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Volumn 141, Issue 6, 2007, Pages 843-853

Kinetic analysis of the activation-and-inhibition dual effects of cobalt ion on thermolysin activity

Author keywords

Cobalt ion; Inhibition; Metalloproteinase; Thermolysin; Zinc ion

Indexed keywords

AMIDE; BROMIDE; CHLORIDE; COBALT; ESTER DERIVATIVE; N [3 (2 FURYL)ACRYLOYL]GLYCYLLEUCINE AMIDE; N CARBOBENZOXY ASPERTYLPHENYLALANINE METHYL ESTER; POTASSIUM; SODIUM; THERMOLYSIN; UNCLASSIFIED DRUG; ZINC; ACRYLIC ACID DERIVATIVE; BROMINE; CHLORINE; DIPEPTIDE; ION; N (3 (2 FURYL)ACRYLOYL)GLYCYL LEUCINAMIDE; N-(3-(2-FURYL)ACRYLOYL)GLYCYL-LEUCINAMIDE; ZINC CHLORIDE; ZINC DERIVATIVE;

EID: 38449112649     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm088     Document Type: Article
Times cited : (15)

References (50)
  • 1
    • 0001094555 scopus 로고
    • Studies on protease produced by thermophilic bacteria
    • Endo, S. (1962) Studies on protease produced by thermophilic bacteria. J. Ferment. Technol. 40, 346-353
    • (1962) J. Ferment. Technol , vol.40 , pp. 346-353
    • Endo, S.1
  • 2
    • 77956941440 scopus 로고    scopus 로고
    • Matsubara, H. and Feder, J. (1971) Other bacterial, mold, and yeast proteases in The Enzymes (Boyer, P.D., ed.) 3, 3rd edn, pp. 721-795, Academic Press, New York
    • Matsubara, H. and Feder, J. (1971) Other bacterial, mold, and yeast proteases in The Enzymes (Boyer, P.D., ed.) Vol. 3, 3rd edn, pp. 721-795, Academic Press, New York
  • 3
    • 84944059375 scopus 로고    scopus 로고
    • Van der Burg, B. and Eijsink, V. (2004) Thermolysin in Handbook of Proteolytic Enzymes (Barrett, J.A., Rawlings, N.D., and Woessner, J. F., eds) 1, 2nd edn, pp. 374-387, Elsevier, Amsterdam, The Netherlands
    • Van der Burg, B. and Eijsink, V. (2004) Thermolysin in Handbook of Proteolytic Enzymes (Barrett, J.A., Rawlings, N.D., and Woessner, J. F., eds) Vol. 1, 2nd edn, pp. 374-387, Elsevier, Amsterdam, The Netherlands
  • 4
    • 41449087922 scopus 로고    scopus 로고
    • Inouye, K. (2003) Thermolysin in Handbook of Food Enzymes (Whitaker, J.R., Voragen, A.G.J., and Wong, D.W.S., eds) pp. 1019-1028, Marcel Dekker, New York, New York
    • Inouye, K. (2003) Thermolysin in Handbook of Food Enzymes (Whitaker, J.R., Voragen, A.G.J., and Wong, D.W.S., eds) pp. 1019-1028, Marcel Dekker, New York, New York
  • 6
    • 0015237801 scopus 로고
    • Studies on the role of calcium in thermolysin
    • Feder, J., Garrett, L.R., and Wildi, B.S. (1971) Studies on the role of calcium in thermolysin. Biochemistry 10, 4552-4555
    • (1971) Biochemistry , vol.10 , pp. 4552-4555
    • Feder, J.1    Garrett, L.R.2    Wildi, B.S.3
  • 7
    • 0017278562 scopus 로고
    • Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease
    • Tajima, M., Urabe, I., Yutani, K., and Okada, H. (1976) Role of calcium ions in the thermostability of thermolysin and Bacillus subtilis var. amylosacchariticus neutral protease. Eur. J. Biochem. 64, 243-247
    • (1976) Eur. J. Biochem , vol.64 , pp. 243-247
    • Tajima, M.1    Urabe, I.2    Yutani, K.3    Okada, H.4
  • 8
    • 0014828815 scopus 로고
    • Thermolysin: Kinetic study with oligopeptides
    • Morihara, K. and Tsuzuki, H. (1970) Thermolysin: kinetic study with oligopeptides. Eur. J. Biochem. 15, 374-380
    • (1970) Eur. J. Biochem , vol.15 , pp. 374-380
    • Morihara, K.1    Tsuzuki, H.2
  • 10
