Substrate specificity of a novel serine protease from soybean [Glycine max (L.) Merrill]

Journal of Biochemistry

Volumn 119, Issue 6, 1996, Pages 1094-1099

  Morita, Shimpei ^a   Fukase, Masami ^a   Yamaguchi, Masami ^a   Morita, Yuhei ^a  

^a FUJI OIL CO LTD   (Japan)

Author keywords

Arginine specific protease; Serine protease; Soybean; Substrate specificity

Indexed keywords

ARGININE; MONOCLONAL ANTIBODY; NEUROPEPTIDE; SERINE PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; CULTIVAR; ENZYME SPECIFICITY; ENZYME SUBSTRATE; NONHUMAN; PLANT SEED; SOYBEAN;

GLYCINE MAX; SUIDAE;

EID: 0029973765     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021353     Document Type: Article

References (27)

1. Morita, S., Fukase, M., Hoshino, K., Fukuda, Y., Yamaguchi, M., and Morita, Y. (1994) A serine protease in soybean seeds that acts specifically on the native α subunit of β-conglycinin. Plant Cell Physiol. 35, 1049-1056
2. Sebastiani, F.L., Farrell, L.B., Schuler, M.A., and Beachy, R.N. (1990) Complete sequence of cDNA of a subunit of β-conglycinin. Plant Mol. Biol. 15, 197-201
3. Morita, S., Fukase, M., Hoshino, K., Fukuda, Y., Yamaguchi, M., and Morita, Y. (1996) Partial purification and characterization of a novel soybean protease which is inhibited by Kunitz and Bowman-Birk trypsin inhibitors. J. Biochem. 119, 711-718
4. Nielsen, N.C., Dickerson, C.D., Cho, T.-J., Thanh, V.H., Scallon, B.J., Fischer, R.L., Sims, T.L., Drews, G.N., and Goldberg, R.B. (1989) Characterization of the glycinin gene family in soybean. Plant Cell 1, 313-328
5. Thanh, V.H. and Shibasaki, K. (1976) Heterogeneity of beta-conglycinin. Biochim. Biophys. Acta 439, 326-338
6. Iwabuchi, S. and Yamauchi, F. (1987) Determination of glycinin and β-conglycinin in soybean proteins by immunological methods. J. Agric. Food Chem. 35, 200-205
7. Iwabuchi, S. and Yamauchi, F. (1987) Electrophoretic analysis of whey proteins in soybean globulin fractions. J. Agric. Food Chem. 35, 205-209
8. Yamauchi, F., Sato, M., Sato,Y., Kamata, Y., and Shibasaki, K. (1981) Isolation and identification of a new type of β-conglycinin in soybean globulins. Agric. Biol. Chem. 45, 2863-2868
9. Sykes, G.E. and Gayler, K.G. (1981) Detection and characterization of a new β-conglycinin from soybean seeds. Arch. Biochem. Biophys. 210, 525-530
10. Sato, W., Kamata, Y., Fukuda, M., and Yamauchi, F. (1984) Improved isolation method and some properties of soybean gamma-conglycinin. Phytochemistry 23, 1523-1526
11. Qi, X., Wilson, K.A., and Tan-Wilson, A.L. (1992) Characterization of the major protease involved in the soybean β-conglycinin in storage protein mobilization. Plant Physiol. 99, 725-733
12. Morita, T., Kato, H., Iwanaga, S., Takada, K., Kimura, T., and Sakakibara, S. (1977) Fluorogenic substrates for α-thrombin, factor Xa, kallikreins, and urokinase. J. Biochem. 82, 1495-1498
13. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
14. Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
15. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
16. Tierney, M.L., Bray, E.A., Allen, R.D., Ma, Y., Drong, R.F., Slighton, J., and Beachy, R.N. (1987) Isolation and characterization of a genomic clone encoding the β-subunit of β-conglycinin. Planta 172, 356-363
17. Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954
18. Spackman, D.H., Stein, W.H., and Moore, S. (1958) Automatic recording apparatus for use in the chromatography of amino acids. Anal. Chem. 30, 1190-1206
19. 2-macroglobulin from porcine gastric mucosa. J. Biol. Chem. 268, 527-533
20. Tsuchiya, Y., Takahashi, T., Sakurai, Y., Iwamatsu, A., and Takahashi, K. (1994) Purification and characterization of a novel membrane-bound arginine-specific serine proteinase from porcine intestinal mucosa. J. Biol. Chem. 269, 32985-32991
21. Doyle, J.J., Schuler, M.A., Godette, W.D., Zenger, V., and Beachy, R.N. (1986) The glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris. J. Biol. Chem. 261, 9228-9238
22. Johnson, S., Grayson, G., Robinson, L., Chahade, R., and McPherson, A. (1982) Biochemical and crystallographic data for phaseolin, a storage protein from Phaseolus vulgaris. Biochemistry 21, 4839-4843
23. Ng, J.D., Ko, T.-P., and McPherson, A. (1993) Cloning, expression, and crystallization of jack bean (Canavalia ensiformis) canavalin. Plant Physiol. 101, 713-728
24. Nishikata, M. (1984) Trypsin-like protease from soybean seeds. Purification and some properties. J. Biochem. 95, 1169-1177
25. Siezen, R.J., Creemers, J.W.M., and van de Ven, W.J.M. (1992) Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases. Eur. J. Biochem. 222, 255-266
26. Schechter, I. and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
27. Perona, J.J. and Craik, C.S. (1995) Structural basis of substrate specificity in the serine proteases. Protein Science 4, 337-360