Identification of reactive site of a proteinaceous metalloproteinase inhibitor from Streptomyces nigrescens TK-23

Journal of Biochemistry

Volumn 121, Issue 6, 1997, Pages 1088-1095

  Seeram, Sailaja S ^a   Hiraga, Kazumi ^a   Saji, Atsushi ^a   Tashiro, Misao ^b   Oda, Kohei ^a  

^a KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

^b KYOTO PREFECTURAL UNIVERSITY   (Japan)

Author keywords

K(i) value; Metalloproteinase; Proteinaceous inhibitor; Reactive site; Streptomyces

Indexed keywords

BACTERIAL ENZYME; METALLOPROTEINASE INHIBITOR; MUTANT PROTEIN; THERMOLYSIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME INHIBITION; ENZYME SPECIFICITY; INHIBITION KINETICS; NONHUMAN; PROTEIN DEGRADATION; STREPTOMYCES; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS); STREPTOMYCES; STREPTOMYCES NIGRESCENS;

EID: 0030873066     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021699     Document Type: Article

References (39)

1. Rawlings, N.D. and Barrett, A.J. (1995) Evolutionary families of metallopeptidases in Methods in Enzymology (Barrett, A.J., ed.) Vol. 248, pp. 183-228, Academic Press, New York
2. Oda, K., Koyama, T., and Murao, S. (1979) Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. Biochim. Biophys. Acta 571, 147-156
3. Murai, H., Hara, S., Ikenaka, T., Oda, K., and Murao, S. (1985) Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. J. Biochem. 97, 173-180
4. Létoffé, S., Delepelaire, P., and Wandersman, C. (1989) Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthemi. Mol. Microbiol. 3, 79-86
5. Duong, F., Lazdunski, A., Cami, B., and Murgier, M. (1992) Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways. Gene 121, 47-54
6. Suh, Y. and Benedik, M.J. (1992) Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysin HlyB and HlyD. J. Bacteriol. 174, 2361-2366
7. Kim, K.S., Kim, T.U., Kim, I.J., Byun, S.M., and Shin, Y.C. (1995) Characterization of a metalloprotease inhibitor protein (SmaPI) of Serratia marcescens. Appl. Environ. Microbiol. 61, 3035-3041
8. Tanabe, M., Asano, T., Moriya, N., Sugino, H., and Kakinuma, A. (1994) Isolation and characterization of Streptoverticillium anticoagulant (SAC), a novel protein inhibitor of blood coagulation produced by Streptoverticillium cinnamoneum subsp. cinnamoneum. J. Biochem. 115, 743-751
9. Tanabe, M., Kawahara, K., Asano, T., Kato, K., and Kakinuma, A. (1994) Primary structure and reactive site of Streptoverticillium anticoagulant (SAC), a novel protein inhibitor of blood coagulation produced by Streptoverticillium cinnamoneum subsp. cinnamoneum. J. Biochem. 115, 752-761
10. Catanese, J.J. and Kress, L.F. (1992) Isolation from opossum serum of a metalloproteinase inhibitor homologous to human α1B-glycoprotein. Biochemistry 31, 410-418
11. Yamakawa, Y. and Omori-Satoh, T. (1992) Primary structure of the antihemorrhagic factor in serum of the Japanese habu: a snake venom metalloproteinase inhibitor with a double-headed cystatin domain. J. Biochem. 112, 583-589
12. Finkenstadt, W.R. and Laskowski, M., Jr. (1965) Peptide bond cleavage on trypsin-trypsin inhibitor complex formation. J. Biol. Chem. 240, 962-963
13. Ozawa, K. and Laskowski, M., Jr. (1966) The reactive site of trypsin inhibitors. J. Biol. Chem. 241, 3955-3961
14. Tanaka, K., Saito, H., Arai, M., Murao, S., and Takahashi, H. (1988) Cloning and expression of the metallo-proteinase inhibitor (S-MPI) gene from Streptomyces nigrescens. Biochem. Biophys. Res. Commun. 155, 487-492
15. Tanaka, K., Aoki, H., Oda, K., Murao, S., Saito, H., and Takahashi, H. (1990) Nucleotide sequence of the gene for a metalloproteinase inhibitor of Streptomyces nigrescens (SMPI). Nucleic Acids Res. 18, 6433
