α-lactalbumin (LA) stimulates milk β-1,4-galactosyltransferase I (β4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine: Crystal structure of β4Gal-T1·LA complex with UDP-Glc

Journal of Biological Chemistry

Volumn 276, Issue 40, 2001, Pages 37665-37671

  Ramakrishnan, Boopathy ^a   Shah, Premal S ^a,b   Qasba, Pradman K ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; HYDROGEN BONDS; SUBSTITUTION REACTIONS; SUBSTRATES;

ACCEPTOR SUBSTRATES;

BIOCHEMISTRY;

ALPHA LACTALBUMIN; BETA 1,4 GALACTOSYLTRANSFERASE I; CYSTEINE; GALACTOSE; GALACTOSYLTRANSFERASE; GLUCOSAMINE DERIVATIVE; GLUCOSE; LACTOSE SYNTHASE; MANGANESE; N ACETYLGLUCOSAMINE; N BUTYRYLGLUCOSAMINE; THREONINE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GALACTOSE; URIDINE DIPHOSPHATE GLUCOSE; BETA-1,4-GALACTOSYLTRANSFERASE I; LACTALBUMIN;

AMINO ACID SUBSTITUTION; ARTICLE; CELL INCLUSION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; GLUCOSE TRANSPORT; HYDROGEN BOND; MILK; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; TRANSPORT KINETICS; ANIMAL; CATALYSIS; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOUSE; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ACETYLGLUCOSAMINE; AMINO ACID SUBSTITUTION; ANIMALS; CATALYSIS; CATTLE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; ENZYME STABILITY; GALACTOSYLTRANSFERASES; GLUCOSE; KINETICS; LACTALBUMIN; MICE; MILK; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SUBSTRATE SPECIFICITY; THREONINE; URIDINE DIPHOSPHATE GLUCOSE;

EID: 0035813137     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102458200     Document Type: Article

References (34)

1. Hill, R. (1979) UCLA Forum Med. Sci. 21, 63-86
2. Shaper, N. L., Shaper, J. H., Meuth, J. L., Fox, J. L., Chang, H., Kirsch, I. R., and Hollis, G. F. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 1573-1577
3. Narimatsu, H., Sinha, S., Brew, K., Okayama, H., and Qasba, P. K. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 4720-4724
4. Sato, T., Furukawa, K., Bakker, H., Van den Eijnden, D. H., and Van Die, I. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 472-477
5. Almeida, R., Amado, M., David, L., Levery, S. B., Holmes, E. H., Merkx, G., van Kessel, A. G., Rygaard, E., Hassan, H., Bennett, E., and Clausen, H. (1997) J. Biol. Chem. 272, 31979-31991
6. Schwientek, T., Almeida, R., Levery, S. B., Holmes, E. H., Bennett, E., and Clausen, H. (1998) J. Biol. Chem. 273, 29331-29340
7. Sato, T., Aoki, N., Matsuda, T., and Furukawa, K. (1998) Biochem. Biophys. Res. Commun. 244, 637-641
8. Lo, N. W., Shaper, J. H., Pevsner, J., and Shaper, N. L. (1998) Glycobiology 8, 517-526
9. Almeida, R., Levery, S. B., Mandel, U., Kresse, H., Schwientek, T., Bennett, E. P., and Clausen, H. (1999) J. Biol. Chem. 274, 26165-26171
10. Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Waskisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M., and Matsuo, N. (1998) J. Biol. Chem. 273, 13570-13577
11. Berliner, L. J., Davis, M. E., Ebner, K. E., Beyer, T. A., and Bell, J. E. (1984) Mol. Cell. Biochem. 62, 37-42
12. Do, K. Y., Do, S. I., and Cummings, R. D. (1995) J. Biol. Chem. 270, 18447-18451
13. Andree, P. J., and Berliner, L. J. (1978) Biochim. Biophys. Acta 544, 489-495
14. Palcic, M. M., and Hindsgaul, O. (1991) Glycobiology 1, 205-209
15. Sprong, H., Kruithof, B., Leijendekker, R., Slot, J. W., van Meer, G., and van der Sluijis, P. (1998) J. Biol. Chem. 273, 25880-25888
16. Qasba, P. K., and Kumar, S. (1997) Crit. Rev. Biochem. Mol. Biol. 32, 255-306
17. Ramakrishnan, B., and Qasba, P. K. (2001) J. Mol. Biol. 310, 205-218
18. Gastinel, L. N., Cambillau, C., and Bourne, Y. (1999) EMBO J. 18, 3546-3557
19. Ausubel, F. M., Brent, R., Kinstom, R. E., Moore, D. D., Smith, J. A., Seidman, J. G., and Struhl, K. (eds) (1987) Current Protocols in Molecular Biology, Greene Publishing Associates and Wiley-Interscience, New York
20. Boeggeman, E. E., Balaji, P. V., Sethi, N., Masibay, A. S., and Qasba, P. K. (1993) Protein Eng. 6, 779-785
21. Noel, J. P., Bingman, C. A., Deng, T. L., Dupureur, C. M., Hamilton, K. J., Jiang, R. T., Kwak, J. G., Sekharudu, C., Sundaralingam, M., and Tsai, M. D. (1991) Biochemistry 30, 11801-11811
22. Wang, M., Scott, W. A., Rao, K. R., Udey, J., Conner, G. E., and Brew, K. (1989) J. Biol. Chem. 264, 21116-21121
23. Qasba, P. K., and Chakrabartty, P. K. (1978) J. Biol. Chem. 253, 1167-1173
24. Zhang, Y., Malinovskii, V. A., Fiedler, T. J., and Brew, K. (1999) Glycobiology 9, 815-822
25. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
26. Navaza, J. (1994) Acta Crystallogr. Sect. A 50, 760-763
27. Brunger, A. T., Adams, P. D., Clore, G. M., De Lano, W. L., and Gross, P. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
28. Karulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
29. Yen, T. Y., Joshi, R. K., Yan, H., Seto, N. O. L., Palcic, M. M., and Macher, B. A. (2000) J. Mass Spectrom. 35, 990-1002
30. Geren, C. R., Magee, S. C., and Ebner, K. E. (1975) Biochemistry 14, 1461-1463
31. Khatra, B. S., Herries, D. G., and Brew, K. (1974) Eur. J. Biochem. 44, 537-560
32. Takayama, S., Chung, S. J., Igarashi, Y. Ichikawa, Y., Sepp, A., Lechler, R. I., Wu, J., Hayashi, T., Siuzdak, G., and Wong, C. H. (1999) Bioorg. Med. Chem. 7, 401-409
33. Yadav, S. P., and Brew, K. (1991) J. Biol. Chem. 266, 698-703
34. Clymer, D. J., Geren, R., and Ebner, K. E. (1976) Biochemistry 15, 1093-1097