Identification of the catalytic acid-base residue of arthrobacter endo-β-N-acetylglucosaminidase by chemical rescue of an inactive mutant

Journal of Biochemistry

Volumn 142, Issue 3, 2007, Pages 301-306

  Fujita, Kiyotaka ^a   Sato, Reiko ^b   Toma, Kazunori ^c   Kitahara, Kanefumi ^a   Suganuma, Toshihiko ^a   Yamamoto, Kenji ^c   Takegawa, Kaoru ^d  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b NOGUCHI INSTITUTE   (Japan)

^c KYOTO UNIVERSITY   (Japan)

^d KAGAWA UNIVERSITY   (Japan)

Author keywords

Azide; Catalytic acid base residue; Chemical rescue; Endo N acetylglucosaminidase; Inactive mutant

Indexed keywords

ASPARAGINE; AZIDE; FORMATE SODIUM; FORMIC ACID; GLUTAMIC ACID; GLYCOPROTEIN; MUTANT PROTEIN; N ACETYL BETA GLUCOSAMINIDASE; OLIGOSACCHARIDE; RETINOL; SODIUM AZIDE; UNCLASSIFIED DRUG;

ARTHROBACTER; ARTICLE; CATALYSIS; ENZYME ASSAY; ENZYME MECHANISM; GLYCOSYLATION; HYDROLYSIS; PROTEOMICS;

AMINO ACID SEQUENCE; ARTHROBACTER; BASE SEQUENCE; CARBOHYDRATE SEQUENCE; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MANNOSYL-GLYCOPROTEIN ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; MOLECULAR SEQUENCE DATA; MUTATION;

ARTHROBACTER;

EID: 36849015794     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm124     Document Type: Article

References (27)

