Role of Tyrosine 114 of L-Methionine γ-lyase from Pseudomonas putida

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 11, 2000, Pages 2336-2343

  Inoue, Hiroyuki ^a,d   Inagaki, Kenji ^a   Adachi, Naoki ^a   Tamura, Takashi ^a   Esaki, Nobuyoshi ^b   Soda, Kenji ^c   Tanaka, Hidehiko ^a  

^a OKAYAMA UNIVERSITY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c KANSAI UNIVERSITY   (Japan)

^d Chugoku National Industrial Research Institute ^*  (Japan)

Author keywords

General acid catalyst; L methionine lyase; Reaction mechanism; Site directed mutagenesis

Indexed keywords

DEUTERIUM OXIDE; HYDROGEN; L-METHIONINE GAMMA-LYASE; LYASE; METHIONINE GAMMA LYASE; PHENYLALANINE; TYROSINE;

ARTICLE; CATALYSIS; CHEMISTRY; DEAMINATION; ENZYMOLOGY; GENETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PSEUDOMONAS PUTIDA; SITE DIRECTED MUTAGENESIS;

CARBON-SULFUR LYASES; CATALYSIS; DEAMINATION; DEUTERIUM OXIDE; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PSEUDOMONAS PUTIDA; TYROSINE;

EID: 0034330323     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.2336     Document Type: Article

References (38)