    • 0028306090 scopus 로고
    • Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin
    • O'Donohue, M.J., Roques, B.P., and Beaumont, A. (1994) Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin. Biochem. J. 300, 599-603
    • (1994) Biochem. J , vol.300 , pp. 599-603
    • O'Donohue, M.J.1    Roques, B.P.2    Beaumont, A.3
  • 11
    • 0020462668 scopus 로고
    • Structure of thermolysin refined at 1.6Å resolution
    • Holmes, M.A. and Matthews, B.W. (1982) Structure of thermolysin refined at 1.6Å resolution. J. Mol. Biol. 160, 623-639
    • (1982) J. Mol. Biol , vol.160 , pp. 623-639
    • Holmes, M.A.1    Matthews, B.W.2
  • 12
    • 0021744255 scopus 로고
    • An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides
    • Hangauer, D.G., Monzingo, A.F., and Matthews, B.W. (1984) An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides. Biochemistry 23, 5730-5741
    • (1984) Biochemistry , vol.23 , pp. 5730-5741
    • Hangauer, D.G.1    Monzingo, A.F.2    Matthews, B.W.3
  • 13
    • 0028169317 scopus 로고
    • Binding to thermolysin of phenolate-containing inhibitors necessitates a revised mechanism of catalysis
    • Mock, W.L. and Aksamawati, M. (1994) Binding to thermolysin of phenolate-containing inhibitors necessitates a revised mechanism of catalysis. Biochem. J. 302, 57-68
    • (1994) Biochem. J , vol.302 , pp. 57-68
    • Mock, W.L.1    Aksamawati, M.2
  • 14
    • 0029896448 scopus 로고    scopus 로고
    • Arazoformyl dipeptide substrate for thermolysin. Confirmation of reverse protonation catalytic mechanism
    • Mock, W.L. and Stanford, D.J. (1996) Arazoformyl dipeptide substrate for thermolysin. Confirmation of reverse protonation catalytic mechanism. Biochemistry 35, 7369-7377
    • (1996) Biochemistry , vol.35 , pp. 7369-7377
    • Mock, W.L.1    Stanford, D.J.2
  • 15
    • 0026799337 scopus 로고
    • Effects of salts on thermolysin: Activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin
    • Inouye, K. (1992) Effects of salts on thermolysin: activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. J. Biochem. 112, 335-340
    • (1992) J. Biochem , vol.112 , pp. 335-340
    • Inouye, K.1
  • 16
    • 0029863639 scopus 로고    scopus 로고
    • Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts
    • Inouye, K., Lee, S.-B., and Tonomura, B. (1996) Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem. J. 315, 133-138
    • (1996) Biochem. J , vol.315 , pp. 133-138
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3
  • 17
    • 0030772527 scopus 로고    scopus 로고
    • Effects of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts
    • Inouye, K., Lee, S.-B., Nambu, K., and Tonomura, B. (1997) Effects of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts. J. Biochem. 122, 358-364
    • (1997) J. Biochem , vol.122 , pp. 358-364
    • Inouye, K.1    Lee, S.-B.2    Nambu, K.3    Tonomura, B.4
  • 18
    • 4644307860 scopus 로고    scopus 로고
    • Substrate-dependent activation of thermolysin by salt
    • Oneda, H., Muta, Y., and Inouye, K. (2004) Substrate-dependent activation of thermolysin by salt. Biosci. Biotechnol. Biochem. 68, 1811-1813
    • (2004) Biosci. Biotechnol. Biochem , vol.68 , pp. 1811-1813
    • Oneda, H.1    Muta, Y.2    Inouye, K.3
  • 19
    • 0028129002 scopus 로고
    • A spectrophotometric study on the interaction of thermolysin with chloride and bromide ions, and the state of tryptophyl residue 115
