Mechanistic investigation of a highly active phosphite dehydrogenase mutant and its application for NADPH regeneration

FEBS Journal

Volumn 272, Issue 15, 2005, Pages 3816-3827

  Woodyer, Ryan ^a   Zhao, Huimin ^a   Van Der Donk, Wilfred A ^a,b  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b Department of Chemistry ^*  (United States)

Author keywords

Biocatalysis; Cofactor regeneration; Dehydrogenases; Homology modelling; Site directed mutagenesis

Indexed keywords

ISOTOPE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHOSPHITE; PHOSPHITE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFITE; TRYPTOPHAN; UNCLASSIFIED DRUG; XYLOSE;

ARTICLE; BINDING AFFINITY; COMPARATIVE STUDY; DISSOCIATION CONSTANT; ENZYME BINDING; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; FLUORESCENCE; MUTANT; PRIORITY JOURNAL;

DEUTERIUM; ESCHERICHIA COLI PROTEINS; KINETICS; MUTATION; NAD; NADH, NADPH OXIDOREDUCTASES; NADP; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURAL HOMOLOGY, PROTEIN; TIME FACTORS; TRYPTOPHAN; XYLITOL;

PSEUDOMONAS SP. 101;

EID: 23644436972     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04788.x     Document Type: Article

References (59)

