A highly specific glyoxylate reductase derived from a formate dehydrogenase

Biochemical and Biophysical Research Communications

Volumn 355, Issue 3, 2007, Pages 782-787

  Shinoda, Takeshi ^a   Arai, Kazuhito ^a   Taguchi, Hayao ^a  

^a TOKYO UNIVERSITY OF SCIENCE   (Japan)

Author keywords

2 Hydroxyacid dehydrogenase; Formate dehydrogenase; Glyoxylate reductase; Lactate dehydrogenase

Indexed keywords

2 OXOACID; FORMATE DEHYDROGENASE; GLUTAMIC ACID; GLYOXYLIC ACID; HISTIDINE; OXIDOREDUCTASE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIUM MUTANT; ENZYME ACTIVITY; ENZYME MECHANISM; NONHUMAN; OXIDATION; PARACOCCUS; PH; PRIORITY JOURNAL;

ALCOHOL OXIDOREDUCTASES; AMINO ACID SUBSTITUTION; CATALYSIS; CATALYTIC DOMAIN; FORMATE DEHYDROGENASES; GLYOXYLATES; HYDROGEN-ION CONCENTRATION; MUTATION; OXIDATION-REDUCTION; PARACOCCUS;

PARACOCCUS SP. 12-A;

EID: 33847265304     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.02.027     Document Type: Article

References (35)

1. Grant G.A. A new family of 2-hydroxyacid dehydrogenases. Biochem. Biophys. Res. Commun. 165 (1989) 1371-1374
2. Taguchi H., and Ohta T. d-Lactate dehydrogenase is a member of the d-isomer-specific 2-hydroxyacid dehydrogenase family. J. Biol. Chem. 266 (1991) 12588-12594
3. Hummel W., Schütte H., and Kula M.R. d-2-Hydroxyisocaproate dehydrogenase from Lactobacillus casei. A new enzyme suitable for stereospecific reduction of 2-ketocarboxylic acids. Appl. Microbiol. Biotechnol. 21 (1985) 7-15
4. Goldberg J.D., Yoshida T., and Brick P. Crystal structure of an NAD-dependent d-glycerate dehydrogenase at 2.4 Å resolution. J. Mol. Biol. 236 (1994) 1123-1140
5. Arthur M., Molinas C., Dutka-Malen S., and Courvalin P. Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid dehydrogenases. Gene 103 (1991) 133-134
6. Ohshima T., Nunoura-Kominato N., Kudome T., and Sakurabe H. A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene cloning, nucleotide sequence and expression in Escherichia coli. Eur. J. Biochem. 268 (2001) 4740-4747
7. Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T., and Chinnadurai G. Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation. Proc. Natl. Acad. Sci. USA 92 (1995) 10467-10471
8. Tokuda C., Ishikura Y., Shigematsu M., Mutoh H., Tsuzuki S., Nakahira Y., Tamura Y., Shinoda T., and Taguchi H. Conversion of Lactobacillus pentosus d-lactate dehydrogenase through a single amino acid replacement. J. Bacteriol. 185 (2003) 5023-5026
9. Ishikura Y., Tsuzuki S., Takahashi O., Tokuda C., Nakanishi R., Shinoda T., and Taguchi H. Recognition site for the side chain of 2-ketoacid substrate in d-lactate dehydrogenase. J. Biochem. 138 (2005) 741-749
10. Taguchi H., and Ohta T. Histidine 296 is essential for the catalysis in Lactobacillus plantarum d-lactate dehydrogenase. J. Biol. Chem. 268 (1993) 18030-18034
11. Schuller D.J., Grant G.A., and Banaszak L.J. Allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 2 (1995) 68-76
12. Stoll V.S., Kimber M.S., and Pai E.F. Insights into substrate binding by d-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus d-lactate dehydrogenase. Structure (Current Biol.) 4 (1996) 437-447
13. + and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640-660
14. Razeto A., Kochhar S., Hottinger H., Dauter M., Wilson K.S., and Lamzin V.S. Domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from Lactobacillus bulgaricus. J. Mol. Biol. 318 (2002) 109-119
15. Kumar V., Carlson J.E., Ohgi K.A., Edwards T.A., Rose D.W., Escalante C.R., Rosenfeld M.G., and Aggarwal A.K. Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase. Mol. Cell 10 (2002) 857-869
16. Blow D.M., Birktoft J.J., and Hartley B.S. Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221 (1969) 337-340
17. Dijkstra B.W., Drenth J., and Kalk K.H. Active site and catalytic mechanism of phospholipase A2. Nature 289 (1981) 604-606
18. Birktoft J.J., and Banaszak L.J. The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase. J. Biol. Chem. 258 (1983) 472-482
19. Carter P., and Wells J.A. Dissecting the catalytic triad of a serine protease. Nature 332 (1988) 564-568
20. Clarke A.R., Wilks H.M., Barstow D.A., Atokinson T., Chia W.N., and Holbrook J.J. An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase. Biochemistry 27 (1988) 1617-1622
21. +-dependent d-lactate dehydrogenase. J. Biol. Chem. 267 (1992) 20298-20301
22. Taguchi H., Ohta T., and Matsuzawa H. Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for d-lactate dehydrogenase. J. Biochem. 122 (1997) 802-809
23. +-dependent formate dehydrogenase. J. Biochem. 301 (1994) 625-643
24. Tishkov V.I., and Popov V.O. Catalytic mechanism and application of formate dehydrogenase. Biochemistry (Moscow) 69 (2004) 1252-1267
25. Tishkov V.I., and Popov V.O. Protein engineering of formate dehydrogenase. Biomol. Eng. 23 (2006) 89-110
26. Baker P.J., Sawa Y., Shibata H., Sedelnikova S.E., and Rice D.W. Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat. Struct. Biol. 5 (1998) 561-567
27. Costas A.M.G., White A.K., and Metcalf W.W. Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88. J. Biol. Chem. 276 (2001) 17429-17436
28. Shinoda T., Arai K., Shigematsu-Iida M., Ishikura Y., Tanaka S., Yamada T., Kimber M.S., Pai E.F., Fushinobu S., and Taguchi H. 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
29. Tishkov V.I., Matorin A.D., Rojkova A.M., Fedorchuk V.V., Savisky P.A., Dementieve L.A., Lamzin V.S., Mezentzev A.V., and Popov V.O. Site-directed mutagenesis of the formate dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysis. FEBS Lett. 390 (1996) 104-108
30. Labrou N.E., and Rigden D.J. Active-site characterization of Candida boidinii formate dehydrogenase. Biochem. J. 354 (2001) 455-463
31. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 742 (1977) 5463-5467
32. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
33. Lamzin V.S., Dauter Z., Popov V.O., Harutyunyan E.H., and Wilson K.S. High resolution structure of holo and apo formate dehydrogenases. J. Mol. Biol. 236 (1994) 759-785
34. Fersht A.R. Enzyme Structure and Mechanism (1977), W. H. Freeman, San Francisco 95-96 (Chapter 3)
35. Holbrook J.J., Liljas A., Steindel S.J., and Rossmann M.G. Lactate dehydrogenase. In: Boyer P.D. (Ed). The Enzymes. third ed. vol. 11 (1975), Academic Press, New York 191-292