Protein engineering of formate dehydrogenase

Biomolecular Engineering

Volumn 23, Issue 2-3, 2006, Pages 89-110

  Tishkov, Vladimir I ^a   Popov, Vladimir O ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

Author keywords

Candida boidinii; Formate dehydrogenase; Mutagenesis; Protein engineering; Pseudomonas sp.101; Stability

Indexed keywords

BACTERIA; ENZYMES; MOLECULAR BIOLOGY; MUTAGENESIS; OPTICAL PROPERTIES; PROTEINS; SYNTHESIS (CHEMICAL); THERMODYNAMIC STABILITY; YEAST;

CANDIDA BOIDINII; CHIRAL COMPOUNDS; LOW OPERATIONAL STABILITY; NADH REGENERATION; NATIVE FDHS; OPTICALLY ACTIVE COMPOUNDS; PRODUCTION COST;

DEHYDROGENATION;

BACTERIAL ENZYME; FORMATE DEHYDROGENASE; FUNGAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PHOSPHITE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; CANDIDA BOIDINII; CATALYSIS; CHIRALITY; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN STRUCTURE; PROTEOMICS; REVIEW; SYNTHESIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; BIOREACTORS; COENZYMES; ESCHERICHIA COLI; FORMATE DEHYDROGENASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; YEASTS;

BACTERIA (MICROORGANISMS); CANDIDA BOIDINII; ESCHERICHIA COLI; PSEUDOMONAS SP. 101;

EID: 33645409623     PISSN: 13890344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioeng.2006.02.003     Document Type: Review

References (114)

1. S.J. Allen, and J.J. Holbrook Isolation, sequence and overexpression of the gene encoding NAD-dependent formate dehydrogenase from the methylotrophic yeast Candida methylica Gene 162 1995 99 104
2. A. Angelov, O. Futterer, O. Valerius, G.H. Braus, and W. Liebl Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus FEBS J. 272 2005 1054 1062
3. T. Baba, F. Takeuchi, M. Kuroda, H. Yuzawa, K.-I. Aoki, A. Oguchi, Y. Nagai, N. Iwama, K. Asano, and T. Naimi Genome and virulence determinants of high virulence community-acquired MRSA Lancet 359 2002 1819 1827
4. M.J. Barnett, R.F. Fisher, T. Jones, C. Komp, A.P. Abola, F. Barloy-Hubler, L. Bowser, D. Capela, F. Galibert, J. Gouzy, M. Gurjal, A. Hong, L. Huizar, R.W. Hyman, D. Kahn, M.L. Kahn, S. Kalman, D.H. Keating, C. Palm, M.C. Peck, R. Surzycki, D.H. Wells, K.C. Yeh, R.W. Davis, N.A. Federspiel, and S.R. Long Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid Proc. Natl. Acad. Sci. U.S.A. 98 2001 9883 9888
5. O. Beja, L. Aravind, E.V. Koonin, M.T. Suzuki, A. Hadd, L.P. Nguyen, S.B. Jovanovich, C.M. Gates, R.A. Feldman, J.L. Spudich, E.N. Spudich, and E.F. DeLong Bacterial rhodopsin: evidence for a new type of phototrophy in the sea Science 289 2000 1902 1906
6. S.J. Berrios-Rivera, G.N. Bennett, and K.Y. San The effect of increasing NADH availability on the redistribution of metabolic fluxes in Escherichia coli chemostat cultures Metab. Eng. 4 2002 230 237
7. +-dependent formate dehydrogenase Metab. Eng. 4 2002 217 229
8. S.J. Berrios-Rivera, A.M. Sanchez, G.N. Bennett, and K.Y. San Effect of different levels of NADH availability on metabolite distribution in Escherichia coli fermentation in minimal and complex media Appl. Microbiol. Biotechnol. 65 2004 426 432
9. A.S. Bommarius, M. Schwarm, K. Stingl, M. Kottenhahn, K. Huthmacher, and K. Drauz Synthesis and use of enantiometrically pure tert-leucine Tetrahedron-Asymmetry 6 1995 2851 2888
10. M.J. Bonete, C. Pire, F.I. Lorca, and M.L. Camacho Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence FEBS Lett. 383 1996 227 229