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1994) A spectrophotometric study on the interaction of thermolysin with chloride and bromide ions, and the state of tryptophyl residue 115. J. Biochem. 116, 530-535
    • (1994) J. Biochem , vol.116 , pp. 530-535
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 20
    • 0031848311 scopus 로고    scopus 로고
    • Effects of nitration and amination of tyrosyl residues in thermolysin on its hydrolytic activity and its remarkable activation by salts
    • Inouye, K., Lee, S.-B., and Tonomura, B. (1998) Effects of nitration and amination of tyrosyl residues in thermolysin on its hydrolytic activity and its remarkable activation by salts. J. Biochem. 124, 72-78
    • (1998) J. Biochem , vol.124 , pp. 72-78
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3
  • 21
    • 0031979332 scopus 로고    scopus 로고
    • Effect of salts on the solubility of thermolysin: A remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1998) Effect of salts on the solubility of thermolysin: a remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin. J. Biochem. 123, 847-852
    • (1998) J. Biochem , vol.123 , pp. 847-852
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 22
    • 0032517347 scopus 로고    scopus 로고
    • Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1998) Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity. Biochim. Biophys. Acta 1388, 209-214
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 209-214
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 23
    • 23844445212 scopus 로고    scopus 로고
    • Preliminary X-ray crystallographic analysis of thermolysin in the presence of 4M NaCl
    • Kamo, M., Inouye, K., Nagata, K., and Tanokura, M. (2005) Preliminary X-ray crystallographic analysis of thermolysin in the presence of 4M NaCl. Acta Crystallogr. D61, 710-712
    • (2005) Acta Crystallogr , vol.D61 , pp. 710-712
    • Kamo, M.1    Inouye, K.2    Nagata, K.3    Tanokura, M.4
  • 24
    • 33645384438 scopus 로고    scopus 로고
    • Characterization of Gly-D-Phe, Gly-L-Leu, and D-Phe as affinity ligands to thermolysin
    • Yasukawa, K., Kusano, M., Nakamura, K., and Inouye, K. (2006) Characterization of Gly-D-Phe, Gly-L-Leu, and D-Phe as affinity ligands to thermolysin. Protein Expr. Purif. 46, 332-336
    • (2006) Protein Expr. Purif , vol.46 , pp. 332-336
    • Yasukawa, K.1    Kusano, M.2    Nakamura, K.3    Inouye, K.4
  • 25
    • 33645411423 scopus 로고    scopus 로고
    • Extracellular production of recombinant thermolysin expressed in Escherichia coli, and its purification and enzymatic characterization
    • Inouye, K., Minoda, M., Takita, T., Sakurama, H., Hashida, Y., Kusano, M., and Yasukawa, K. (2006) Extracellular production of recombinant thermolysin expressed in Escherichia coli, and its purification and enzymatic characterization. Protein Expr. Purif. 46, 248-255
    • (2006) Protein Expr. Purif , vol.46 , pp. 248-255
    • Inouye, K.1    Minoda, M.2    Takita, T.3    Sakurama, H.4    Hashida, Y.5    Kusano, M.6    Yasukawa, K.7
  • 26
    • 33746883914 scopus 로고    scopus 로고
    • Engineering of the pH dependence of thermolysin activity as examined by site-directed mutagenesis of Asn 112 located at the active site of thermolysin
