The role of a conserved histidine residue, His324, in Trigonopsis variabilis D-amino acid oxidase

FEMS Microbiology Letters

Volumn 176, Issue 2, 1999, Pages 443-448

  Lin, Long Liu ^a   Wang, Wen Ching ^b   Ju, Sheau Shya ^c   Chien, Hungchien Roger ^d   Hsu, Wen Hwei ^c  

^a HUNGKUANG UNIVERSITY   (Taiwan)

^b NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^c NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^d CHUNG SHAN MEDICAL UNIVERSITY   (Taiwan)

Author keywords

D Amino acid oxidase; FAD binding; Trigonopsis variabilis

Indexed keywords

DEXTRO AMINO ACID OXIDASE; FLAVINE ADENINE NUCLEOTIDE; HISTIDINE; KIDNEY ENZYME; MUTANT PROTEIN; RECOMBINANT DNA; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTROPHORESIS; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STRUCTURE; MICROORGANISM; MOLECULAR WEIGHT; NONHUMAN; PLASMID; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; SWINE; TRIGONOPSIS VARIABILIS; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; D-AMINO-ACID OXIDASE; ESCHERICHIA COLI; HISTIDINE; HUMANS; MITOSPORIC FUNGI; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

FELIS CATUS; SUS SCROFA; TRIGONOPSIS VARIABILIS;

EID: 0033051960     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00270-0     Document Type: Article

References (25)

1. Hafner E.W., Wellner D. Demonstration of imino acids as products of the reactions catalyzed by D- and L-amino acid oxidases. Proc. Natl. Acad. Sci. USA. 68:1971;987-991.
2. Curti, B., Ronchi, S. and Pilone, S.M. (1992) D- And L-amino acid oxidases. In: Chemisrty and Biochemistry of Flavoenzymes (Muller, F. and Raton, B., Eds.), pp. 69-94. CRC Press, New York.
3. Denu J.M., Fitzpatrick P.F. pH and kinetic isotope effects on the oxidative half-reaction of D-amino acid oxidase. J. Biol. Chem. 269:1994;15054-15059.
4. Pollegioni L., Blodig W., Ghisla S. On the mechanism of D-amino acid oxidase. J. Biol. Chem. 272:1997;4924-4934.
5. D'Anicello A., D'Onofrio G., Pischetola M., D'Aniello G., Vetere A., Petrucelli L., Fischer G.H. Biological role of D-amino acid oxidase and D-aspartate oxidase: effects of D-amino acids. J. Biol. Chem. 268:1993;26941-26949.
6. Gonzalez F.J., Montes J., Martin F., Lopez M.C., Ferminan E., Catalan J., Galan M.A., Mominguez A. Molecular cloning of TvDAO1, a gene encoding a D-amino acid oxidase from Trigonopsis variabilis and its expression in Saccharomyces cerevisiae and Kluyveromyces lactis. Yeast. 13:1997;1399-1408.
7. Isogai T., Ono H., Ishitani Y., Kojo H., Ueda Y., Kohsaka M. Structure and expression of cDNA for D-amino acid oxidase active against cephalosporin C from Fusarium solani. J. Biochem. 108:1990;1063-1069.
8. Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S. The primary structure of D-amino acid oxidase from Rhodotorula gracilis. Biotechnol. Lett. 17:1995;193-198.
9. Liao G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S. Structure and expression of the D-amino acid oxidase gene from the yeast Rhodosporidium totuloides. Biotechnol. Appl. Biochem. 27:1998;55-61.
10. Fukui K., Watanabe F., Shibata T., Miyake Y. Molecular cloning and sequence analysis of cDNA encoding porcine kidney D-amino acid oxidase. Biochemistry. 26:1987;3612-3618.
11. Ju S.S., Lin L.L., Wang W.C., Hsu W.H. A conserved aspartate is essential for FAD binding and catalysis in the D-amino acid oxidase from Trigonopsis variabilis. FEBS Lett. 436:1998;119-122.
12. Ronchi S., Minchiotti L., Galliano M., Curti B., Swenson R.P., Williams C.H. Jr., Massey V. The primary structure of D-amino acid oxidase from pig kidney: isolation and sequemce of overlap peptide and complete sequence. J. Biol. Chem. 257:1982;8824-8834.
13. Swenson R.P., Williams C.H. Jr., Massey V. Chemical modification of D-amino acid oxidase: amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene. J. Biol. Chem. 257:1982;1937-1944.
14. Watanabe F., Fukui K., Momoi K., Miyake Y. Site-specific mutagenesis of Lysine-204, Tyrosine-224, Tyrosine-228, and Histidine-307 of porcine kidney D-amino acid oxidase and the implications as to its catalytic function. J. Biochem. 105:1989;1024-1029.
15. 2. Proc. Natl. Acad. Sci. USA. 93:1996;7496-7501.
16. Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M., Miyake Y. Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization. J. Biochem. 109:1991;171-177.
17. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
18. Kunkel T.A., Roberts J.D., Zakour R.A. Rapid and efficient site-specific mutagenesis without phenotype selection. Methods Enzymol. 154:1987;367-382.
19. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Mannual, pp. 17.2-17.44, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
20. Lee Y.H., Chu W.S., Hsu W.H. Bioconversion of cephalosporin C with D-amino acid oxidase from the yeast Rhodosporidium toruloides. Biotechnol. Lett. 16:1994;467-472.
21. Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
22. Nishino T., Massey V., Williams C.H. Jr. Chemical modifications of D-amino acid oxidase: evidence for active site histidine, tyrosine, and arginine residues. J. Biol. Chem. 255:1980;3610-3616.
23. Swenson R.P., Williams C.H. Jr., Massey V. Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalenel-sulfonyl chloride. J. Biol. Chem. 258:1983;497-502.
24. Swenson R.P., Williams C.H. Jr., Massey V. Methylation of the active center histidine 217 in D-amino acid oxidase by methyl-p-nitrobenzenesulfonate. J. Biol. Chem. 259:1984;5585-5590.
25. Watanabe F., Fukui K., Momoi K., Miyake Y. Effect of site-specific mutagenesis of tyrosine-55, methionine-110, and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function. FEBS Lett. 238:1988;269-272.