11. J.R. Bright, D. Byrom, M.J. Danson, D.W. Hough, and P. Towner Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum Eur. J. Biochem. 211 1993 549 554
12. S.G. Burton Oxidizing enzymes as biocatalysts Trends Biotechnol. 21 2003 543 549
13. C. Cazalet, C. Rusniok, H. Bruggemann, N. Zidane, A. Magnier, L. Ma, M. Tichit, S. Jarraud, C. Bouchier, F. Vandenesch, F. Kunst, J. Etienne, P. Glaser, and C. Buchrieser Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity Nat. Genet. 36 2004 1165 1173
14. M. Chien, I. Morozova, S. Shi, H. Sheng, J. Chen, S.M. Gomez, G. Asamani, K. Hill, J. Nuara, M. Feder, J. Rineer, J.J. Greenberg, V. Steshenko, S.H. Park, B. Zhao, E. Teplitskaya, J.R. Edwards, S. Pampou, A. Georghiou, I.-C. Chou, W. Iannuccilli, M.E. Ulz, D.H. Kim, A. Geringer-Sameth, C. Goldsberry, P. Morozov, S.G. Fischer, G. Segal, X. Qu, A. Rzhetsky, P. Zhang, E. Cayanis, P.J. De Jong, J. Ju, S. Kalachikov, H.A. Shuman, and J.J. Russo The genomic sequence of the accidental pathogen Legionella pneumophila Science 305 2004 1966 1968
15. C. Colas des Francs-Small, F. Ambard-Bretteville, I.D. Small, and R. Rémy Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase Plant Physiol. 102 1993 1171 1177
16. A.M. Costas, A.K. White, and W.W. Metcalf Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88 J. Biol. Chem. 276 2001 17429 17436
17. D.C. Davidson Studies on plant formic dehydrogenase Biochem. J. 49 1951 520 526
18. A.P. Demchenko, O.I. Rusyn, A.M. Egorov, and V.I. Tishkov The solvent effects on the kinetics of bacterial formate dehydrogenase Biochim. Biophys. Acta 1039 1990 290 296
19. B. Dujon, D. Sherman, G. Fischer, P. Durrens, S. Casaregola, I. Lafontaine, J. De Montigny, C. Marck, C. Neuveglise, E. Talla, N. Goffard, L. Frangeul, M. Aigle, V. Anthouard, A. Babour, V. Barbe, S. Barnay, S. Blanchin, J.M. Beckerich, E. Beyne, C. Bleykasten, A. Boisrame, J. Boyer, L. Cattolico, F. Confanioleri, A. De Daruvar, L. Despons, E. Fabre, C. Fairhead, H. Ferry-Dumazet, A. Groppi, F. Hantraye, C. Hennequin, N. Jauniaux, P. Joyet, R. Kachouri, A. Kerrest, R. Koszul, M. Lemaire, I. Lesur, L. Ma, H. Muller, J.M. Nicaud, M. Nikolski, S. Oztas, O. Ozier-Kalogeropoulos, S. Pellenz, S. Potier, G.F. Richard, M.L. Straub, A. Suleau, D. Swennen, F. Tekaia, M. Wesolowski-Louvel, E. Westhof, B. Wirth, M. Zeniou-Meyer, I. Zivanovic, M. Bolotin-Fukuhara, A. Thierry, C. Bouchier, B. Caudron, C. Scarpelli, C. Gaillardin, J. Weissenbach, P. Wincker, and J.L. Souciet Genome evolution in yeasts Nature 430 2004 35 44
20. T. Endo, and S. Koizumi Microbial conversion with cofactor regeneration using genetically engineered bacteria Adv. Synth. Catal. 343 2001 521 526
21. M. Ernst, B. Kaup, M. Muller, S. Bringer-Meyer, and H. Sahm Enantioselective reduction of carbonyl compounds by whole-cell biotransformation, combining a formate dehydrogenase and a (R)-specific alcohol dehydrogenase Appl. Microbiol. Biotechnol. 66 2005 629 634
22. V.V. Fedorchuk, A.G. Galkin, I.E. Yasny, L.B. Kulakova, A.M. Rojkova, A.A. Filippova, and V.I. Tishkov Influence of interactions between amino acid residues 43 and 61 on thermal stability of bacterial formate dehydrogenases Biochemistry (Mosc.) 67 2002 1145 1151
23. Felber, S., 2001. Optimierung der NAD-abhängigen Formiatdehydrogenase aus Candida boidinii für den Einsatz in der Biokatalyse. Ph.D. Thesis. Heinrich-Heine University of Duesseldorf. URL: http://diss.ub.uni-duesseldorf.de/ebib/diss/file?dissid=78.
