Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids
Bakonyi D, Hummel W (2017)
ENZYME AND MICROBIAL TECHNOLOGY 99: 16-24.
Zeitschriftenaufsatz
| Veröffentlicht | Englisch
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Bakonyi, Daniel;
Hummel, WernerUniBi
Abstract / Bemerkung
A gene encoding a novel 7 alpha-specific NADP(+)-dependent hydroxysteroid dehydrogenase from Clostridium difficile was cloned and heterologously expressed in Escherichia coli. The enzyme was purified using an N-terminal hexa-his-tag and biochemically characterized. The optimum temperature is at 60 degrees C, but the enzyme is inactivated at this temperature with a half-life time of 5 min. Contrary to other known 7 alpha-HSDHs, for example from Clostridium sardiniense or E. coli, the enzyme from C. difficile does not display a substrate inhibition. In order to demonstrate the applicability of this enzyme, a small-scale biotransformation of the bile acid chenodeoxycholic acid (CDCA) into 7-ketolithocholic acid (7-KLCA) was carried out with simultaneous regeneration of NADP(+) using an NADPH oxidase that resulted in a complete conversion (<99%). Furthermore, by a structure-based site-directed mutagenesis, cofactor specificity of the 7 alpha-HSDH from Clostridium difficile was altered to accept NAD(H). This mutant was biochemically characterized and compared to the wild-type.(C) 2016 Published by Elsevier Inc.
Stichworte
7 alpha-hydroxysteroid dehydrogenase;
Clostridium difficile;
Bile acids;
7-ketolithocholic acid;
Cofactor specificity;
NAD(P)H oxidase
Erscheinungsjahr
2017
Zeitschriftentitel
ENZYME AND MICROBIAL TECHNOLOGY
Band
99
Seite(n)
16-24
ISSN
0141-0229
eISSN
1879-0909
Page URI
https://pub.uni-bielefeld.de/record/2916563
Zitieren
Bakonyi D, Hummel W. Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids. ENZYME AND MICROBIAL TECHNOLOGY. 2017;99:16-24.
Bakonyi, D., & Hummel, W. (2017). Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids. ENZYME AND MICROBIAL TECHNOLOGY, 99, 16-24. doi:10.1016/j.enzmictec.2016.12.006
Bakonyi, Daniel, and Hummel, Werner. 2017. “Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids”. ENZYME AND MICROBIAL TECHNOLOGY 99: 16-24.
Bakonyi, D., and Hummel, W. (2017). Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids. ENZYME AND MICROBIAL TECHNOLOGY 99, 16-24.
Bakonyi, D., & Hummel, W., 2017. Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids. ENZYME AND MICROBIAL TECHNOLOGY, 99, p 16-24.
D. Bakonyi and W. Hummel, “Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids”, ENZYME AND MICROBIAL TECHNOLOGY, vol. 99, 2017, pp. 16-24.
Bakonyi, D., Hummel, W.: Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids. ENZYME AND MICROBIAL TECHNOLOGY. 99, 16-24 (2017).
Bakonyi, Daniel, and Hummel, Werner. “Cloning, expression, and biochemical characterization of a novel NADP(+)-dependent 7 alpha-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids”. ENZYME AND MICROBIAL TECHNOLOGY 99 (2017): 16-24.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
2 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
NAD+ -Dependent Enzymatic Route for the Epimerization of Hydroxysteroids.
Tonin F, Otten LG, Arends IWCE., ChemSusChem 12(13), 2019
PMID: 30265441
Tonin F, Otten LG, Arends IWCE., ChemSusChem 12(13), 2019
PMID: 30265441
Latest development in the synthesis of ursodeoxycholic acid (UDCA): a critical review.
Tonin F, Arends IWCE., Beilstein J Org Chem 14(), 2018
PMID: 29520309
Tonin F, Arends IWCE., Beilstein J Org Chem 14(), 2018
PMID: 29520309
44 References
Daten bereitgestellt von Europe PubMed Central.
Bile salt biotransformations by human intestinal bacteria
Ridlon, J. Lipid Res. 47(), 2005
Ridlon, J. Lipid Res. 47(), 2005
Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme.
Yoshimoto T, Higashi H, Kanatani A, Lin XS, Nagai H, Oyama H, Kurazono K, Tsuru D., J. Bacteriol. 173(7), 1991
PMID: 2007545
Yoshimoto T, Higashi H, Kanatani A, Lin XS, Nagai H, Oyama H, Kurazono K, Tsuru D., J. Bacteriol. 173(7), 1991
PMID: 2007545
Cloning and characterization of the NAD-dependent 7alpha-Hydroxysteroid dehydrogenase from Bacteroides fragilis.
