Five crucial carboxyl residues of 1,2-α-mannosidase from Aspergillus saitoi (A. phoenicis), a food microorganism, are identified by site-directed mutagenesis

Biochemical and Biophysical Research Communications

Volumn 238, Issue 3, 1997, Pages 779-783

  Fujita, Akiko ^a   Yoshida, Takashi ^a   Ichishima, Eiji ^a,b  

^a TOHOKU UNIVERSITY   (Japan)

^b SOKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CARBOXYL GROUP; FUNGAL PROTEIN; GLUTAMIC ACID; MANNOSE; MANNOSIDASE; MUTANT PROTEIN; OLIGOSACCHARIDE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ASPERGILLUS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; PH; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

EID: 0031590277     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1997.7389     Document Type: Article

References (26)

1. Ichishima E., Arai M., Shigematsu Y., Kumagai H., Sumida-Tanaka R. Biochim. Biophys. Acta. 658:1981;45-53.
2. Yamashita K., Ichishima E., Arai M., Kobata. Biochem. Biophys. Res. Commun. 96:1980;1335-1342.
3. Shigematsu Y., Tsukahara K., Tanaka T., Takeuchi M., Ichishima E. Curr. Microbiol. 13:1986;43-46.
4. Yoshida T., Shimidzu S., Ichishima E. Phytochemistry. 5:1994;267-269.
5. Inoue T., Yoshida T., Ichishima E. Biochim. Biophys. Acta. 1253:1995;141-145.
6. Creighton T. E. Proteins - Structure and Molecular Properties. 1993;W. H. Freeman and Co. New York. p. 437-441.
7. Moremanen K. W., Trimble R. B., Herscovics A. Glycobiology. 4:1994;113-125.
8. Ockerman P. A. Lancet. II:1996;239-241.
9. Norden N. C., Lindblad A., Ockerman P. A., Jolly R. D. FEBS Lett. 35:1973;209-212.
10. Phillips N. C., Robinson D., Winchester B. C., Jolly R. D. Biochem. J. 137:1974;363-371.
11. Burditt I. J., Phillips N. C., Robinson D., Winchester B. R., Van-De-Water N. S., Jolly R. D. Biochem. J. 175:1978;1013-1022.
12. Webb E. C. NC-IUBMB. Enzyme Nomenclature. 1992;Academic Press, San Diego.
13. Yoshida T., Ichishima E. Biochim. Biophys. Acta. 1263:1995;159-162.
14. Camirand A., Heysen A., Grondin B., Herscovics A. J. Biol. Chem. 266:1991;15120-15127.
15. Herscovics A., Schneikert K., Athanassiadis A., Moremen K. W. J. Biol. Chem. 269:1994;9864-9871.
16. Kunkel T. A., Roberts J. D., Zakour R. A. Methods in Enzymology. 1987;Academic Press, San Diego. p. 367-382.
17. Somogyi M. J. Biol. Chem. 195:1952;19-23.
18. Hase S., Ikenaka T., Matsushima Y. Biochem. Biophys. Res. Commun. 85:1978;257-263.
19. Laemmli U. K. Nature. 227:1970;680-685.
20. Chou P. Y., Fasman G. D. Adv. Enzymol. Relat. Areas Mol. Biol. 47:1978;45-148.
21. Miki T., Yasukochi T., Nagatani H., Furuno M., Orita T., Yamada H., Imoto T., Horiuchi T. Protein Engineering. 1:1987;327-332.
22. Imoto T., Yamada H., Yasukochi T., Yamada E., Ito Y., Ueda T., Nagatani H., Miki T., Horiuchi T. Protein Engineering. 1:1987;333-338.
23. Neubeger A., Brocklehurst K. Neubeger A., Brocklehurst K. Hydrolytic Enzymes. 1987;1-37 Elsevier, Amsterdam/New York/Oxford.
24. Totsuka A., Nong V. H., Kadokawa H., Kim C.-S., Itoh Y., Fukazawa C. Eur. J. Biochem. 221:1994;649-654.
25. Totsuka A., Fukazawa C. Eur. J. Biochem. 240:1996;655-659.
26. Nishio T., Miyake Y., Tsuji H., Hakamata W., Kadokura K., Oku T. Biosci. Biotech. Biochem. 60:1996;2038-2042.