24. +-dependent formate dehydrogenase with a resolution of 2.1 Å Crystallogr. Rep. 50 2005 796 800
25. +-dependent formate dehydrogenase from Pseudomonas sp.101 in complex with formate Crystallogr. Rep. 51 2006 N2
26. A. Galkin, L. Kulakova, V. Tishkov, N. Esaki, and K. Soda Cloning of formate dehydrogenase gene from a methanol-utilizing bacterium Mycobacterium vaccae N10 Appl. Microbiol. Biotechnol. 44 1995 479 483
27. A. Galkin, L. Kulakova, T. Yoshimura, K. Soda, and N. Esaki Synthesis of optically active amino acids from alpha-keto acids with Escherichia coli cells expressing heterologous genes Appl. Environ. Microbiol. 63 1997 4651 4656
28. A. Galkin, L. Kulakova, H. Yamamoto, K. Tanizawa, H. Tanaka, N. Esaki, and K. Soda Conversion of alpha-keto acids to D-amino acids by coupling of four enzyme reactions J. Ferment. Bioeng. 83 1997 299 300
29. N. Gul-Karaguler, R.B. Sessions, A.R. Clarke, and J. Holbrook A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP Biotechnol. Lett. 23 2001 283 287
30. K. Hofstetter, J. Lutz, I. Lang, B. Witholt, and A. Schmid Coupling of biocatalytic asymmetric epoxidation with NADH regeneration in organic-aqueous emulsions Angew. Chem. Int. Ed. 43 2004 2163 2166
31. W. Hummel, and M.R. Kula Dehydrogenases for the synthesis of chiral compounds Eur. J. Biochem. 184 1989 1 13
32. L. Hwang, D. Hocking-Murray, A.K. Bahrami, M. Andersson, J. Rine, and A. Sil Identifying phase-specific genes in the fungal pathogen Histoplasma capsulatum using a genomic shotgun microarray Mol. Biol. Cell 14 2003 2314 2326
33. +-specific formate dehydrogenase from Pseudomonas sp.101. Product description. URL: http://www.innotech-msu.com/products/NADPFDH.pdf.
34. + and increased chemical and thermal stability (version PseFDH GAV) overexpressed in E. coli. Product description. URL: http://www.innotech- msu.com/products/NADFDHGAV.pdf.
35. T. Ishige, K. Honda, and S. Shimizu Whole organism biocatalysis Curr. Opin. Chem. Biol. 9 2005 174 180
36. T.W. Johannes, R.D. Woodyer, and H. Zhao Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration Appl. Environ. Microbiol. 71 2005 5728 5734
37. T. Jones, N.A. Federspiel, H. Chibana, J. Dungan, S. Kalman, B.B. Magee, G. Newport, Y.R. Thorstenson, N. Agabian, P.T. Magee, R.W. Davis, and S. Scherer The diploid genome sequence of Candida albicans Proc. Natl. Acad. Sci. U.S.A. 101 2004 7329 7334