Bennett MJ, McKnight SL, Coleman JP., Curr. Microbiol. 47(6), 2003
PMID: 14756531
Bennett MJ, McKnight SL, Coleman JP., Curr. Microbiol. 47(6), 2003
PMID: 14756531
Review: bacterial transformations of bile acids
Prabha, World J. Microb. Biot. 22(), 2005
Prabha, World J. Microb. Biot. 22(), 2005
7alpha-OH epimerisation of bile acids via oxido-reduction with Xanthomonas maltophilia.
Medici A, Pedrini P, Bianchini E, Fantin G, Guerrini A, Natalini B, Pellicciari R., Steroids 67(1), 2002
PMID: 11728521
Medici A, Pedrini P, Bianchini E, Fantin G, Guerrini A, Natalini B, Pellicciari R., Steroids 67(1), 2002
PMID: 11728521
Xanthomonas maltophilia CBS 897.97 as a source of new 7beta- and 7alpha-hydroxysteroid dehydrogenases and cholylglycine hydrolase: improved biotransformations of bile acids.
Pedrini P, Andreotti E, Guerrini A, Dean M, Fantin G, Giovannini PP., Steroids 71(3), 2005
PMID: 16307764
Pedrini P, Andreotti E, Guerrini A, Dean M, Fantin G, Giovannini PP., Steroids 71(3), 2005
PMID: 16307764
7alpha- and 12alpha-Hydroxysteroid dehydrogenases from Acinetobacter calcoaceticus lwoffii: a new integrated chemo-enzymatic route to ursodeoxycholic acid.
Giovannini PP, Grandini A, Perrone D, Pedrini P, Fantin G, Fogagnolo M., Steroids 73(14), 2008
PMID: 18674553
Giovannini PP, Grandini A, Perrone D, Pedrini P, Fantin G, Fogagnolo M., Steroids 73(14), 2008
PMID: 18674553
Characterization and regulation of the NADP-linked 7 alpha-hydroxysteroid dehydrogenase gene from Clostridium sordellii.
Coleman JP, Hudson LL, Adams MJ., J. Bacteriol. 176(16), 1994
PMID: 8050999
Coleman JP, Hudson LL, Adams MJ., J. Bacteriol. 176(16), 1994
PMID: 8050999
The three-dimensional structure of Clostridium absonum 7α-hydroxysteroid dehydrogenase, new insights into the conserved arginines for NADP(H) recognition
Lou, Nat. Protoc. 6(), 2016
Lou, Nat. Protoc. 6(), 2016
Purification and characterization of a microbial, NADP-dependent bile acid 7α-hydroxysteroid dehydrogenase
Franklund, J. Biol. Chem. (), 1990
Franklund, J. Biol. Chem. (), 1990
Cloning, sequencing, and expression of the gene coding for bile acid 7 alpha-hydroxysteroid dehydrogenase from Eubacterium sp. strain VPI 12708.
Baron SF, Franklund CV, Hylemon PB., J. Bacteriol. 173(15), 1991
PMID: 1856160
Baron SF, Franklund CV, Hylemon PB., J. Bacteriol. 173(15), 1991
PMID: 1856160
Cloning, expression and characterization of a putative 7alpha-hydroxysteroid dehydrogenase in Comamonas testosteroni.
Ji W, Chen Y, Zhang H, Zhang X, Li Z, Yu Y., Microbiol. Res. 169(2-3), 2013
PMID: 23972763
Ji W, Chen Y, Zhang H, Zhang X, Li Z, Yu Y., Microbiol. Res. 169(2-3), 2013
PMID: 23972763
Multiple forms of 7-alpha-hydroxysteroid dehydrogenase in selected strains of Bacteroides fragilis.
Hylemon PB, Sherrod JA., J. Bacteriol. 122(2), 1975
PMID: 236279
Hylemon PB, Sherrod JA., J. Bacteriol. 122(2), 1975
PMID: 236279
The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative.
Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U., Chem. Biol. Interact. 178(1-3), 2008
PMID: 19027726
Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U., Chem. Biol. Interact. 178(1-3), 2008
PMID: 19027726
Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.
Kavanagh KL, Jornvall H, Persson B, Oppermann U., Cell. Mol. Life Sci. 65(24), 2008
PMID: 19011750
Kavanagh KL, Jornvall H, Persson B, Oppermann U., Cell. Mol. Life Sci. 65(24), 2008
PMID: 19011750
The catalytic promiscuity of a microbial 7α-hydroxysteroid dehydrogenase. Reduction of non-steroidal carbonyl compounds.