1. Tanaka, H., Esaki, N., and Soda, K., Properties of L-methionine y-lyase from Pseudomonas ovalis. Biochemistry, 16, 100-106 (1977).
2. Tanaka, H., Esaki, N., and Soda, K., A versatile bacterial enzyme: L-methionine y-lyase. Enzyme Microb. Technol., 7, 530-537 (1985).
3. Tanaka, H., Esaki, N., Yamamoto, T., and Soda, K., Purification and properties of methioninase from Pseudomonas ovalis. FEBSLett., 66, 307-311 (1976).
4. Nakayama, T., Esaki, N., Sugie, K., Beresov, T. T., Tanaka, H., and Soda, K., Purification of bacterial l-methionine y-lyase. Anal. Biochem., 138, 421-424 (1984).
5. Nakayama, T., Esaki, N., Lee, K. W.-J., Tanaka, I., Tanaka, FI., and Soda, K., Purification and properties of L-methionine y-lyase from Aeromonas sp. Agric. Biol. Chem., 48, 2367-2369 (1984).
6. Kreis, W. and Hession, C., Isolation and purification of L-methionine a-deamino-y-mercaptomethane-lyase (L-methioninase) from Clostridium sporogenes. Cancer Res., 33, 1862-1865 (1973).
7. Lockwood, B. and Coombs, G. H., Purification and characterization of methionine y-lyase from Trichomonas vaginalis. Biochem. J., 279, 675-682 (1991).
8. Inoue, H., Inagaki, K., Sugimoto, M., Esaki, N., Soda, K., and Tanaka, H., Structural analysis of the L-methionine y-lyase gene from Pseudomonasputida. J. Biochem., 117, 1120-1125 (1995).
9. Alexander, F. W., Sandmeier, E., Mehta, P. K., and Christen, P., Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific a, (3 and y families. Eur. J. Biochem., 219, 953-960 (1994).
10. Ono, B., Tanaka, K., Naito, K., Heike, C., Shinoda, S., Yamamoto, S., Ohmori, S., Oshima, T., and Toh-e, A., Cloning and characterization of the cys3 (cyil) gene of Saccharomyces cerevisiae. J. Bac-teriol., 174, 3339-3347 (1992).
11. Lu, Y., O’Dowd, B. F., Orrego, H., and Israel, Y., Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine y-lyase. Biochem. Biophys. Res. Commun., 189, 749-758 (1992).
12. Duchange, N., Zakin, M. M., Ferrara, P., Saint-Girons, I., Park, I., Tran, S. V., Py, M. C., and Cohen, G. N., Structure of the metJBLF cluster in Escherichia coli K12. Sequence of the metB structural gene and the 5'- and 3'-flanking regions of the metBL operon. J. Biol. Chem., 258, 14868-14871 (1983).
13. Kerjan, P., Cherest, H., and Surdin-Kerjan, Y., Nucleotide sequence of the Saccharomyces cerevisiae met25 gene. Nucl. Acids Res., 14, 787861-7871 (1986).
14. JH NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine y-lyase. Biochemistry, 24, 3857-3862 (1985).
15. Davis, L. and Metzler, D. E., Pyridoxal-linked elimination and replacement reactions. In “The Enzyme 3rd ed”, ed. Boyer, P. P., Academic Press, New York, vol. 7, pp. 33-74 (1972).
16. Esaki, N., Takada, H., Moriguchi, M., Hatanaka, S., Tanaka, H., and Soda, K., Mechanism-based inactivation of L-methionine y-lyase by L-2-amino-4-chloro-4-pentanoate. Biochemistry, 28, 2111-2116 (1989).
17. Johnston, M., Raines, R., Walsh, C., and Frestone, R. A., Mechanism-based enzyme inactivation using an allyl sulfoxide-allyl sulfenante ester rearrangement. J. Am. Chem. Soc., 102, 4241-4250 (1980).
18. Nakayama, T., Esaki, N., Tanaka, H., and Soda, K., Specific labeling of the essential cysteine residue of L-methionine y-lyase with a cofactor analogue, N-(bromoacetyl)pyridoxamine phosphate. Biochemistry, 27, 1587-1591 (1988).
19. Nakayama, T., Esaki, N., Tanaka, FL, and Soda, K., Chemical modification of cysteine residues of l-methionine y-lyase. Agric. Biol. Chem., 52, 177-183 (1988).
20. McKie, A. E., Edlind, T., Walker, J., Mottram, J. C., and Coombs, G. H., The primitive protozoon Trichomonas vaginalis contains two methionine y-lyase genes that encode members of the y-family of pyridoxal 5'-phosphate-dependent enzymes. J. Biol. Chem., 273, 5549-5556 (1998).
21. Clausen, T., Huber, R., Laber, B., Pohlenz, H. D., and Messerschmidt, A., Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 A. J. Mol. Biol., 262, 202-224 (1996).
22. Clausen, T., Huber, R., Prade, L., Wahl, M. C., and Messerschmidt, A., Crystal structure of Escherichia coli cystathionine y-synthase at 1.5 A resolution. EMBO J., 17, 6827-6838 (1998).
23. Nagai, S. and Flavin, M., Synthesis of O-acetyl-homoserine. In “Methods in Enzymology”, eds. Tabor, H. and Tabor, C. E., Academic Press, New York, vol. 17B, pp. 423-424 (1971).
24. Kunkel, T. A., Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA, 82, 488-492 (1985).
25. Tartof, K. D. and Hobbs, C. A., Improved media for growing plasmid and cosmid clones. Bethesda Res. Lab. Focus, 9, 12 (1987).
26. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227, 680-685 (1970).
27. Soda, K., Microdetermination of D-amino acids and D-amino acid oxidase activity with 3-methyl-2-bnzothiazolone hydrazone hydrochloride. Anal. Biochem., 25, 228-235 (1968).
28. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
29. Esaki, N., Suzuki, T., Tanaka, H., Soda, K., and Rando, R. R., Deamination and y-addition reactions of vinylglycine by L-methionine y-lyase. FEBS Lett., 84, 309-312 (1977).
30. Esaki, N., Nakayama, T., Sawada, S., Tanaka, H., and Soda, K., Reactions of O-substituted L-homoser-ines catalyzed by L-methionine y-lyase and their mechanism. Agric. Biol. Chem., 48, 1991-1996 (1984).
31. Johnston, M., Jankowski, D., Marcotte, P., Tanaka, H., Esaki, N., Soda, K., and Walsh, C., Suicide inactivation of bacterial cystathionine y-synthase and methionine y-lyase during processing of L-propargyl-glycine. Biochemistry, 18, 4690-4701 (1979).
32. Clausen, T., Huber, R., Messerschmidt, A., Pohlenz, H. D., and Laber, B., Slow-binding inhibition of Escherichia coli cystathionine /Myase by L-aminoethox-yvinylglycine: a kinetic and X-ray study. Biochemistry, 36, 12633-12643 (1997).
33. Esaki, N., Tanaka, H., Uemura, S., Suzuki, T., and Soda, K., Catalytic action of L-methionine y-lyase on selenomethionine and selenols. Biochemistry, 18, 407-410 (1979).
34. Chen, H. Y., Demidkina, T. V., and Phillips, R. S., Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding. Biochemistry, 34, 12276-12283 (1995).
35. Tai, C. H., Nalabolu, S. R., Simmons, J. W. Ill, Jacobson, T. M., and Cook, P. F., Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies. Biochemistry, 34, 12311-12322 (1995).
36. Ravanel, S., Ruifet, M. L., and Douce, R., Cloning of an Arabidopsis thaliana cDNA encoding cystathionine /Myase by functional complementation in Escherichia coli. Plant Mol. Biol., 29, 875-882 (1995).
37. Gentry-Weeks, C. R., Keith, J. M., and Thompson, J., Toxicity of Bordetella avium β-cystathionase toward MC3T3-E1 osteogenic cells. J. Biol. Chem., 268, 7298-7314 (1993).
38. Belfaiza, J., Parsot, C., Martel, A., Bouthier de la Tour, C., Margarita, D., Chohen, G. N., and Saint-Girons, I., Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proc. Natl. Acad. Sci. USA, 83, 867-871 (1986).