38. Julich Fine Chemicals, 2005. Product Catalog.
39. N.G. Karaguler, R.B. Sessions, K.M. Moreton, A.R. Clarke, and J.J. Holbrook Estimating the energetic contribution of hydrogen bonding to the stability of Candida methylica formate dehydrogenase by using double mutant cycle Biotechnol. Lett. 26 2004 1137 1140
40. M. Kataoka, L.P. Rohani, K. Yamamoto, M. Wada, H. Kawabata, K. Kita, H. Yanase, and S. Shimizu Enzymatic production of ethyl (R)-4-chloro-3- hydroxybutanoate: asymmetric reduction of ethyl 4-chloro-3-oxobutanoate by an Escherichia coli transformant expressing the aldehyde reductase gene from yeast Appl. Microbiol. Biotechnol. 48 1997 699 703
41. M. Kataoka, K. Kita, M. Wada, Y. Yasohara, J. Hasegawa, and S. Shimizu Novel bioreduction system for the production of chiral alcohols Appl. Microbiol. Biotechnol. 62 2003 437 445
42. M. Kataoka, A. Kotaka, R. Thiwthong, M. Wada, S. Nakamori, and S. Shimizu Cloning and overexpression of the old yellow enzyme gene of Candida macedoniensis, and its application to the production of a chiral compound J. Biotechnol. 114 2004 1 9
43. B. Kaup, S. Bringer-Meyer, and H. Sahm Metabolic engineering of Escherichia coli: construction of an efficient biocatalyst for d-mannitol formation in a whole-cell biotransformation Appl. Microbiol. Biotechnol. 64 2004 333 339
44. M.-R. Kula, and C. Wandrey Continuous enzymatic transformation in an enzyme-membrane reactor with simultaneous NADH regeneration Methods Enzymol. 136 1987 9 21
45. + binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis Eur. J. Biochem. 267 2000 6657 6664
46. N.E. Labrou, and D.J. Rigden Active-site characterization of Candida boidinii formate dehydrogenase Biochem. J. 354 2001 455 463
47. V.S. Lamzin, Z. Dauter, V.O. Popov, E.H. Harutyunyan, and K.S. Wilson High resolution structures of holo and apo formate dehydrogenase J. Mol. Biol. 236 1994 759 785
48. V.S. Lamzin, Z. Dauter, and K.S. Wilson How nature deals with stereoisomers Curr. Opin. Struct. Biol. 5 1995 830 836
49. R.D. LaReau, and V.E. Anderson Lactate dehydrogenase displays absolute stereospecificity in the transfer of the prochiral hydrogen of NADH J. Biol. Chem. 264 1989 15338 15343
50. P. Larsson, P.C. Oyston, P. Chain, M.C. Chu, M. Duffield, H.H. Fuxelius, E. Garcia, G. Halltorp, D. Johansson, K.E. Isherwood, P.D. Karp, E. Larsson, Y. Liu, S. Michell, J. Prior, R. Prior, S. Malfatti, A. Sjostedt, K. Svensson, N. Thompson, L. Vergez, J.K. Wagg, B.W. Wren, L.E. Lindler, S.G. Andersson, M. Forsman, and R.W. Titball The complete genome sequence of Francisella tularensis, the causative agent of tularemia Nat. Genet. 37 2005 153 159
51. L. Li, J.P. Bannantine, Q. Zhang, A. Amonsin, B.J. May, D. Alt, N. Banerji, S. Kanjilal, and V. Kapur The complete genome sequence of Mycobacterium avium subspecies paratuberculosis Proc. Natl. Acad. Sci. U.S.A. 102 2005 12344 12349
52. A. Liese, and M. Villela Production of fine chemicals using biocatalysis Curr. Opin. Biotechnol. 10 1999 595 603
