In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed

FEBS Letters

Volumn 588, Issue 17, 2014, Pages 2993-2999

  Ochsner, Andrea M ^a   Müller, Jonas E N ^a   Mora, Carlos A ^a   Vorholt, Julia A ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Alcohol dehydrogenase; Bacillus methanolicus; Methylotrophy

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE TYPE III; METHANOL; NICOTINAMIDE ADENINE DINUCLEOTIDE; NUDIX HYDROLASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS; BACILLUS METHANOLICUS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; IN VITRO STUDY; METHYLOTROPHIC BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

BACILLUS METHANOLICUS; POSIBACTERIA;

ALCOHOL DEHYDROGENASE; BACILLUS METHANOLICUS; METHYLOTROPHY;

ALCOHOL OXIDOREDUCTASES; BACTERIA; CATALYTIC DOMAIN; ENZYME ACTIVATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; NAD; PYROPHOSPHATASES; SPECIES SPECIFICITY;

EID: 84906246256     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.06.008     Document Type: Article

References (24)

1. C. Anthony, and P. Williams The structure and mechanism of methanol dehydrogenase Biochim. Biophys. Acta 1647 2003 18 23
2. L. Chistoserdova Modularity of methylotrophy, revisited Environ. Microbiol. 13 2011 2603 2622
3. T.M. Heggeset, A. Krog, S. Balzer, A. Wentzel, T.E. Ellingsen, and T. Brautaset Genome sequence of thermotolerant Bacillus methanolicus: features and regulation related to methylotrophy and production of l-lysine and L-glutamate from methanol Appl. Environ. Microbiol. 78 2012 5170 5181
4. J.E. Muller, B. Litsanov, M. Bortfeld-Miller, C. Trachsel, J. Grossmann, T. Brautaset, and J.A. Vorholt Proteomic analysis of the thermophilic methylotroph Bacillus methanolicus MGA3 Proteomics 14 2014 725 737
5. + dependent methanol dehydrogenase paralogs with different catalytic and biochemical properties PLoS One 8 2013 e59188
6. J. Vonck, N. Arfman, G.E. De Vries, J. Van Beeumen, E.F. Van Bruggen, and L. Dijkhuizen Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1 J. Biol. Chem. 266 1991 3949 3954
7. N. Arfman, H.J. Hektor, L.V. Bystrykh, N.I. Govorukhina, L. Dijkhuizen, and J. Frank Properties of an NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus Eur. J. Biochem. 244 1997 426 433
8. N. Arfman, J. Van Beeumen, G.E. De Vries, W. Harder, and L. Dijkhuizen Purification and characterization of an activator protein for methanol dehydrogenase from thermotolerant Bacillus spp J. Biol. Chem. 266 1991 3955 3960
9. A.G. McLennan The Nudix hydrolase superfamily Cell. Mol. Life Sci. 63 2006 123 143
10. A.S. Mildvan, Z. Xia, H.F. Azurmendi, V. Saraswat, P.M. Legler, M.A. Massiah, S.B. Gabelli, M.A. Bianchet, L.W. Kang, and L.M. Amzel Structures and mechanisms of Nudix hydrolases Arch. Biochem. Biophys. 433 2005 129 143
11. H. Kloosterman, J.W. Vrijbloed, and L. Dijkhuizen Molecular, biochemical, and functional characterization of a Nudix hydrolase protein that stimulates the activity of a nicotinoprotein alcohol dehydrogenase J. Biol. Chem. 277 2002 34785 34792
12. H.J. Hektor, H. Kloosterman, and L. Dijkhuizen Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus J. Biol. Chem. 277 2002 46966 46973
13. R. Silva-Rocha, E. Martinez-Garcia, B. Calles, M. Chavarria, A. Arce-Rodriguez, A. de Las Heras, A.D. Paez-Espino, G. Durante-Rodriguez, J. Kim, P.I. Nikel, R. Platero, and V. de Lorenzo The Standard European Vector Architecture (SEVA): a coherent platform for the analysis and deployment of complex prokaryotic phenotypes Nucleic Acids Res. 41 2013 D666 D675
14. M. Kitagawa, T. Ara, M. Arifuzzaman, T. Ioka-Nakamichi, E. Inamoto, H. Toyonaga, and H. Mori Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research DNA Res. 12 2005 291 299
15. J. Haas, S. Roth, K. Arnold, F. Kiefer, T. Schmidt, L. Bordoli, and T. Schwede The Protein Model Portal - a comprehensive resource for protein structure and model information Database 2013 2013, bat031
16. N. Fernandez-Fuentes, C.J. Madrid-Aliste, B.K. Rai, J.E. Fajardo, and A. Fiser M4T: a comparative protein structure modeling server Nucleic Acids Res. 35 2007 W363 W368
17. T.A. Hall BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT Nucleic Acids Symp Ser. 41 1999 95 98
18. B. Markert, J. Stolzenberger, T. Brautaset, and V.F. Wendisch Characterization of two transketolases encoded on the chromosome and the plasmid pBM19 of the facultative ribulose monophosphate cycle methylotroph Bacillus methanolicus BMC Microbiol. 14 2014 7
19. J. Stolzenberger, S.N. Lindner, M. Persicke, T. Brautaset, and V.F. Wendisch Characterization of fructose 1,6-bisphosphatase and sedoheptulose 1,7-bisphosphatase from the facultative ribulose monophosphate cycle methylotroph Bacillus methanolicus J. Bacteriol. 195 2013 5112 5122
20. T Stand Genomic Sci. 8 2013 69 87
21. M.F. Reid, and C.A. Fewson Molecular characterization of microbial alcohol dehydrogenases Crit. Rev. Microbiol. 20 1994 13 56
22. S.F. O'Handley, D.N. Frick, C.A. Dunn, and M.J. Bessman Orf186 represents a new member of the Nudix hydrolases, active on adenosine(5')triphospho(5') adenosine, ADP-ribose, and NADH J. Biol. Chem. 273 1998 3192 3197
23. C. Montella, L. Bellsolell, R. Perez-Luque, J. Badia, L. Baldoma, M. Coll, and J. Aguilar Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli J. Bacteriol. 187 2005 4957 4966
24. K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 28 2011 2731 2739