Characterization of cyanobacterial biliverdin reductase: Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis

Journal of Biological Chemistry

Volumn 272, Issue 21, 1997, Pages 13562-13569

  Schluchter, Wendy M ^a   Glazer, Alexander N ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BILIVERDIN; BILIVERDIN REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; CYANOBACTERIUM; ENZYME ACTIVITY; ENZYME ANALYSIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BILIRUBIN; BILIVERDINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CLONING, MOLECULAR; CYANOBACTERIA; ESCHERICHIA COLI; HUMANS; KINETICS; LIGHT-HARVESTING PROTEIN COMPLEXES; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PHYCOBILISOMES; PIGMENTS, BIOLOGICAL; PLANT PROTEINS; RATS; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); CYANOBACTERIA; ESCHERICHIA COLI; MAMMALIA; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

EID: 0030925429     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.21.13562     Document Type: Article

References (49)

1. O'hEocha, C. (1965) in Chemistry and Biochemistry of Plant Pigments (Goodwin, T. W., ed) pp. 175-196, Academic Press, New York
2. Glazer, A. N. (1985) Annu. Rev. Biophys. Biophys. Chem. 14, 47-77
3. Glazer, A. N., and Wedemayer, G. J. (1995) Photosyn. Res. 46, 93-105
4. Beale, S. I. (1993) Chem. Rev. 93, 785-802
5. McDonagh, A. F. (1979) in The Porphyrins (Dolphin, D., ed) Vol. 6, pp. 243-491, Academic Press, New York
6. Beale, S. I., and Cornejo, J. (1983) Arch. Biochem. Biophys. 227, 279-286
7. Beale, S. I., and Cornejo, J. (1984) J. Plant Physiol. 76, 7-15
8. Schmid, R., and McDonagh, A. F. (1978) in The Metabolic Basis of Inherited Disease (Stanbury, J. B., and Wyngaarden, J. B., eds) pp. 1221-1257, McGraw Hill, New York
9. Beale, S. I., and Cornejo, J. (1991) J. Biol. Chem. 266, 22328-22332
10. Beale, S. I., and Cornejo, J. (1991) J. Biol. Chem. 266, 22333-22340
11. Beale, S. I., and Cornejo, J. (1991) J. Biol. Chem. 266, 22341-22345
12. Rhie, G., and Beale, S. I. (1992) J. Biol. Chem. 267, 16088-16093
13. Singleton, J. W., and Laster, L. (1965) J. Biol. Chem. 240, 4780-4789
14. Cornejo, J., and Beale, S. I. (1996) Plant Physiol. 111, 104
15. Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., Miyajima, N., Hirosawa, M., Sugiura, M., Sasamoto, S., Kimura, T., Hosouchi, T., Matsuno, A., Muraki, A., Nakazaki, N., Naruo, K., Okumura, S., Shimpo, S., Takeuchi, C., Wada, T., Watanabe, A., Yamada, M., Yasuda, M., and Tabata, S. (1996) DNA Res. 3, 109-136
16. Gingrich, J. C., Lundell, D. J., and Glazer, A. N. (1983) J. Cell. Biochem. 22, 1-14
17. Glazer, A. N., Lundell, D. J., Yamanaka, G., and Williams, R. C. (1983) Ann. Microbiol. (Inst. Pasteur) 134B, 159-180
18. Elhai, J., and Wolk, C. P. (1988) Gene (Amst.) 68, 119-138
19. Schluchter, W. M., and Bryant, D. A. (1992) Biochemistry 31, 3092-3102
20. Stanier, R. Y., Kunisawa, R., Mandel, M., and Cohen-Bazire, G. (1971) Bacteriol Rev. 35, 171-205
21. Hegy, G. B., Shackleton, C. H. L., Carlquist, M., Bonn, T., Engström, O., Sjöholm, P., and Witkowska, W. E. (1996) Steroids 61, 367-373
22. Williams, J. G. K. (1988) Methods Enzymol. 167, 304-312
23. Howitt, C. A. (1996) BioTechniques 21, 32-34
24. Kutty, R. K., and Maines, M. D. (1981) J. Biol. Chem. 256, 3956-3962
25. Arciero, D. M., Bryant, D. A., and Glazer, A. N. (1988) J. Biol. Chem. 263, 18343-18349
26. Cole, W. J., Chapman, D. J., and Siegelman, W. H. (1967) J. Am. Chem. Soc. 89, 3643-3645
27. Glazer, A. N. (1988) Methods Enzymol. 167, 304-312
28. Glazer, A. N. (1988) Methods Enzymol. 167, 291-303
29. Fakhrai, H., and Maines, M. D. (1992) J. Biol. Chem. 267, 4023-4029
30. Komuro, A., Tobe, T., Nakano, Y., Yamaguchi, T., and Tomita, M. (1996) Biochim. Biophys. Acta 1309, 89-99
31. Hein, J. (1990) Methods Enzymol. 183, 626-645
32. McCoubrey, W. K., Jr., and Maines, M. D. (1994) Eur. J. Biochem. 242, 597-603
33. Troxler, R. F., and Lester, R. (1968) Plant Physiol. 43, 1737-1739
34. Troxler, R. F., Brown, A., Lester, R., and White, P. (1970) Science 167, 192-193
35. Troxler, R. F., Dokos, J. M. (1973) Plant Physiol 51, 72-75
36. Beale, S. I., and Cornejo, J. (1984) Arch. Biochem. Biophys. 235, 371-384
37. Zhou, J., Gasparich, G. E., Stirewalt, V. L., de Lorimier, R., and Bryant, D. A. (1992) J. Biol. Chem. 267, 16138-16145
38. Swanson, R. V., Zhou, J., Leary, J. A., Williams, T., de Lorimier, R., Bryant, D. A., and Glazer, A. N. (1992) J. Biol. Chem. 267, 16146-16154
39. Fairchild, C. D., Zhao, J., Zhou, J. Colson, S. E., Bryant, D. A., and Glazer, A. N. (1992) Proc. Nat. Acad. Sci. U. S. A. 89, 7017-7021
40. Bhalerao, R. P., Kind, L. K., and Gustafsson, P. (1994) Plant Mol. Biol. 26, 313-326
41. Jung, L. J., Chan, C. F., and Glazer, A. N. (1995) J. Biol. Chem. 270, 12877-12884
42. Bari, S., Frydman, R. B., Grosman, C., and Frydman, B. (1992) Biochem. Biophys. Res. Commun. 188, 48-56
43. Terry, M. J., Maines, M. D., and Lagarias, J. C. (1993) J. Biol. Chem. 268, 26099-26106
44. Fairchild, C. D., and Glazer, A. N. (1994) J. Biol. Chem. 269, 28988-28996
45. Troxler, R. F., Lin, S., and Offner, G. D. (1989) J. Biol. Chem. 264, 20596-20601
46. Maines, M. D., Polevoda, B. V., Huang, T.-J., and McCoubrey, W. K., Jr. (1996) Eur. J. Biochem. 235, 372-381
47. Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., and Ames, B. N. (1987) Science 235, 1043-1046
48. Stocker, R., McDonagh, A. F., Glazer, A. N., and Ames, B. N. (1990) Methods Enzymol. 186, 301-309
49. Dennery, P. A., McDonagh, A. F., Spitz, D. R., Rodgers, P. A., and Stevenson, D. K. (1995) Free Radical Biol. & Med. 19, 395-404