53. A. Liese Technical application of biological principles in asymmetric catalysis Adv. Biochem. Eng./Biotechnol. 92 2005 197 224
54. Y. Liu, Z. Xu, K. Jing, X. Jiang, J. Lin, F. Wang, and P. Cen Asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3- hydroxybutanoate with two co-existing, recombinant Escherichia coli strains Biotechnol. Lett. 27 2005 119 125
55. B.J. Loftus, E. Fung, P. Roncaglia, D. Rowley, P. Amedeo, D. Bruno, J. Vamathevan, M. Miranda, I.J. Anderson, J.A. Fraser, J.E. Allen, I.E. Bosdet, M.R. Brent, R. Chiu, T.L. Doering, M.J. Donlin, C.A. D'Souza, D.S. Fox, V. Grinberg, J. Fu, M. Fukushima, B.J. Haas, J.C. Huang, G. Janbon, S.J. Jones, H.L. Koo, M.I. Krzywinski, J.K. Kwon-Chung, K.B. Lengeler, R. Maiti, M.A. Marra, R.E. Marra, C.A. Mathewson, T.G. Mitchell, M. Pertea, F.R. Riggs, S.L. Salzberg, J.E. Schein, A. Shvartsbeyn, H. Shin, M. Shumway, C.A. Specht, B.B. Suh, A. Tenney, T.R. Utterback, B.L. Wickes, J.R. Wortman, N.H. Wye, J.W. Kronstad, J.K. Lodge, J. Heitman, R.W. Davis, C.M. Fraser, and R.W. Hyman The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans Science 307 2005 1321 1324
56. M.B. Mathews, and B. Vennesland Enzymic oxidation of formic acid J. Biol. Chem. 186 1950 667 682
57. + cofactor recycling system: towards a technical application of heme-containing monooxygenases in fine chemical synthesis Adv. Synth. Catal. 345 2003 802 810
58. S.C. Maurer, K. Kuehnel, L.A. Kaysser, S. Eiben, R.D. Schmid, and V.B. Urlacher Catalytic hydroxylation in biphasic systems using CYP102A1 mutants Adv. Synth. Catal. 347 2005 1090 1098
59. +-dependent formate dehydrogenase Biochem. J. 321 1997 475 480
60. Mitsunaga, T., Tanaka, Y., Yoshida, T., Watanabe, K., 2000. New Hyphomicrobium sp. formate dehydrogenase gene for producing formate dehydrogenase of high specific activity, high temperature stability and high pH stability. Patent of Japan JP245471A2, 12.09.2000.
61. T. Nagao, T. Mitamura, X.H. Wang, S. Negoro, T. Yomo, I. Urabe, and H. Okada Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isozymes from Bacillus megaterium IAM1030 J. Bacteriol. 174 1992 5013 5020
62. H. Nanba, Y. Takaoka, and J. Hasegawa Purification and characterization of an alpha-haloketone-resistant formate dehydrogenase from Thiobacillus sp. strain KNK65MA, and cloning of the gene Biosci. Biotechnol. Biochem. 67 2003 2145 2153
63. H. Nanba, Y. Takaoka, and J. Hasegawa Purification and characterization of formate dehydrogenase from Ancylobacter aquaticus strain KNK607M, and cloning of the gene Biosci. Biotechnol. Biochem. 67 2003 720 728
64. W. Neuhauser, M. Steininger, D. Haltrich, K.D. Kulbe, and B. Nidetzky A pH-controlled fed-batch process can overcome inhibition by formate in NADH-dependent enzymatic reductions using formate dehydrogenase-catalyzed coenzyme regeneration Biotechnol. Bioeng. 60 1998 277 282
65. E.R. Odintseva, A.S. Popova, A.M. Rojkova, and V.I. Tishkov Role of cysteine residues in stability of bacterial formate dehydrogenase Bull. Moscow Univ., Ser. 2 Chem. 43 2002 356 359
