Inhibition and pH dependence of phosphite dehydrogenase

Biochemistry

Volumn 44, Issue 17, 2005, Pages 6640-6649

  Relyea, Heather A ^a   Vrtis, Jennifer M ^a   Woodyer, Ryan ^a   Rimkus, Stacey A ^a   Van Der Donk, Wilfred A ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; HYDRIDES; NEGATIVE IONS; ORGANIC ACIDS; OXIDATION; PH EFFECTS;

D-HYDROXY ACID DEHYDROGENASES; DIANIONS; PHOSPHITE DEHYDROGENASE (PTDH); REVERSE PROTONATION;

BIOCHEMISTRY;

OXIDOREDUCTASE; PHOSPHITE;

ARTICLE; CANDIDA BOIDINII; CATALYSIS; CONTROLLED STUDY; HYPHOMICROBIUM; LACTOBACILLUS; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; PH MEASUREMENT; PRIORITY JOURNAL; THERMODYNAMICS; TITRIMETRY;

AMINO ACID SEQUENCE; BINDING, COMPETITIVE; CATALYSIS; DEUTERIUM EXCHANGE MEASUREMENT; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; NAD; NADH, NADPH OXIDOREDUCTASES; PHOSPHITES; PROTEIN BINDING; SOLVENTS; SUBSTRATE SPECIFICITY; SULFITES;

FELIS CATUS;

EID: 15444369597     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047640p     Document Type: Article

References (59)