1. Zaks A (2001) Industrial biocatalysis. Curr Opin Chem Biol 5, 130-136.
2. Schmid A, Dordick JS, Hauer B, Kiener A, Wubbolts M & Witholt B (2001) Industrial biocatalysis today and tomorrow. Nature 409, 258-268.
3. Liese A & Filho MV (1999) Production of fine chemicals using biocatalysis. Curr Opin Biotechnol 10, 595-603.
4. Koeller KM & Wong CH (2001) Enzymes for chemical synthesis. Nature 409, 232-240.
5. Zhao H, Chockalingam K & Chen Z (2002) Directed evolution of enzymes and pathways for industrial biocatalysis. Curr Opin Biotechnol 13, 104-110.
6. Schoemaker HE, Mink D & Wubbolts MG (2003) Dispelling the myths - biocatalysis in industrial synthesis. Science 299, 1694-1697.
7. Hummel W (1999) Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol 17, 487-492.
8. Zhao H & van der Donk WA (2003) Regeneration of cofactors for use in biocatalysis. Curr Opin Biotechnol 14, 583-589.
9. van der Donk WA & Zhao H (2003) Recent developments in pyridine nucleotide regeneration. Curr Opin Biotechnol 14, 421-426.
10. Chenault HK, Simon ES & Whitesides GM (1988) Cofactor regeneration for enzyme-catalysed synthesis. Biotechnol Genet Eng Rev 6, 221-270.
11. Chenault HK & Whitesides GM (1987) Regeneration of nicotinamide cofactors for use in organic synthesis. Appl Biochem Biotechnol 14, 147-197.
12. Woodyer RD, Johannes TW & Zhao H (2005) Regeneration of cofactors for enzyme biocatalysis. In Enzyme Technology (Pandey A, Webb C, Soccol CS & Larroche C, eds), pp. 85-103. Asiatech Publishers Inc., New Delhi, India.
13. Berrios-Rivera SJ, Bennett GN & San KY (2002) Metabolic engineering of Escherichia coli: increase of NADH availability by overexpressing an NAD(+)-dependent formate dehydrogenase. Metab Eng 4, 217-229.
14. Leonida MD (2001) Redox enzymes used in chiral syntheses coupled to coenzyme regeneration. Curr Medical Chem 8, 345-369.
15. Woodyer R, van der Donk WA & Zhao H (2005) Optimizing a biocatalyst for improved NAD(P)H regeneration: Directed evolution of phosphite dehydrogenase. Comb Chem High Throughput Screening (in press).
16. Wagenknecht PS, Penney JM & Hembre RT (2003) Transition-metal- catalyzed regeneration of nicotinamide coenzymes with hydrogen. Organometallics 22, 1180-1182.
17. Tishkov VI, Galkin AG, Marchenko GN, Egorova OA, Sheluho DV, Kulakova LB, Dementieva LA & Egorov AM (1993) 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, 976-981.
18. Bommarius AS & Drauz K (1994) An enzymatic route to L-ornithine from arginine - activation, selectivity and stabilization of L-arginase. Bioorg Med Chem 2, 617-626.
19. McCoy M (2001) Making drugs with little bugs. Chem Engineer News 79, 37-43.
20. Carugo O & Argos P (1997) NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins 28, 10-28.
21. Costas AM, White AK & Metcalf WW (2001) Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88. J Biol Chem 276, 17429-17436.
22. Vrtis JM, White A, Metcalf WW & van der Donk WA (2002) Phosphite dehydrogenase, a new versatile cofactor regeneration enzyme. Angew Chem Int Ed Engl 41, 3257-3259.
23. Woodyer R, van der Donk WA & Zhao H (2003) Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design. Biochemistry 42, 11604-11614.
24. Nishiyama M, Birktoft JJ & Beppu T (1993) Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis. J Biol Chem 268, 4656-4660.
25. Wiegert T, Sahm H & Sprenger GA (1997) The substitution of a single amino acid residue (Ser-116?Asp) alters NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis into a glucose dehydrogenase with dual coenzyme specificity. J Biol Chem 272, 13126-13133.
26. Steen IH, Lien T, Madsen MS & Birkeland NK (2002) Identification of cofactor discrimination sites in NAD-isocitrate dehydrogenase from Pyrococcus furiosus. Arch Microbiol 178, 297-300.
27. Bocanegra JA, Scrutton NS & Perham RN (1993) Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering. Biochemistry 32, 2737-2740.
28. Zhang L, Ahvazi B, Szittner R, Vrielink A & Meighen E (1999) Change of nucleotide specificity and enhancement of catalytic efficiency in single point mutants of Vibrio harveyi aldehyde dehydrogenase. Biochemistry 38, 11440-11447.
29. Schepens I, Johansson K, Decottignies P, Gillibert M, Hirasawa M, Knaff DB & Miginiac-Maslow M (2000) Inhibition of the thioredoxin-dependent activation of the NADP-malate dehydrogenase and cofactor specificity. J Biol Chem 275, 20996-21001.
30. Nakanishi M, Matsuura K, Kaibe H, Tanaka N, Nonaka T, Mitsui Y & Hara A (1997) Switch of coenzyme specificity of mouse lung carbonyl reductase by substitution of threonine 38 with aspartic acid. J Biol Chem 272, 2218-2222.