Liu Y, Lv T, Ren J, Wang M, Wu Q, Zhu D., Steroids 76(10-11), 2011
PMID: 21600233
Liu Y, Lv T, Ren J, Wang M, Wu Q, Zhu D., Steroids 76(10-11), 2011
PMID: 21600233
Isolates from normal human intestinal flora but not lactic acid bacteria exhibit 7α- and 7β-hydroxysteroid dehydrogenase activities
Lepercq, Microb. Ecol. Heal. Dis. 16(), 2004
Lepercq, Microb. Ecol. Heal. Dis. 16(), 2004
Targets for current pharmacologic therapy in cholesterol gallstone disease
Di, Gastroenterol. Clin. N. 39(), 2010
Di, Gastroenterol. Clin. N. 39(), 2010
Modulation of the fecal bile acid profile by gut microbiota in cirrhosis.
Kakiyama G, Pandak WM, Gillevet PM, Hylemon PB, Heuman DM, Daita K, Takei H, Muto A, Nittono H, Ridlon JM, White MB, Noble NA, Monteith P, Fuchs M, Thacker LR, Sikaroodi M, Bajaj JS., J. Hepatol. 58(5), 2013
PMID: 23333527
Kakiyama G, Pandak WM, Gillevet PM, Hylemon PB, Heuman DM, Daita K, Takei H, Muto A, Nittono H, Ridlon JM, White MB, Noble NA, Monteith P, Fuchs M, Thacker LR, Sikaroodi M, Bajaj JS., J. Hepatol. 58(5), 2013
PMID: 23333527
Steroid-binding properties of the rat seminal vesicle androgen receptor: short-term and long-term competition of various steroids with radioactive dihydrotestosterone.
Zakar T, Toth M., J. Steroid Biochem. 17(3), 1982
PMID: 7132347
Zakar T, Toth M., J. Steroid Biochem. 17(3), 1982
PMID: 7132347
Formation of ursodeoxycholic acid from chenodeoxycholic acid by a 7 beta-hydroxysteroid dehydrogenase-elaborating Eubacterium aerofaciens strain cocultured with 7 alpha-hydroxysteroid dehydrogenase-elaborating organisms.
MacDonald IA, Rochon YP, Hutchison DM, Holdeman LV., Appl. Environ. Microbiol. 44(5), 1982
PMID: 6758698
MacDonald IA, Rochon YP, Hutchison DM, Holdeman LV., Appl. Environ. Microbiol. 44(5), 1982
PMID: 6758698
Enzymatic routes for the synthesis of ursodeoxycholic acid.
Eggert T, Bakonyi D, Hummel W., J. Biotechnol. 191(), 2014
PMID: 25131646
Eggert T, Bakonyi D, Hummel W., J. Biotechnol. 191(), 2014
PMID: 25131646
Exploitation of a Laccase/Meldola’s blue system for NAD+ regeneration in preparative scale hydroxysteroid dehydrogenase-catalyzed oxidations
Ferrandi, Adv. Synth. Catal. 354(), 2012
Ferrandi, Adv. Synth. Catal. 354(), 2012
The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O2 into two water molecules by the flavoenzyme
Lountos, J. Am. Chem. Soc. 45(), 2006
Lountos, J. Am. Chem. Soc. 45(), 2006
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
Bradford MM., Anal. Biochem. 72(), 1976
PMID: 942051
Bradford MM., Anal. Biochem. 72(), 1976
PMID: 942051
SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information
Biasini, Nucleic Acids Res. (), 2014
Biasini, Nucleic Acids Res. (), 2014
The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling.
Arnold K, Bordoli L, Kopp J, Schwede T., Bioinformatics 22(2), 2005
PMID: 16301204
Arnold K, Bordoli L, Kopp J, Schwede T., Bioinformatics 22(2), 2005
PMID: 16301204
The SWISS-MODEL Repository and associated resources.
Kiefer F, Arnold K, Kunzli M, Bordoli L, Schwede T., Nucleic Acids Res. 37(Database issue), 2008
PMID: 18931379
Kiefer F, Arnold K, Kunzli M, Bordoli L, Schwede T., Nucleic Acids Res. 37(Database issue), 2008
PMID: 18931379
Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: a historical perspective.
Guex N, Peitsch MC, Schwede T., Electrophoresis 30 Suppl 1(), 2009
PMID: 19517507
Guex N, Peitsch MC, Schwede T., Electrophoresis 30 Suppl 1(), 2009
PMID: 19517507
3DLigandSite: predicting ligand-binding sites using similar structures.