1. Metcalf, W. W., and Wolfe, R. S. (1998) Molecular genetic analysis of phosphite and hypophosphite oxidation by Pseudomonas stutzeri WM88, J. Bacteriol. 180, 5547-5558.
2. Costas, A. M., White, A. K., and Metcalf, W. W. (2001) Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88, J. Biol. Chem. 276, 17429-17436.
3. Vrtis, J. M., White, A., Metcalf, W. W., and van der Donk, W. A. (2001) Phosphite Dehydrogenase: An unusual Phosphoryl Transfer Reaction, J. Am. Chem. Soc. 123, 2672-2673.
4. Taguchi, H., and Ohta, T. (1991) D-Lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum, J. Biol. Chem. 266, 12588-12594.
5. Taguchi, H., and Ohta, T. (1993) Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase, J. Biol. Chem. 268, 18030-18034.
6. +-dependent D-lactate dehydrogenase, J. Biol. Chem. 267, 20298-20301.
7. Goldberg, J. D., Yoshida, T., and Brick, P. (1994) Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution, J. Mol. Biol. 236, 1123-1140.
8. +-specific D-lactate dehydrogenase, Eur. J. Biochem. 267, 1633-1639.
9. Woodyer, R., Wheatley, J., Relyea, H., Rimkus, S., and van der Donk, W. A. (2005) Site-Directed Mutagenesis of Active Site Residues of Phosphite Dehydrogenase, Biochemistry 44, 4765-4774.
10. Woodyer, R., van der Donk, W. A., and Zhao, H. (2003) Relaxing the Nicotinamide Cofactor Specificity of Phosphite Dehydrogenase by Rational Design, Biochemistry 42, 11604-11614.
11. +-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site, J. Biol. Chem. 267, 8499-8513.
12. Schütte, H., Flossdorf, J., Sahm, H., and Kula, M. R. (1976) Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii, Eur. J. Biochem. 62, 151-160.
13. Walsh, D. A., and Sallach, H. J. (1965) Purification and properties of chicken liver D-3-phosphoglycerate dehydrogenase, Biochemistry 4, 1076-1085.
14. Ellis, K. J., and Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes, Methods Enzymol. 87, 405-426.
15. Cleland, W. W. (1982) The use of pH studies to determine chemical mechanisms of enzyme-catalyzed reactions, Methods Enzymol. 87, 390-405.
16. Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies, Adv. Enzymol. 45, 273-387.
17. Fritzsche, T. M., McIntyre, J. O., Fleischer, S., and Trommer, W. E. (1984) Complex formation between nucleotides and D-β-hydroxybutyrate dehydrogenase studied by fluorescence and EPR spectroscopy, Biochim. Biophys. Acta 791, 173-185.
18. Glasoe, P. K., and Long, F. A. (1960) Use of Glass Electrodes to Measure Acidities in Deuterium Oxide, J. Phys. Chem. 64, 188-191.
19. Dawson, R., Elliott, D., Elliott, W., and Jones, K. (1986) Data for Biochemical Research, 3rd ed., Oxford University Press, Oxford, U.K.
20. Robertson, J. G. (1979) KinetAsyst, Intellikinetics, State College, PA.
21. Cleland, W. W. (1979) Statistical Analysis of Enzyme Kinetic Data, Methods Enzymol. 63, 103-138.
22. Quinn, D. M., and Sutton, L. D. (1991) in Enzyme Mechanism from Isotope Effects (Cook, P. R., Ed.) pp 73-126, CRC Press, Boca Raton, FL.
23. Lakowicz, J. R. (1999) Principles of Fluorescence Spectroscopy, Kluwer Academic/Plenum, New York.
24. Seto, H., and Kuzuyama, T. (1999) Bioactive Natural Products with Carbon-Phosphorus Bonds and Their Biosynthesis, Nat. Prod. Rep. 16, 589-596.
25. Willems, H. A. M., Veeneman, G. H., and Westerduin, P. (1992) Synthesis of Racemic Myoinositol 1,4,5-Trismethylphosphonate, Myoinositol 4,5-Bismethylphosphonate and Myoinositol 5-Methylphosphonate Via a Phosphinate Approach, Tetrahedron Lett. 33, 2075-2078.
26. Seeberger, P. H., Jorgensen, P. N., Bankaitis-Davis, D. M., Beaton, G., and Caruthers, M. H. (1996) 5′-Dithiophosphoryl deoxyoligonucleotides: Synthesis and biological studies, J. Am. Chem. Soc. 118, 9562-9566.
27. Gerrard, A. F., and Hamer, N. K. (1968) Evidence for a Planar Intermediate in Alkaline Solvolysis of Methyl N-Cyclohexylphosphoramidothioic Chloride, J. Chem. Soc. B, 539-543.
28. Cullis, P. M., and Iagrossi, A. (1986) Thiophosphoryl-Transfer Reactions: Stereochemical Course of Solvolysis of p-Nitrophenyl Thiophosphate in Protic solvent and the Possible Role of Thiometaphosphate, J. Am. Chem. Soc. 108, 7870-7871.
29. Cullis, P. M., Misra, R., and Wilkins, D. J. (1987) Free Monomeric Thiometaphosphate in Protic Solvents: Complete Racemisation at Phosphorus in the Ethanolysis of 4-Nitrophenyl Thiophosphate, J. Chem. Soc., Chem. Commun., 1594-1596.
30. Burgess, J., Blundell, N., Cullis, P. M., Hubbard, C. D., and Misra, R. (1988) Evidence for Free Monomeric Thiametaphosphate Anion in Aqueous Solution, J. Am. Chem. Soc. 110, 7900-7901.
31. Yang, Y. S., and Frey, P. A. (1990) Solvent Effects on the Solvolysis of ADPβS, Bioorg. Chem. 18, 373-380.
