. strain DTB. Appl Microbiol Biotechnol 69:335–340
24. Moreno-Horn M, Martinez-Rojas E, Görisch H, Tressl R, Garbe LA (2007) Oxidation of 1,4-alkanediols into γ-lactones via γ-lactols using Rhodococcus erythropolis as biocatalyst. J Mol Catal B: Enzym 49:24–27
25. Romano D, Contente M, Granato T, Remmelli W, Zambelli P, Molinari F (2013) Biocatalytic oxidation of 1,4-diols and γ-lactols into γ-lactones: application to chemoenzymatic synthesis of drospirenone. Monatsh Chem 144:735–737
26. Schenkels P, Duine JA (2000) Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. Microbiology 146:4775–4785
27. Shimizu S, Kobayashi H, Masai E, Fukuda M (2001) Characterization of the 450-kb linear plasmid in a polychlorinated biphenyl degrader, Rhodococcus sp. strain RHA1. Appl Environ Microbiol 67:2021–2028
28. Si D, Urano N, Nozaki S, Honda K, Shimizu S, Kataoka M (2012) L-pantoyl lactone dehydrogenase from Rhodococcus erythropolis: genetic analyses and application to the stereospecific oxidation of L-pantoyl lactone. Appl Microbiol Biotechnol 95:431–440
29. Solyanikova IP, Moiseeva OV, Boeren S, Boersma MG, Kolomytseva MP, Vervoot J, Rietjens ICM, Golovleva LA, van Berkel JH (2003) Conversion of 2-fluoromuconate to cis-dienelactone by purified enzyme of Rhodococcus opacus 1cp. Appl Environ Microbiol 69:5636–5642
30. Takarada H, Sekine M, Hosoyama A, Yamada R, Fujisawa T, Omata S, Shimizu A, Tsukatani N, Tanikawa S, Fujita N, Harayama S (2009) Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4. EMBL/GenBank/DDBJ databases. Accessed Mar 2009
31. Tamura H, Appel M, Richling E, Schreier P (2006) Gamma-butyrolactones: streptomyces signalling molecules regulating antibiotic production and differentiation. Curr Opin Microbiol 3:287–294
32. Vera-Cabrera L, Johnson WM, Welsh O, Resendiz-Uresti FL, Salinas-Carmona MC (1999) Distribution in members of the genera Nocardia, Gordona, and Rhodoccus. J Clin Microbiol 3:1971–1976
33. Zhang T, Heym B, Allen B, Young D, Cole S (1992) The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358:591–593