Wass MN, Kelley LA, Sternberg MJ., Nucleic Acids Res. 38(Web Server issue), 2010
PMID: 20513649
Wass MN, Kelley LA, Sternberg MJ., Nucleic Acids Res. 38(Web Server issue), 2010
PMID: 20513649
Epimerization of chenodeoxycholic acid to ursodeoxycholic acid by Clostridium baratii isolated from human feces.
Lepercq P, Gerard P, Beguet F, Raibaud P, Grill JP, Relano P, Cayuela C, Juste C., FEMS Microbiol. Lett. 235(1), 2004
PMID: 15158263
Lepercq P, Gerard P, Beguet F, Raibaud P, Grill JP, Relano P, Cayuela C, Juste C., FEMS Microbiol. Lett. 235(1), 2004
PMID: 15158263
Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli.
Tanabe T, Tanaka N, Uchikawa K, Kabashima T, Ito K, Nonaka T, Mitsui Y, Tsuru M, Yoshimoto T., J. Biochem. 124(3), 1998
PMID: 9722677
Tanabe T, Tanaka N, Uchikawa K, Kabashima T, Ito K, Nonaka T, Mitsui Y, Tsuru M, Yoshimoto T., J. Biochem. 124(3), 1998
PMID: 9722677
Short-chain dehydrogenases/reductases (SDR)
Jörnvall, J. Am. Chem. Soc. 34(), 1995
Jörnvall, J. Am. Chem. Soc. 34(), 1995
Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs)
Persson, Chem. Biol. Interact. 143–144(143), 2003
Persson, Chem. Biol. Interact. 143–144(143), 2003
Kinetics of enzymes subject to very strong product inhibition: analysis using simplified integrated rate equations and average velocities.
Schmidt ND, Peschon JJ, Segel IH., J. Theor. Biol. 100(4), 1983
PMID: 6876816
Schmidt ND, Peschon JJ, Segel IH., J. Theor. Biol. 100(4), 1983
PMID: 6876816
Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli
Tanaka, J. Am. Chem. Soc. 35(), 1996
Tanaka, J. Am. Chem. Soc. 35(), 1996
Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase.
Chen Z, Lee WR, Chang SH., Eur. J. Biochem. 202(2), 1991
PMID: 1761031
Chen Z, Lee WR, Chang SH., Eur. J. Biochem. 202(2), 1991
PMID: 1761031
Alteration of coenzyme specificity in halophilic NAD(P)+ glucose dehydrogenase by site-directed mutagenesis
Pire, J. Mol. Catal. B Enzym. 59(), 2009
Pire, J. Mol. Catal. B Enzym. 59(), 2009
Enzymatic dehydrogenation of testosterone coupled to pyruvate reduction in a two-phase system.
Cremonesi P, Carrea G, Ferrara L, Antonini E., Eur. J. Biochem. 44(2), 1974
PMID: 4365838
Cremonesi P, Carrea G, Ferrara L, Antonini E., Eur. J. Biochem. 44(2), 1974
PMID: 4365838
Preparation of 12-ketochenodeoxy- cholic acid from cholic acid using dehydrogenase and glutamate dehydrogenase with NADP+ cycling at high efficiency
Carrea, Enzym. Microb. Technol. 7(), 1985
Carrea, Enzym. Microb. Technol. 7(), 1985
Exploitation of the alcohol dehydrogenase-acetone NADP-regeneration system for the enzymatic preparative-scale production of 12-ketochenodeoxycholic acid.
Fossati E, Polentini F, Carrea G, Riva S., Biotechnol. Bioeng. 93(6), 2006
PMID: 16245351
Fossati E, Polentini F, Carrea G, Riva S., Biotechnol. Bioeng. 93(6), 2006
PMID: 16245351
Enzyme-mediated oxidations for the chemist
Hollmann, Green Chem. (), 2011
Hollmann, Green Chem. (), 2011
In search of sustainable chemical processes: cloning, recombinant expression, and functional characterization of the 7α- and 7β-hydroxysteroid dehydrogenases from Clostridium absonum
Ferrandi, Appl. Microbiol. Biotechnol. 95(), 2011
Ferrandi, Appl. Microbiol. Biotechnol. 95(), 2011
Molecular and enzymatic properties of 7α-hydroxysteroid dehydrogenase from Pseudomonas sp
Ueda, J. Biol. Macromol. (), 2004
Ueda, J. Biol. Macromol. (), 2004
Export
Markieren/ Markierung löschen
Markierte Publikationen
Web of Science
Dieser Datensatz im Web of Science®Quellen
PMID: 28193327
PubMed | Europe PMC
Suchen in
Google Scholar