32. Banner, M. R., and Rosalki, S. B. (1967) Glyoxylate as a substrate for lactate dehydrogenase, Nature 213, 726-727.
33. Warren, W. A. (1970) Catalysis of both oxidation and reduction of glyoxylate by pig heart lactate dehydrogenase isozyme 1, J. Biol. Chem. 245, 1675-1681.
34. Lluis, C., and Bozal, J. (1977) Kinetic formulations for the oxidation and the reduction of glyoxylate by lactate dehydrogenase, Biochim. Biophys. Acta 480, 333-342.
35. Duncan, R. J., and Tipton, K. F. (1969) The oxidation and reduction of glyoxylate by lactic dehydrogenase, Eur. J. Biochem. 11, 58-61.
36. White, A. K., and Metcalf, W. W. (2004) The htx and ptx operons of Pseudomonas stutzeri WM88 are new members of the pho regulon, J. Bacteriol. 186, 5876-5882.
37. Pfeiderer, G., Jeckel, D., and Wieland, T. (1956) Action of sulfite on diphosphopyridine nucleotide (DPN) hydrogenating enzymes, Biochem. Z. 328, 187-194.
38. Carelli, V., Liberatore, F., Scipione, L., Musio, R., and Sciacovelli, O. (2000) On the structure of intermediate adducts arising from dithionite reduction of pyridinium salts: A novel class of derivatives of the parent sulfinic acid, Tetrahedron Lett. 41, 1235-1240.
39. Parker, D. M., Lodola, A., and Holbrook, J. J. (1978) Use of the sulphite adduct of nicotinamide-adenine dinucleotide to study ionizations and the kinetics of lactate dehydrogenase and malate dehydrogenase, Biochem. J. 173, 959-967.
40. Jencks, W. P. (1981) On the Attribution and Additivity of Binding Energies, Proc. Natl. Acad. Sci. U.S.A. 78, 4046-4050.
41. Jencks, W. P. (1975) Binding Energy, Specificity, and Enzymic Catalysis: The Circe Effect, Adv. Enzymol. 43, 219-410.
42. Lide, D. R. (1991) in CAC Handbook of Chemistry and Physics, CRC Press, Boca Raton, FL.
43. Fersht, A. (1985) Enzyme Structure and Mechanism, Freeman & Co., New York.
44. 18O isotope effects as a tool for studying reactions of phosphate mono-, di-, and triesters, FASEB J. 4, 2899-2905.
45. Williams, N. H. (2004) Models for biological phosphoryl transfer, Biochim. Biophys. Acta 1697, 279-287.
46. Northrop, D. B. (1977) in Isotope Effects on Enzyme-Catalyzed Reaction (Cleland, W. W., O'Leary, M. H., and Northrop, D. B., Eds.) pp 122-152, University Park Press, Baltimore.
47. Duggleby, R. G., and Northrop, D. B. (1989) The Expression of Kinetic Isotope Effects during the Time Course of Enzyme Catalyzed Reactions, Bioorg. Chem. 17, 177-193.
48. Martin, R. B. (1959) The Rate of Exchange of the Phosphorus Bonded Hydrogen in Phosphorous Acid, J. Am. Chem. Soc. 81, 1574-1576.
49. Schowen, K. B., and Schowen, R. L. (1982) Solvent isotope effects on enzyme systems, Methods Enzymol. 87, 551-606.
50. Salomaa, P., Hakala, R., Vesala, S., and Aalto, T. (1969) Solvent deuterium isotope effects on acid-base reactions. III. Relative acidity constants of inorganic oxyacids in light and heavy water. Kinetic applications, Acta Chem. Scand. 23, 2116-2126.
51. Relyea, H., and van der Donk, W. A. (2005) Mechanism and Applications of Phosphite Dehydrogenase, Bioorg. Chem. (in press).
52. Hermes, J. D., Roeske, C. A., O'Leary, M. H., and Cleland, W. W. (1982) Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase, Biochemistry 21, 5106-5114.
53. Belasco, J. G., Albery, W. J., and Knowles, J. R. (1983) Double isotope fractionation: Test for concertedness and for transition-state dominance, J. Am. Chem. Soc. 105, 2475-2477.
54. Taguchi, H., Ohta, T., and Matsuzawa, H. (1997) Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis, J. Biochem. 122, 802-809.
55. Taguchi, H., and Ohta, T. (1994) Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase, J. Biochem. 115, 930-936.
56. Yoshida, T., Yamaguchi, K., Hagishita, T., Mitsunaga, T., Miyata, A., Tanabe, T., Toh, H., Ohshiro, T., Shimao, M., and Izumi, Y. (1994) Cloning and expression of the gene for hydroxypyruvate reductase (D-glycerate dehydrogenase from an obligate methylotroph Hyphomicrobium methylovorum GM2), Eur. J. Biochem. 223, 727-732.
57. Tobey, K. L., and Grant, G. A. (1986) The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase, J. Biol. Chem. 261, 12179-12183.
58. Bernard, N., Ferain, T., Garmyn, D., Hols, P., and Delcour, J. (1991) Cloning of the D-lactate dehydrogenase gene from Lactobacillus delbrueckii subsp. bulgaricus by complementation in Escherichia coli, FEBS Lett. 290, 61-64.
59. Popov, V. O., Shumilin, I. A., Ustinnikova, T. B., Lamzin, V. S., and Egorov, Ts. A. (1990) NAD-dependent formate dehydrogenase from methylotrophic bacteria Pseudomonas sp. 101. I. Amino acid sequence, Bioorg. Khim. 16, 324-335.