16. Higuchi, R. (1990) Recombinant PCR in PCR Protocols: A Guide to Methods and Applications (Innis, M.A., Gelfand, D.H., Sninsky, J.J., and White, T.J., eds.) pp. 177-183, Academic Press, New York
17. Habig, W.H., Pabst, M.J., and Jakoby, W.B. (1974) Glutathione S-transferases. J. Biol. Chem. 249, 7130-7139
18. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
19. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
20. 2-terminal sequences of peptides electroblotted onto PVDF membranes from tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Application to peptide mapping of human complement component C3. Anal. Biochem. 181, 33-39
21. Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
22. Kitagishi, K. and Hiromi, K. (1984) Binding between thermolysin and its specific inhibitor, phosphoramidon. J. Biochem. 95, 529-534
23. Knight, C.G., Willenbrock, F., and Murphy, G. (1992) A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett. 296, 263-266
24. Tashiro, M., Kihira, Y., Katayama, Y., and Maki, Z. (1989) Purification and characterization of a major trypsin inhibitor, FMTI-II, from foxtail millet grain. Agric. Biol. Chem. 53, 443-451
25. Murao, S., Katsura, M., Fukuhara, K., and Oda, K. (1980) New metalloproteinase inhibitor (MK-I) produced by Streptomyces mozunensis MK-23. Agric. Biol. Chem. 44, 701-703
26. Murphy, G., Koklitis, P., and Carne, A.F. (1989) Dissociation of tissue inhibitor of metalloproteinases (TIMP) from enzyme complexes yields fully active inhibitor. Biochem. J. 261, 1031-1034
27. Laskowski, M., Jr. and Kato, I. (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626
28. Laskowski, M., Jr. (1980) An algorithmic approach to sequence →reactivity of proteins. Biochem. Pharmacol. 29, 2089-2094
29. Ghrayeb, J., Kimura, H., Takahara, M., Hsiung, H., Masui, Y., and Inouye, M. (1984) Secretion cloning vectors in Escherichia coli. EMBO J. 3, 2437-2442
30. Taguchi, S., Yoshida, Y., Matsumoto, K., and Momose, H. (1993) Improved leader and putative terminator sequences for high-level production of Streptomyces subtilisin inhibitor in Escherichia coli. Appl. Microbiol. Biotechnol. 39, 732-737
31. Tsuru, D., Fujita, Y., Morikawa, S., Ito, K., and Yoshimoto, T. (1992) Degradation of Streptomyces metalloproteinase inhibitor (SMPI) by neutral protease from Bacillus subtilis var. amylosacchariticus. Biosci. Biotech. Biochem. 56, 1275-1278
32. Matsubara, H. (1970) Purification and assay of thermolysin in Methods in Enzymology (Perlmann, G.E. and Lorand, L., eds.) Vol. XIX, pp. 642-651, Academic Press, New York and London
33. Morihara, K. and Tsuzuki, H. (1970) Thermolysin: Kinetic study with oligopeptides. Eur. J. Biochem. 15, 374-380
34. Pozsgay, M., Michaud, C., Liebman, M., and Orlowski, M. (1986) Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions. Comparison with bacterial thermolysin. Biochemistry 25, 1292-1299
35. Hersh, L.B. and Morihara, K. (1986) Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin. J. Biol. Chem. 261, 6433-6437
36. Matsubara, H., Sasaki, R., Singer, A., and Jukes, T.H. (1966) Specific nature of hydrolysis of insulin and tobacco mosaic virus protein by thermolysin. Arch. Biochem. Biophys. 115, 324-331
37. Matsubara, H. (1966) Observations of the specificity of thermolysin with synthetic peptides. Biochem. Biophys. Res. Commun. 24, 427-430
38. Matsubara, H., Singer, A., Sasaki, R., and Jukes, T.H. (1965) Observations on the specificity of a thermostable bacterial protease "Thermolysin." Biochem. Biophys. Res. Commun. 21, 242-247
39. Schechter, I. and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162