    • Kusano, M., Yasukawa, K., Hashida, Y., and Inouye, K. (2006) Engineering of the pH dependence of thermolysin activity as examined by site-directed mutagenesis of Asn 112 located at the active site of thermolysin. J. Biochem. 139, 1017-1023
    • (2006) J. Biochem , vol.139 , pp. 1017-1023
    • Kusano, M.1    Yasukawa, K.2    Hashida, Y.3    Inouye, K.4
  • 27
    • 34748868292 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis of the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity
    • in press, doi:10.1093/jb/mvm087
    • Tatsumi, C., Hashida, Y., Yasukawa, K., and Inouye, K. (2007) Effects of site-directed mutagenesis of the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity. J. Biochem. 141 (in press); doi:10.1093/jb/mvm087
    • (2007) J. Biochem , vol.141
    • Tatsumi, C.1    Hashida, Y.2    Yasukawa, K.3    Inouye, K.4
  • 28
    • 2442670073 scopus 로고    scopus 로고
    • Analysis of autodegradation sites of thermolysin and enhancement of its thermostability by modifying Leu155 at an autodegradation site
    • Matsumiya, Y., Nishikawa, K., Aoshima, H., Inouye, K., and Kubo, M. (2004) Analysis of autodegradation sites of thermolysin and enhancement of its thermostability by modifying Leu155 at an autodegradation site. J. Biochem. 135, 547-553
    • (2004) J. Biochem , vol.135 , pp. 547-553
    • Matsumiya, Y.1    Nishikawa, K.2    Aoshima, H.3    Inouye, K.4    Kubo, M.5
  • 29
    • 17644368559 scopus 로고    scopus 로고
    • Mutational effect for stability in a conserved region of thermolysin
    • Matsumiya, Y., Nishikawa, K., Inouye, K., and Kubo, M. (2005) Mutational effect for stability in a conserved region of thermolysin. Lett. Appl. Microbiol. 40, 329-334
    • (2005) Lett. Appl. Microbiol , vol.40 , pp. 329-334
    • Matsumiya, Y.1    Nishikawa, K.2    Inouye, K.3    Kubo, M.4
  • 30
    • 0014431088 scopus 로고
    • A spectrophotometric assay for neutral protease
    • Feder, J. (1968) A spectrophotometric assay for neutral protease. Biochem. Biophys. Res. Commun. 32, 326-332
    • (1968) Biochem. Biophys. Res. Commun , vol.32 , pp. 326-332
    • Feder, J.1
  • 31
    • 0037067022 scopus 로고    scopus 로고
    • Improvement and biological applications of fluorescent probes for zinc, ZnAFs
    • Hirano, T., Kikuchi, K., Urano, Y., and Nagano, T. (2002) Improvement and biological applications of fluorescent probes for zinc, ZnAFs. J. Am. Chem. Soc. 124, 6555-6562
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6555-6562
    • Hirano, T.1    Kikuchi, K.2    Urano, Y.3    Nagano, T.4
  • 32
    • 0035660278 scopus 로고    scopus 로고
    • Effect of cobalt-substitution of active zinc ion in thermolysin on its activity and active-site microenvironment
    • Kuzuya, K. and Inouye, K. (2001) Effect of cobalt-substitution of active zinc ion in thermolysin on its activity and active-site microenvironment. J. Biochem. 130, 783-788
    • (2001) J. Biochem , vol.130 , pp. 783-788
    • Kuzuya, K.1    Inouye, K.2
  • 33
    • 0015220760 scopus 로고
    • Studies on the inhibition of neutral proteases by 1,10-phenanthroline
    • Feder, J., Garrett, L.R., and Kochavi, D. (1971) Studies on the inhibition of neutral proteases by 1,10-phenanthroline. Biochim. Biophys. Acta 235, 370-377
    • (1971) Biochim. Biophys. Acta , vol.235 , pp. 370-377
    • Feder, J.1    Garrett, L.R.2    Kochavi, D.3
  • 34
    • 0016170446 scopus 로고
    • Metal substitutions and inhibition of thermolysin: Spectra of the cobalt enzyme