66. B.J. Olson, M. Skavdahl, H. Ramberg, J.C. Osterman, and J. Markwell Formate dehydrogenase in Arabidopsis thaliana: characterization and possible targeting to the chloroplast Plant Sci. 159 2000 205 212
67. S. Omura, H. Ikeda, J. Ishikawa, A. Hanamoto, C. Takahashi, M. Shinose, Y. Takahashi, H. Horikawa, H. Nakazawa, T. Osonoe, H. Kikuchi, T. Shiba, Y. Sakaki, and M. Hattori Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites Proc. Natl. Acad. Sci. U.S.A. 98 2001 12215 12220
68. J. Parkhill, M. Sebaihia, A. Preston, L.D. Murphy, N. Thomson, D.E. Harris, M.T.G. Holden, C.M. Churcher, S.D. Bentley, K.L. Mungall, A.M. Cerdeno-Tarraga, L. Temple, K. James, B. Harris, M.A. Quail, M. Achtman, R. Atkin, S. Baker, D. Basham, N. Bason, I. Cherevach, T. Chillingworth, M. Collins, A. Cronin, P. Davis, J. Doggett, T. Feltwell, A. Goble, N. Hamlin, H. Hauser, S. Holroyd, K. Jagels, S. Leather, S. Moule, H. Norberczak, S. O'Neil, D. Ormond, C. Price, E. Rabbinowitsch, S. Rutter, M. Sanders, D. Saunders, K. Seeger, S. Sharp, M. Simmonds, J. Skelton, R. Squares, S. Squares, K. Stevens, L. Unwin, S. Whitehead, B.G. Barrell, and D.J. Maskell Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica Nat. Genet. 35 2003 32 40
69. V.O. Popov, I.A. Shumilin, T.B. Ustinnikova, V.S. Lamzin, and Ts.A. Egorov NAD-dependent formate dehydrogenase from methylotrophic bacterium Pseudomonas sp.101. I. Amino acid sequence Bioorgan. Chem. 16 1990 324 335 (Russ.)
70. +-dependent formate dehydrogenase Biochem. J. 301 1994 625 643
71. +-dependent formate dehydrogenase. From a model enzyme to a versatile biocatalyst V.N. Uversky Protein Structures: Kaleidoscope of Structural Properties and Functions 2003 Research Signpost Kerala 441 473
72. H.A. Relyea, and W.A. van der Donk Mechanism and applications of phosphite dehydrogenase Bioorg. Chem. 33 2005 171 189
73. H.A. Relyea, J.M. Vrtis, R. Woodyer, S.A. Rimkus, and W.A. van der Donk Inhibition and pH dependence of phosphite dehydrogenase Biochemistry 44 2005 6640 6649
74. A. Resch, R. Rosenstein, C. Nerz, and F. Gotz Differential gene expression profiling of Staphylococcus aureus cultivated under biofilm and planktonic conditions Appl. Environ. Microbiol. 71 2005 2663 2676
75. S. Rissom, U. Schwarz-Linek, M. Vogel, V.I. Tishkov, and U. Kragl Synthesis of chiral epsilon-lactones in a two-enzyme system of cyclohexanone mono-oxygenase and formate dehydrogenase with integrated bubble-free aeration Tetrahedron-Asymmetry 8 1997 2523 2526
76. A.M. Rojkova, A.G. Galkin, L.B. Kulakova, A.E. Serov, P.A. Savitsky, V.V. Fedorchuk, and V.I. Tishkov Bacterial formate dehydrogenase. Increasing the enzyme thermal stability by hydrophobization of alpha helices FEBS Lett. 445 1999 183 188
77. Rozzell, J.D., Hua, L., Mayhew, M., Novick, S., 2004. Mutants of enzymes and methods for their use. US Patent Application Publication US2004/0115691, 17.06.2004.
