Thiolactomycin inhibits d-aspartate oxidase: A novel approach to probing the active site environment

Biochimie

Volumn 92, Issue 10, 2010, Pages 1371-1378

  Katane, Masumi ^a   Saitoh, Yasuaki ^a   Hanai, Toshihiko ^a   Sekine, Masae ^a   Furuchi, Takemitsu ^a   Koyama, Nobuhiro ^a   Nakagome, Izumi ^a   Tomoda, Hiroshi ^a   Hirono, Shuichi ^a   Homma, Hiroshi ^a  

^a KITASATO UNIVERSITY   (Japan)

Author keywords

Active site probe; D Amino acid oxidase; D Aspartate oxidase; Flavoprotein; Thiolactomycin

Indexed keywords

ASPARTATE OXIDASE; DEXTRO AMINO ACID OXIDASE; MALONIC ACID; TARTARIC ACID; THIOLACTOMYCIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; COENZYME; COMPETITIVE INHIBITION; CONTROLLED STUDY; DRUG BINDING SITE; DRUG PROTEIN BINDING; DRUG SCREENING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; HUMAN; HUMAN CELL; MALE; MOUSE; NONHUMAN; SITE DIRECTED MUTAGENESIS;

ANIMALS; BINDING, COMPETITIVE; CATALYTIC DOMAIN; D-ASPARTATE OXIDASE; ENZYME INHIBITORS; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; SUBSTRATE SPECIFICITY; THIOPHENES;

MAMMALIA;

EID: 77957142807     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.06.021     Document Type: Article

References (31)

1. Matsui T., Sekiguchi M., Hashimoto A., Tomita U., Nishikawa T., Wada K. Functional comparison of d-serine and glycine in rodents: the effect on cloned NMDA receptors and the extracellular concentration. J. Neurochem. 1995, 65:454-458.
2. Mothet J.P., Parent A.T., Wolosker H., et al. d-Serine is an endogenous ligand for the glycine site of the N-methyl-d-aspartate receptor. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:4926-4931.
3. Nishikawa T. Metabolism and functional roles of endogenous d-serine in mammalian brains. Biol. Pharm. Bull. 2005, 28:1561-1565.
4. Scolari M.J., Acosta G.B. d-Serine: a new word in the glutamatergic neuro-glial language. Amino Acids 2007, 33:563-574.
5. D'Aniello A. d-Aspartic acid: an endogenous amino acid with an important neuroendocrine role. Brain Res. Rev. 2007, 53:215-234.
6. Homma H. Biochemistry of d-aspartate in mammalian cells. Amino Acids 2007, 32:3-11.
7. Fagg G.E., Matus A. Selective association of N-methyl aspartate and quisqualate types of l-glutamate receptor with brain postsynaptic densities. Proc. Natl. Acad. Sci. U. S. A. 1984, 81:6876-6880.
8. 3H]d-2-amino-5-phosphonopentanoic acid binding in rat brain membranes. Neuroscience 1988, 26:17-31.
9. D'Aniello A., Vetere A., Petrucelli L. Further study on the specificity of d-amino acid oxidase and of d-aspartate oxidase and time course for complete oxidation of d-amino acids. Comp. Biochem. Physiol. B 1993, 105:731-734.
10. Negri A., Tedeschi G., Ceciliani F., Ronchi S. Purification of beef kidney d-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors. Biochim. Biophys. Acta 1999, 1431:212-222.
11. D'Aniello A., D'Onofrio G., Pischetola M., et al. Biological role of d-amino acid oxidase and d-aspartate oxidase. Effects of d-amino acids. J. Biol. Chem. 1993, 268:26941-26949.
12. Errico F., Pirro M.T., Affuso A., et al. A physiological mechanism to regulate d-aspartic acid and NMDA levels in mammals revealed by d-aspartate oxidase deficient mice. Gene 2006, 374:50-57.
13. Hashimoto A., Nishikawa T., Konno R., et al. Free d-serine, d-aspartate and d-alanine in central nervous system and serum in mutant mice lacking d-amino acid oxidase. Neurosci. Lett. 1993, 152:33-36.
14. Huang A.S., Beigneux A., Weil Z.M., et al. d-Aspartate regulates melanocortin formation and function: behavioral alterations in d-aspartate oxidase-deficient mice. J. Neurosci. 2006, 26:2814-2819.
15. Yamada R., Nagasaki H., Nagata Y., Wakabayashi Y., Iwashima A. Administration of d-aspartate increases d-aspartate oxidase activity in mouse liver. Biochim. Biophys. Acta 1989, 990:325-328.
16. Pilone M.S. d-Amino acid oxidase: new findings. Cell. Mol. Life Sci. 2000, 57:1732-1747.
17. Tishkov V.I., Khoronenkova S.V. d-Amino acid oxidase: structure, catalytic mechanism, and practical application. Biochem. Mosc. 2005, 70:40-54.
18. Omura S., Shiomi K. Discovery, chemistry, and chemical biology of microbial products. Pure Appl. Chem. 2007, 79:581-591.
19. Oishi H., Noto T., Sasaki H., et al. Thiolactomycin, a new antibiotic. I. Taxonomy of the producing organism, fermentation and biological properties. J. Antibiot. 1982, 35:391-395.
20. Katane M., Seida Y., Sekine M., Furuchi T., Homma H. Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases. FEBS J. 2007, 274:137-149.
21. Wilkinson G.N. Statistical estimations in enzyme kinetics. Biochem. J. 1961, 80:324-332.
22. Dixon M. Graphical determination of equilibrium constants. Biochem. J. 1965, 94:760-762.
23. Dixon M., Webb E.C. Enzymes 1979, Longman Group Ltd., London, U.K., pp. 332-467. third ed.
24. De Marco C., Crifò C. d-Aspartate oxidase from pig kidney. III. Competitive inhibition by dicarboxylic hydroxyacids. Enzymologia 1967, 33:325-330.
25. Dixon M., Kenworthy P. d-Aspartate oxidase of kidney. Biochim. Biophys. Acta 1967, 146:54-76.
26. Katane M., Hanai T., Furuchi T., Sekine M., Homma H. Hyperactive mutants of mouse d-aspartate oxidase: mutagenesis of the active site residue serine 308. Amino Acids 2008, 35:75-82.
27. Iwana S., Kawazoe T., Park H.K., et al. Chlorpromazine oligomer is a potentially active substance that inhibits human d-amino acid oxidase, product of a susceptibility gene for schizophrenia. J. Enzyme Inhib. Med. Chem. 2008, 23:901-911.
28. Massey V., Ganther H. On the interpretation of the absorption spectra of flavoproteins with special reference to d-amino acid oxidase. Biochemistry 1965, 4:1161-1173.
29. Kawazoe T., Tsuge H., Pilone M.S., Fukui K. Crystal structure of human d-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006, 15:2708-2717.
30. Katane M., Furuchi T., Sekine M., Homma H. Molecular cloning of a cDNA encoding mouse d-aspartate oxidase and functional characterization of its recombinant proteins by site-directed mutagenesis. Amino Acids 2007, 32:69-78.
31. 2. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:7496-7501.