Catalytic and Thermodynamic Properties of Tetrahydromethanopterin-dependent Serine Hydroxymethyltransferase from Methanococcus jannaschii

Journal of Biological Chemistry

Volumn 278, Issue 43, 2003, Pages 41789-41797

  Angelaccio, Sebastiana ^c   Chiaraluce, Roberta ^c   Consalvi, Valerio ^c   Buchenau, Bärbel ^b   Giangiacomo, Laura ^c   Bossa, Francesco ^a   Contestabile, Roberto ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; CARBON; CATALYSIS; PURIFICATION; THERMODYNAMIC STABILITY;

EUBACTERIA;

ENZYMES;

FOLIC ACID; GLYCINE HYDROXYMETHYLTRANSFERASE; HYDROXYMETHYLTRANSFERASE; METHANOPTERIN; METHYLTRANSFERASE; SULFATE; TETRAHYDROFOLIC ACID; TETRAHYDROMETHANOPTERIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CATALYST; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; METHANOCOCCUS JANNASCHII; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SPECTROSCOPY; THERMODYNAMICS;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; ENZYME STABILITY; GLYCINE HYDROXYMETHYLTRANSFERASE; METHANOCOCCUS; PROTEIN DENATURATION; PTERINS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SPECTRUM ANALYSIS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ACTINOBACTERIA (CLASS); ARCHAEA; BACTERIA (MICROORGANISMS); METHANOCALDOCOCCUS JANNASCHII; METHANOCOCCUS; UNCULTURED ACTINOMYCETE;

EID: 0142149170     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M306747200     Document Type: Article

References (42)

1. Schirch, L. (1984) in Folates and Pterins (Blakley, R. L., and Benkovic, S. J., eds) Vol I, pp. 399-431, John Wiley & Sons, Inc., New York
2. Maden, B. E. (2000) Biochem. J. 350, 509-529
3. Paiardini, A., Gianese, G., Bossa, F., and Pascarella, S. (2003) Proteins 50, 122-134
4. Hoyt, J. C., Oren, A., Escalante-Semerena, J. C., and Wolfe, R. S. (1986) Arch. Microbiol. 145, 153-158
5. Wasserfallen, A., Nolling, J., Pfister, P., Reeve, J., and Conway de Macario, E. (2000) Int. J. Syst. Evol. Microbiol. 50, 43-53
6. Delle Fratte, S., White, R. H., Maras, B., Bossa, F., and Schisch, V. (1997) J. Bacteriol. 179, 7456-7461
7. White, R. H. (1991) J. Bacteriol. 173, 1987-1991
8. Schirch, V., Hopkins, S., Villar, E., and Angelaccio, S. (1985) J. Bacteriol. 163, 1-7
9. Fu, T. F., di Salvo, M., and Schirch, V. (2001) Anal. Biochem. 290, 359-365
10. Gill, S. C., and von Hippel, P. H. (1989) Anal. Biochem. 182, 319-326
11. Schuck, P., and Rossmanith, P., (2000) Biopolymers 54, 328-341
12. Johnson, M. L., Correia, J. J., Yphantis, D. A., and Halvorson, H. R. (1981) Biophys. J. 36, 575-588
13. Vorholt, J. A., Chistoserdova, L., Lidstrom, M. E., and Thauer, R. K. (1998) J. Bacteriol. 180, 5351-5356
14. Schirch, V., and Peterson, D. (1980) J. Biol. Chem. 255, 7801-7806
15. Ulevitch, R. J., and Kallen, R. G. (1977) Biochemistry 16, 5342-5350
16. Shostak, K., and Schirch, V. (1988) Biochemistry 27, 8007-8014
17. Henry, E. R., and Hofrichter, J. (1992) Methods Enzymol. 210, 129-192
18. Ionescu, R. M., Smith, V. F., O'Neill, J. C., Jr., and Matthews, C. R. (2000) Biochemistry 39, 9540-9550
19. Johnson, W. C., Jr. (1992) Methods Enzymol. 210, 426-447
20. Santoro, M. M., and Bolen, D. W. (1988) Biochemistry 27, 8063-8068
21. Chen, M. S., and Schirch, L. (1973) J. Biol. Chem. 248, 7979-7984
22. Schirch, L. V., and Jenkins, T. (1964) J. Biol. Chem. 239, 3801-3806
23. Arrio-Dupont, M. (1971) Biochem. Biophys. Res. Commun. 44, 653-659
24. Bertoldi, M., Cellini, B., Clausen, T., and Borri Voltattorni, C. (2002) Biochemistry 41, 9153-9164
25. Shaltiel, S., and Cortijo, M. (1970) Biochem. Biophys. Res. Commun. 41, 594-600
26. Deléage, G., and Geourjon, C. (1993) Comp. Appl. Biosci. 9, 197-199
27. Andrade, M. A., Chacon, P., Merelo, J. J., and Moran, F. (1993) Protein Eng. 6, 383-390
28. Sreerama, N., and Woody, R. W. (1994) J. Mol. Biol. 242, 497-507
29. Rost, B. (1996) Methods Enzymol. 266, 525-539
30. Wyman, J., Jr., and Ingalls, E. N. (1943) J. Biol. Chem. 147, 297-318
31. Schirch, V. (1998) in Comprehensive Biological Catalysis (Sinnot, M., ed) Vol. 1, pp. 211-252, Academic Press, San Diego, CA
32. Renwick, S. B., Snell, K., and Baumann, U. (1998) Structure 6, 1105-1116
33. Scarsdale, J. N., Kazanina, G., Radaev, S., Schirch, V., and Wright, H. T. (1999) Biochemistry 38, 8347-8358
34. Scarsdale, J. N., Radaev, S., Kazanina, G., Schirch, V., and Wright, H. T. (2000) J. Mol. Biol. 296, 155-168
35. Szebenyi, D. M. E., Xiaowen, L., Kriksunov, I. A., Stover, P., and Thiel, D. J. (2000) Biochemistry 39, 13313-13323
36. Trivedi, V., Gupta, A., Jala, V. R., Saravanan, P., Jagannatha Rao, G. S., Appaji Rao, N., Savithri, H. S., and Subramanya, H. S. (2002) J. Biol. Chem. 277, 17161-17169
37. Notredame, C., Higgins, D., and Heringa, J. (2000) J. Mol. Biol. 302, 205-217
38. Fu, T. F., Scarsdale, J. N., Kazanina, G., Schirch, V., and Wright, H. T. (2003) J. Biol. Chem. 278, 2645-2653
39. Lin, Z., and Sparling, R. (1998) Can. J. Microbiol. 44, 652-656
40. Schirch, V., Shostak, K., Zamora, M., and Gautam-Basak, M. (1991) J. Biol. Chem. 266, 759-764
41. Cai, K., Schirch, D., and Schirch, V. (1995) J. Biol. Chem. 270, 19294-19299
42. Myers J. K., Pace, N. C., and Scholtz, M. J. (1995) Protein Sci. 4, 2138-2148