    • Holmquist, B. and Vallee, B.L. (1974) Metal substitutions and inhibition of thermolysin: Spectra of the cobalt enzyme. J. Biol. Chem. 249, 4601-4607
    • (1974) J. Biol. Chem , vol.249 , pp. 4601-4607
    • Holmquist, B.1    Vallee, B.L.2
  • 35
    • 0028892387 scopus 로고
    • Structural analysis of zinc substitutions in the active site of thermolysin
    • Holland, D.R., Hausrath, A.C., Juers, D., and Matthews, B.W. (1995) Structural analysis of zinc substitutions in the active site of thermolysin. Protein Sci. 4, 1955-1965
    • (1995) Protein Sci , vol.4 , pp. 1955-1965
    • Holland, D.R.1    Hausrath, A.C.2    Juers, D.3    Matthews, B.W.4
  • 36
    • 0001020311 scopus 로고
    • Metallocarboxypeptidases
    • Coleman, J.E. and Vallee, B.L. (1960) Metallocarboxypeptidases. J. Biol. Chem. 235, 390-395
    • (1960) J. Biol. Chem , vol.235 , pp. 390-395
    • Coleman, J.E.1    Vallee, B.L.2
  • 37
    • 0001023773 scopus 로고
    • Metallocarboxypeptidases: Stability constants and enzymatic characteristics
    • Coleman, J.E. and Vallee, B.L. (1961) Metallocarboxypeptidases: stability constants and enzymatic characteristics. J. Biol. Chem. 236, 2244-2249
    • (1961) J. Biol. Chem , vol.236 , pp. 2244-2249
    • Coleman, J.E.1    Vallee, B.L.2
  • 38
    • 0022364289 scopus 로고
    • The functional role of zinc in angiotensin converting enzyme: Implications for the enzyme mechanism
    • Bünning, P. and Riordan, J.F. (1985) The functional role of zinc in angiotensin converting enzyme: implications for the enzyme mechanism. J. Inorg. Biochem. 24, 183-198
    • (1985) J. Inorg. Biochem , vol.24 , pp. 183-198
    • Bünning, P.1    Riordan, J.F.2
  • 39
    • 0021093462 scopus 로고
    • Kinetic parameters of metal-substituted leucine aminopeptidase from bovine lens
    • Allen, M.P., Yamada, A.H., and Carpenter, F.H. (1983) Kinetic parameters of metal-substituted leucine aminopeptidase from bovine lens. Biochemistry 22, 3778-3783
    • (1983) Biochemistry , vol.22 , pp. 3778-3783
    • Allen, M.P.1    Yamada, A.H.2    Carpenter, F.H.3
  • 40
    • 0022392470 scopus 로고
    • Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: Nonidentical, interacting metal-binding sites
    • Prescott, J.M., Wagner, F.W., Holmquist, B., and Vallee, B.L. (1985) Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites. Biochemistry 24, 5350-5356
    • (1985) Biochemistry , vol.24 , pp. 5350-5356
    • Prescott, J.M.1    Wagner, F.W.2    Holmquist, B.3    Vallee, B.L.4
  • 42
    • 0042628178 scopus 로고    scopus 로고
    • Substrate specificities of deuterolysin from Aspergillus oryzae and electron paramagnetic resonance measurement of cobalt-substituted deuterolysin
    • Doi, Y., Lee, B.R., Ikeguchi, M., Ohoba, Y., Ikoma, T., Tero-Kubota, S., Yamauchi, S., Takahashi, K., and Ichishima, E. (2003) Substrate specificities of deuterolysin from Aspergillus oryzae and electron paramagnetic resonance measurement of cobalt-substituted deuterolysin. Biosci. Biotechnol. Biochem. 67, 264-270
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 264-270
    • Doi, Y.1    Lee, B.R.2    Ikeguchi, M.3    Ohoba, Y.4    Ikoma, T.5    Tero-Kubota, S.6    Yamauchi, S.7    Takahashi, K.8    Ichishima, E.9
  • 43
    • 0028302761 scopus 로고
    • Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel(II), and mercury(II) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity
    • Gomis-Ruth, F.X., Grams, F., Yiallouros, I., Nar, H., Kusthardt, U., Zwilling, R., Bode, W., and Stocker, W. (1994) Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel(II), and mercury(II) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity. J. Biol. Chem. 269, 17111-17117
    • (1994) J. Biol. Chem , vol.269 , pp. 17111-17117
    • Gomis-Ruth, F.X.1    Grams, F.2    Yiallouros, I.3    Nar, H.4    Kusthardt, U.5    Zwilling, R.6    Bode, W.7    Stocker, W.8
  • 44
    • 0036936933 scopus 로고    scopus 로고
    • Mechanistic studies of the astacin-like Serratia metalloendopeptidase serralysin: Highly active (>2000%) Co(II) and Cu(II) derivatives for further corroboration of a "metallotriad" mechanism
    • Park, H.I. and Ming, L.J. (2002) Mechanistic studies of the astacin-like Serratia metalloendopeptidase serralysin: highly active (>2000%) Co(II) and Cu(II) derivatives for further corroboration of a "metallotriad" mechanism. J. Biol. Inorg. Chem. 7, 600-610
    • (2002) J. Biol. Inorg. Chem , vol.7 , pp. 600-610
    • Park, H.I.1    Ming, L.J.2
  • 45
    • 0024293209 scopus 로고
    • Preparation and reconstitution with divalent metal ions of class I and class II Clostridium histolyticum apocollagenases
    • Angleton, E.L. and Van Wart, H.E. (1988) Preparation and reconstitution with divalent metal ions of class I and class II Clostridium histolyticum apocollagenases. Biochemistry 27, 7406-7412
    • (1988) Biochemistry , vol.27 , pp. 7406-7412
    • Angleton, E.L.1    Van Wart, H.E.2
  • 46
    • 0024293238 scopus 로고
    • Preparation by direct metal exchange and kinetic study of active site metal substituted class I and class II Clostridium histolyticum collagenases
    • Angleton, E.L. and Van Wart, H.E. (1988) Preparation by direct metal exchange and kinetic study of active site metal substituted class I and class II Clostridium histolyticum collagenases. Biochemistry 27, 7413-7418
    • (1988) Biochemistry , vol.27 , pp. 7413-7418
    • Angleton, E.L.1    Van Wart, H.E.2
  • 48
    • 0023646690 scopus 로고
    • Excess zinc ions are a competitive inhibitor for carboxypeptidase A
    • Hirose, J., Ando, S., and Kidani, Y. (1987) Excess zinc ions are a competitive inhibitor for carboxypeptidase A. Biochemistry 26, 6561-6565
    • (1987) Biochemistry , vol.26 , pp. 6561-6565
    • Hirose, J.1    Ando, S.2    Kidani, Y.3
  • 49
    • 0024817526 scopus 로고
    • Carboxypeptidase A: Mechanism of zinc inhibition
    • Larsen, K.S. and Auld, D.S. (1989) Carboxypeptidase A: mechanism of zinc inhibition. Biochemistry 28, 9620-9625
    • (1989) Biochemistry , vol.28 , pp. 9620-9625
    • Larsen, K.S.1    Auld, D.S.2
  • 50
    • 38449121504 scopus 로고    scopus 로고
    • Molecular mechanism of the inhibitory effect of cobalt ion on thermolysin activity and the suppressive effect of calcium ion on the cobalt iondependent inactivation of thermolysin
    • in press, doi:10.1093/jb/mvm089
    • Hashida, Y. and Inouye, K. (2007) Molecular mechanism of the inhibitory effect of cobalt ion on thermolysin activity and the suppressive effect of calcium ion on the cobalt iondependent inactivation of thermolysin. J. Biochem. 141 (in press); doi:10.1093/jb/mvm089
    • (2007) J. Biochem , vol.141
    • Hashida, Y.1    Inouye, K.2


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