78. E.G. Sadykhov, A.E. Serov, N.S. Voinova, S.V. Uglanova, A.S. Petrov, A.A. Alexeeva, S.Yu. Kleimenov, V.O. Popov, and V.I. Tishkov Comparable study of thermal stability of formate dehydrogenases from microorganisms and plants Appl. Biochem. Microbiol. 42 2006 N3
79. Y. Sakai, A.P. Murdanoto, T. Konishi, A. Iwamatsu, and N. Kato Regulation of the formate dehydrogenase gene, FDH1, in the methylotrophic yeast Candida boidinii and growth characteristics of an FDH1-disrupted strain on methanol, methylamine, and choline J. Bacteriol. 179 1997 4480 4485
80. J.A. Saleeba, C.S. Cobbett, and M.J. Hynes Characterization of the amdA-regulated aciA gene of Aspergillus nidulans Mol. Gen. Genet. 235 1992 349 358
81. K.Y. San, G.N. Bennett, S.J. Berrios-Rivera, R.V. Vadali, Y.T. Yang, E. Horton, F.B. Rudolph, B. Sariyar, and K. Blackwood Metabolic engineering through cofactor manipulation and its effects on metabolic flux redistribution in Escherichia coli Metab. Eng. 4 2002 182 192
82. A.M. Sanchez, G.N. Bennett, and K.Y. San Effect of different levels of NADH availability on metabolic fluxes of Escherichia coli chemostat cultures in defined medium J. Biotechnol. 117 2005 395 405
83. U. Schwarz-Linek, A. Krodel, F.A. Ludwig, A. Schulze, S. Rissom, U. Kragl, V.I. Tishkov, and M. Vogel Synthesis of natural product precursors by Baeyer-Villiger oxidation with cyclohexanone monooxygenase from Acinetobacter Synthesis-Stuttgart 33 2001 947 951
84. K. Seelbach, B. Riebel, W. Hummel, M.-R. Kula, V.I. Tishkov, A.M. Egorov, C. Wandrey, and U. Kragl A novel, efficient regenerating method of NADPH using a new formate dehydrogenase Tetrahedron Lett. 37 1996 1377 1380
85. A.E. Serov, A.S. Popova, V.V. Fedorchuk, and V.I. Tishkov Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae Biochem. J. 367 2002 841 847
86. Serov, A.E., 2002. Structure-function relationship in recombinant formate dehydrogenases from baker's yeast and methylotrophic bacterium. Ph.D. Thesis. M.V. Lomonosov Moscow State University, Moscow, Russian Federation.
87. A.E. Serov, and V.I. Tishkov Role of Pro residues in stability of prokaryotic and euacaryotic formate dehydrogenases Bull. Moscow Univ., Ser. 2 Chem. 43 2002 345 349
88. A.E. Serov, E.R. Odintzeva, I.V. Uporov, and V.I. Tishkov Use of Ramachandran plot for increasing thermal stability of bacterial formate dehydrogenase Biochemistry (Mosc.) 70 2005 804 808
89. Z. Shaked, and G.M. Whitesides Enzyme-catalyzed organic synthesis: NADH regeneration by using FDH J. Am. Chem. Soc. 102 1980 7104 7105
90. T. Shinoda, T. Satoh, S. Mineki, M. Iida, and H. Taguchi Cloning, nucleotide sequencing, and expression in Escherichia coli of the gene for formate dehydrogenase of Paracoccus sp.12-A, a formate-assimilating bacterium Biosci. Biotechnol. Biochem. 66 2002 271 276
91. T. Shinoda, K. Arai, M. Shigematsu-Iida, Y. Ishikura, S. Tanaka, T. Yamada, M.S. Kimber, E.F. Pai, S. Fushinobu, and H. Taguchi Distinct conformation-mediated functions of an active site loop in the catalytic reactions of NAD-dependent d-lactate dehydrogenase and formate dehydrogenase J. Biol. Chem. 280 2005 17068 17075
92. Schirwitz, K., Schmidt, A., Lamzin, V.S., 2005. Site-directed mutagenesis and high-resolution structures of Candida boidinii formate dehydrogenase. HASYLAB Annual Report, DESY, Hamburg. http://www-hasylab.desy.de/science/ annual_reports/2005_report/part2/contrib/72/14698.pdf.
93. H. Slusarczyk, S. Felber, M.R. Kula, and M. Pohl Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues Eur. J. Biochem. 267 2000 1280 1289
94. Slusarczyk, H., Felber, S., Kula, M.-R., Pohl, M., 2003. Novel mutants of formate dehydrogenase from Candida boidinii. US Patent Application Publication US2003/0157664, 21.09.2003.