1. Suzuki, T., Yano, K., Sugimoto, S., Kitajima, K., Lennarz, W.J., Inoue, S., Inoue, Y., and Emori, Y. (2002) Endo-β-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol. Proc. Natl. Acad. Sci. USA 99, 9691-9696
2. Maeda, M. and Kimura, Y. (2005) N-Glycan metabolism and plant cell differentiation and growth. Trends Glycosci. Glycotech. 17, 205-214
3. Kato, T., Fujita, K., Takeuchi, M., Kobayashi, K., Natsuka, S., Ikura, K., Kumagai, H., and Yamamoto, K. (2002) Identification of an endo-β-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli. Glycobiology 12, 581-587
4. Fujita, K., Kobayashi, K., Iwamatsu, A., Takeuchi, M., Kumagai, H., and Yamamoto, K. (2004) Molecular cloning of Mucor hiemalis endo-β-N-acetylglucosaminidase and some properties of the recombinant enzyme. Arch. Biochem. Biophys. 432, 41-49
5. Fujita, K., Takami, H., Yamamoto, K., and Takegawa, K. (2004) Characterization of endo-β-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125. Biosci. Biotechnol. Biochem. 68, 1059-1066
6. Takegawa, K., Yamabe, K., Fujita, K., Tabuchi, M., Mita, M., Izu, H., Watanabe, A., Asada, Y., Sano, M., Kondo, A., Kato, I., and Iwahara, S. (1997) Cloning, sequencing, and expression of Arthrobacter protophormiae endo-β-N-acetylglucosaminidase in Escherichia coli. Arch. Biochem. Biophys. 338, 22-28
7. Muramatsu, H., Tachikui, H., Ushida, H., Song, X., Qiu, Y., Yamamoto, S., and Muramatsu, T. (2001) Molecular cloning and expression of endo-β-N-acetylglucosaminidase D, which acts on the core structure of complex type asparagine-linked oligosaccharides. J. Biochem. 129, 923-928
8. Takegawa, K., Tabuchi, M., Yamaguchi, S., Kondo, A., Kato, I., and Iwahara, S. (1995) Synthesis of neoglycoproteins using oligosaccharide-transfer activity with endo-β-N-acetylglucosaminidase. J. Biol. Chem. 270, 3094-3099
9. Fujita, K. and Yamamoto, K. (2006) A remodeling system for the oligosaccharide chains on glycoproteins with microbial endo-β-N- acetylglucosaminidases. Biochim. Biophys. Acta. 1760, 1631-1635
10. Fujita, K. and Takegawa, K. (2001) Tryptophan-216 is essential for the transglycosylation activity of endo-β-N-acetylglucosaminidase A. Biochem. Biophys. Res. Commun. 283, 680-686
11. Yamamoto, S., Muramatsu, H., and Muramatsu, T. (2005) Mutational studies on endo-β-N-acetylglucosaminidase D which hydrolyzes core portion of asparagine-linked complex type oligosaccharides. Glycoconj. J. 22, 35-42
12. Ly, H.D. and Withers, S.G. (1999) Mutagenesis of glycosidases. Annu. Rev. Biochem. 68, 487-522
13. Huang, C.C., Mayer, H.E.J., and Montgomery, R. (1970) Microheterogeneity and paucidispersity of glycoproteins; Part 1. The carbohydrate of chicken ovalbumin. Carbohydr. Res. 13, 127-137
14. Takegawa, K., Nakoshi, M., Iwahara, S., Yamamoto, K., and Tochikura, T. (1989) Induction and purification of endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae grown in ovalbumin. Appl. Environ. Microbiol. 55, 3107-3112
15. 1H coupling constants. Carbohydr. Res. 143, 21-41
16. Tews, I., Terwisscha van Scheltinga, A.C., Perrakis, A., Wilson, K.S., and Dijkstra, B.W. (1997) Substrate-assisted catalysis unifies two families of ehitinolytic enzymes. J. Am. Chem. Soc. 119, 7954-7959
17. Rao, V., Cui, T., Guan, C., and Van Roey, P. (1999) Mutations of endo-β-N-acetylglucosaminidase H active site residue Asp130 and Glu132: activities and conformations. Protein Sci. 8, 2338-2346
18. Waddling, C.A., Plummer Jr, T.H., Tarentino, A.L., and Van Roey, P. (2000) Structural basis for the substrate specificity of endo-β-N- acetylglucosaminidase F(3). Biochemistry 39, 7878-7885
19. Takegawa, K., Yamaguchi, S., Kondo, A., Iwamoto, H., Nakoshi, M., Kato, I., and Iwahara, S. (1991) Transglycosylation activity of endo-β-N- acetylglucosaminidase from Arthrobacter protophormiae. Biochim. Int. 24, 849-855
20. Fan, J.Q., Takegawa, K., Iwahara, S., Kondo, A., Kato, I., Abeygunawardana, C., and Lee, Y.C. (1995) Enhanced transglycosylation activity of Arthrobacter protophormiae endo-β-N-acetylglucosaminidase in media containing organic solvents. J. Biol. Chem. 270, 17723-17729
21. Terwisscha van Scheltinga, A.C., Armand, S., Kalk, K.H., Isogai, A., Henrissat, B., and Dijkstra, B.W. (1995) Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry 34, 15619-15623
22. Mark, B.L., Vocadlo, D.J., Knapp, S., Triggs-Raine, B.L., Withers, S.G., and James, M.N. (2001) Crystallographic evidence for substrate-assisted catalysis in a bacterial β-hexosaminidase. J. Biol. Chem. 276, 10330-10337
23. Markovic-Housley, Z., Miglierini, G., Soldatova, L., Rizkallah, P.J., Muller, U., and Schirmer, T. (2000) Crystal structure of hyaluronidase, a major allergen of bee venom. Structure 8, 1025-1035
24. Macauley, M.S., Whitworth, G.E., Debowski, A.W., Chin, D., and Vocadlo, D.J. (2005) O-GlcNAcase uses substrate-assisted catalysis: Kinetic analysis and development of highly selective mechanism-inspired inhibitors. J. Biol. Chem. 280, 25313-25322
25. Fujita, M., Shoda, S., Haneda, K., Inazu, T., Takegawa, K., and Yamamoto, K. (2001) A novel disaccharide substrate having 1,2-oxazoline moiety for detection of transglycosylating activity of endoglycosidases. Biochim. Biophys. Acta. 1528, 9-14
26. Zeng, Y., Wang, J., Li, B., Hauser, S., Li, H., and Wang, L.X. (2006) Glycopeptide synthesis through endo-glycosidase-catalyzed oligosaccharide transfer of sugar oxazolines: probing substrate structural requirement. Chemistry 12, 3355-3364
27. Li, B., Song, H., Hauser, S., and Wang, L.X. (2006) A highly efficient chemoenzymatic approach toward glycoprotein synthesis. Org. Lett. 8, 3081-3084