31. Danielson UH, Jiang F, Hansson LO & Mannervik B (1999) Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site. Biochemistry 38, 9254-9263.
32. Galkin A, Kulakova L, Ohshima T, Esaki N & Soda K (1997) Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme. Protein Eng 10, 687-690.
33. Woodyer R, Simurdiak M, van der Donk WA & Zhao H (2005) Heterologous expression, purification and characterization of a highly active xylose reductase from Neurospora crassa. Appl Environ Microbiol 71, 1642-1647.
34. Relyea H & van der Donk WA (2005) Mechanism and applications of phosphite dehydrogenase. Bioorg Chem 33, 171-189.
35. Martin R (1959) The rate of exchange of the phosphorus bonded hydrogen in phosphorous acid. J Am Chem Soc 81, 1574-1576.
36. Vrtis JM, White AK, Metcalf WW & van der Donk WA (2001) Phosphite dehydrogenase: an unusual phosphoryl transfer reaction. J Am Chem Soc 123, 2672-2673.
37. Northrop DB (1977) Determining the absolute magnitude of hydrogen isotope effects. In Isotope Effects on Enzyme-Catalyzed Reaction (Cleland, W W, O'Leary, M H & Northrop, D B, eds), pp. 122-152. University Park Press, Baltimore, MD.
38. Duggleby RG & Northrop DB (1989) The expression of kinetic isotope effects during the time course of enzyme catalyzed reactions. Bioorg Chem 17, 177-193.
39. Cleland WW (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Adv Enzymol Relat Areas Mol Biol 45, 273-387.
40. Nidetzky B, Helmer H, Klimacek M, Lunzer R & Mayer G (2003) Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in Escherichia coli. Chem Biol Interact 143-144, 533-542.
41. Dunning Hotopp JC, Auchtung TA, Hogan DA & Hausinger RP (2003) Intrinsic tryptophan fluorescence as a probe of metal and alpha-ketoglutarate binding to TfdA, a mononuclear non-heme iron dioxygenase. J Inorg Biochem 93, 66-70.
42. Espinosa V, Kettlun AM, Zanocco A, Cardemil E & Valenzuela MA (2003) Differences in nucleotide-binding site of isoapyrases deduced from tryptophan fluorescence. Phytochemistry 63, 7-14.
43. Garnier C, Lafitte D, Tsvetkov PO, Barbier P, Leclerc-Devin J, Millot JM, Briand C, Makarov AA, Catelli MG & Peyrot V (2002) Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain. J Biol Chem 277, 12208-12214.
44. Hegde SS, Dam TK, Brewer CF & Blanchard JS (2002) Thermodynamics of aminoglycoside and acyl-coenzyme A binding to the Salmonella enterica AAC (6′)-Iy aminoglycoside N-acetyltransferase. Biochemistry 41, 7519-7527.
45. Liu J, Tian JN, Zhang J, Hu Z & Chen X (2003) Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study. Anal Bioanal Chem 376, 864-867.
46. Nagase T, Nakata E, Shinkai S & Hamachi I (2003) Construction of artificial signal transducers on a lectin surface by post-photoaffinity-labeling modification for fluorescent saccharide biosensors. Chemistry 9, 3660-3669.
47. Serov AE, Popova AS, Fedorchuk VV & Tishkov VI (2002) Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae. Biochem J 367, 841-847.
48. +/glucose cotransporter assessed by intrinsic tryptophan fluorescence. Biochemistry 42, 6115-6120.
49. Zang H & Gates KS (2000) DNA binding and alkylation by the 'left half' of azinomycin B. Biochemistry 39, 14968-14975.
50. Relyea HA, Vrtis JM, Woodyer R, Rimkus SA & van der Donk WA (2005) Inhibition and pH dependence of phosphite dehydrogenase. Biochemistry 44, 6640-6649.
51. Kitpreechavanich V, Nishio N, Hayashi M & Nagai S (1985) Regeneration and retention of NADP(H) for xylitol production in an ionized membrane reactor. Biotechnol Lett 7, 657-662.
52. Nidetzky B, Schmidt B, Neuhauser W, Haltrich D & Kulbe KD (1994) Application of charged ultrafiltration membranes in continuous, enzyme-catalyzed processes with coenzyme regeneration. In Separations for Biotechnology (Pyle, D L, ed.), pp. 351-357. Royal Society of Chemistry, London.
53. Nidetzky B, Neuhauser W, Haltrich D & Kulbe KD (1996) Continuous enzymatic production of xylitol with simultaneous coenzyme regeneration in a charged membrane reactor. Biotechnol Bioeng 52, 387-396.
54. Nidetzky B, Klimacek M & Mayr P (2001) Transient-state and steady-state kinetic studies of the mechanism of NADH-dependent aldehyde reduction catalyzed by xylose reductase from the yeast Candida tennis. Biochemistry 40, 10371-10381.
55. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
56. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
57. Robertson JG (1979) Kinetasyst. In Intellikinetics. State College, PA.
58. Cleland WW (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol 63, 103-138.
59. Lakowics JR (1999) Principles of Fluorescence Spectroscopy, 2nd edn. Kluwer Academic/Plenum, New York.