95. V.I. Tishkov, A.G. Galkin, and A.M. Egorov NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp.101: cloning, expression, and study of the gene structure Dokl. Akad. Nauk SSSR 317 1991 745 748
96. V.I. Tishkov, A.G. Galkin, G.N. Marchenko, O.A. Egorova, D.V. Sheluho, L.B. Kulakova, L.A. Dementieva, and A.M. Egorov Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements Biochem. Biophys. Res. Commun. 192 1993 976 981
97. +-specific formate dehydrogenases Biotechnol. Bioeng. 64 1999 187 193
98. V.I. Tishkov, and V.O. Popov Catalytic mechanism and application of formate dehydrogenase Biochemistry (Mosc.) 69 2004 1252 1267
99. V.B. Urlacher, and R.D. Schmid Protein engineering of the cytochrome P450 monooxygenase from Bacillus megaterium Methods Enzymol. 388 2004 208 224
100. V.B. Urlacher, A. Makhsumkhanov, and R.D. Schmid Biotransformation of beta-ionone by engineered cytochrome P450 BM-3 Appl. Microbiol. Biotechnol 2005 Published online: July 7, 2005
101. W.A. van der Donk, and H.M. Zhao Recent developments in pyridine nucleotide regeneration Curr. Opin. Biotechnol. 14 2003 421 426
102. C. Vinals, E. Depiereux, and E. Feytmans Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase Biochem. Biophys. Res. Commun. 192 1993 182 188
103. J.M. Vrtis, A.K. White, W.W. Metcalf, and W.A. van der Donk Phosphite dehydrogenase: versatile cofactor-regeneration enzyme Angew. Chem. Int. Ed. Engl. 41 2002 3257 3259
104. M. Wada, A. Yoshizumi, Y. Noda, M. Kataoka, S. Shimizu, H. Takagi, and S. Nakamori Production of a doubly chiral compound (4R,6R)-4-hydroxy-2,2,6- trimethylcyclohexanone, by two-step enzymatic asymmetric reduction Appl. Environ. Microbiol. 69 2003 933 937
105. P.A. Weerasinghe, M.L.M.C. Weerasekera, and L.H.J. van Holm Use of isoenzymes to differentiate growth categories of Pericopsis mooniana trees Biol. Plant. 42 1999 41 547
106. E.G. Weinhold, A. Glasfeld, A.D. Ellington, and S.A. Benner Structural determinants of stereospecificity in yeast alcohol dehydrogenase Proc. Natl. Acad. Sci. U.S.A. 88 1991 8420 8424
107. D. Weuster-Botz, H. Paschold, B. Striegel, H. Gieren, M.-R. Kula, and C. Wandrey Continuous computer controlled production of formate dehydrogenase (FDH) and isolation on a pilot scale Chem. Eng. Technol. 17 1994 131 137
108. R. Wichmann, C. Wandrey, A.F. Buckmann, and M.R. Kula Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration Biotechnol. Bioeng. 23 1981 2789 2802
109. R. Wichmann, and D. Vasic-Racki Cofactor regeneration at the lab scale Adv. Biochem. Eng./Biotechnol. 92 2005 225 260
110. R. Woodyer, W.A. van der Donk, and H. Zhao Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design Biochemistry 42 2003 11604 11614
111. R. Woodyer, H. Zhao, and W.A. van der Donk Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration FEBS J. 72 2005 3816 3827
112. Z. Xu, Y. Liu, L. Fang, X. Jiang, K. Jing, and P. Cen Construction of a two-strain system for asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to (S)-4-chloro-3-hydroxybutanoate ethyl ester Appl. Microbiol. Biotechnol. 2005 Published on-line: September 21, 2005
113. H. Yamamoto, K. Mitsuhashi, N. Kimoto, Y. Kobayashi, and N. Esaki Robust NADH-regenerator: improved alpha-haloketone-resistant formate dehydrogenase Appl. Microbiol. Biotechnol. 67 2005 33 39
114. H. Yun, H.L. Choi, N.W. Fadnavis, and B.G. Kim Stereospecific synthesis of (R)-2-hydroxy carboxylic acids using recombinant E. coli BL21 overexpressing YiaE from Escherichia coli K12 and glucose dehydrogenase from Bacillus subtilis Biotechnol. Prog. 21 2005 366 371