Trp-49 of the family 3 β-glucosidase from Aspergillus niger is important for its transglucosidic activity: Creation of novel β-glucosidases with low transglucosidic efficiencies

Archives of Biochemistry and Biophysics

Volumn 455, Issue 2, 2006, Pages 110-118

  Seidle, Heather F ^a   Allison, Sandra J ^a   George, Erica ^a   Huber, Reuben E ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

Glucosidase; Aspergillus niger; Binding; Family 3; Hydrolytic reactions; Kinetics; Transglucosidic reactions; Tryptophan

Indexed keywords

BETA GLUCOSIDASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; ASPERGILLUS NIGER; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; HYDROLYSIS; KINETICS; NONHUMAN; PRIORITY JOURNAL; STATISTICAL SIGNIFICANCE; WILD TYPE;

ASPERGILLUS NIGER; CELLULASES; ENZYME ACTIVATION; ENZYME STABILITY; FUNGAL PROTEINS; GLUCOSE; MOLECULAR WEIGHT;

ASPERGILLUS NIGER;

EID: 33750704622     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2006.09.016     Document Type: Article

References (20)

1. Dan S., Marton I., Dekel M., Bravdo B.A., He S., Withers S.G., and Shoseyov O. J. Biol. Chem. 275 (2000) 4973-4980
2. Seidle H.F., Marten I., Shoseyov O., and Huber R.E. Protein J. 23 (2004) 11-23
3. Quiocho F.A. Annu. Rev. Biochem. 55 (1986) 287-315
4. Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L., Withers S.G., and Matthews B.W. Biochemistry 40 (2001) 14781-14794
5. Huber R.E., Hakda S., Cheng C., Cupples C.G., and Edwards R.A. Biochemistry 42 (2003) 1796-1803
6. Sujatha M.S., Sasidhar Y.U., and Balaji P.V. Protein Sci. 13 (2004) 2502-2514
7. Weis W.I., and Drickamer K. Annu. Rev. Biochem. 65 (1996) 441-473
8. Seidle H.F., and Huber R.E. Arch. Biochem. Biophys. 436 (2005) 254-264
9. Gusakov A.V., Sinitsyn A.P., Goldsteins G.H., and Klyosov A.A. Enzyme Microb. Technol. 6 (1984) 275-282
10. Davies G.J., Wilson K.S., and Henrissat B. Biochem. J. 321 Pt 2 (1997) 557-559
11. Ohnishi M., Okada G., and Yazaki T. Carbohydr. Res. 308 (1998) 201-205
12. Yazaki T., Ohnishi M., Rokushika S., and Okada G. Carbohydr. Res. 298 (1997) 51-57
13. Pemberton M.S., Brown R.D., and Emert G.H. Can. J. Chem. Eng. 58 (1980) 723-729
14. Bollok M., and Reczey K. Acta Alimentaria 29 (2000) 155-168
15. Fujita Y., Ito J., Ueda M., Fukuda H., and Kondo A. Appl. Environ. Microbiol. 70 (2004) 1207-1212
16. Zaldivar M., Velasquas J.C., Contreras I., and Perez L.M. Electron. J. Biotechnol. [online] 4 (2001) 160-168
17. Zhou S., and Ingram L.O. Biotechnol. Lett. 23 (2001) 1455-1462
18. Kuriki T., Kaneko H., Yanase M., Takata H., Shimada J., Handa S., Takada T., Umeyama H., and Okada S. J. Biol. Chem. 271 (1996) 17321-17329
19. Seidle H.F., McKenzie K., Marten I., Shoseyov O., and Huber R.E. Arch. Biochem. Biophys. 444 (2005) 66-75
20. Varghese J.N., Hrmova M., and Fincher G.B. Struct. Fold Des. 7 (1999) 179-190