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Volumn 72, Issue 6, 2006, Pages 4154-4162

Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: The propeptide is a potent inhibitor of the mature domain but is not required for its folding

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CALCIUM; DEGRADATION; ENZYME INHIBITION; ESCHERICHIA COLI;

EID: 33745182284     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02696-05     Document Type: Article
Times cited : (50)

References (68)
  • 1
    • 0028006334 scopus 로고
    • Crystallization and preliminary crystallographic analysis of sfericase. A Bacillus sphaericus calcium-dependent serine proteinase
    • Almog, O., D. Klein, S. Braun, and G. Shoham. 1994. Crystallization and preliminary crystallographic analysis of sfericase. A Bacillus sphaericus calcium-dependent serine proteinase. J. Mol. Biol. 235:760-762.
    • (1994) J. Mol. Biol. , vol.235 , pp. 760-762
    • Almog, O.1    Klein, D.2    Braun, S.3    Shoham, G.4
  • 2
    • 0041384380 scopus 로고    scopus 로고
    • The 0.93Å crystal structure of sphericase: A calcium-loaded serine protease from Bacillus sphaericus
    • Almog, O., A. Gonzalez, D. Klein, H. M. Greenblatt, S. Braun, and G. Shoham. 2003. The 0.93Å crystal structure of sphericase: a calcium-loaded serine protease from Bacillus sphaericus. J. Mol. Biol. 332:1071-1082.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1071-1082
    • Almog, O.1    Gonzalez, A.2    Klein, D.3    Greenblatt, H.M.4    Braun, S.5    Shoham, G.6
  • 4
    • 13444251072 scopus 로고    scopus 로고
    • Crystal structure of a subtilisin-like serine proteinase from a psychotrophic Vibrio species reveals structural aspects of cold adaptation
    • Arnorsdottir, J., M. M. Kristjansson, and R. Ficner. 2005. Crystal structure of a subtilisin-like serine proteinase from a psychotrophic Vibrio species reveals structural aspects of cold adaptation. FEBS J. 272:832-845.
    • (2005) FEBS J. , vol.272 , pp. 832-845
    • Arnorsdottir, J.1    Kristjansson, M.M.2    Ficner, R.3
  • 5
    • 0029910771 scopus 로고    scopus 로고
    • Evidence for propeptide-assisted folding of the calcium-dependent protease of the cyanobacterium Anabaena
    • Baier, K., S. Nicklisch, I. Maldener, and W. Lockau. 1996. Evidence for propeptide-assisted folding of the calcium-dependent protease of the cyanobacterium Anabaena. Eur. J. Biochem. 241:750-755.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 750-755
    • Baier, K.1    Nicklisch, S.2    Maldener, I.3    Lockau, W.4
  • 6
    • 0024959484 scopus 로고
    • Long-range structural changes in proteinase K triggered by calcium ion removal
    • Bajorath, J., S. Raghunathan, W. Hinrichs, and W. Saenger. 1989. Long-range structural changes in proteinase K triggered by calcium ion removal. Nature 337:481-484.
    • (1989) Nature , vol.337 , pp. 481-484
    • Bajorath, J.1    Raghunathan, S.2    Hinrichs, W.3    Saenger, W.4
  • 7
    • 0037668063 scopus 로고    scopus 로고
    • Synthetic peptides derived from the prosegments of proprotein convertase 1/3 and furin are potent inhibitors of both enzymes
    • Basak, A., and C. Lazure. 2003. Synthetic peptides derived from the prosegments of proprotein convertase 1/3 and furin are potent inhibitors of both enzymes. Biochem. J. 373:231-239.
    • (2003) Biochem. J. , vol.373 , pp. 231-239
    • Basak, A.1    Lazure, C.2
  • 8
    • 0024191755 scopus 로고
    • Three-dimensional structure of proteinase K at 0.15-nm resolution
    • Betzel, C., G. P. Pal, and W. Saenger. 1988. Three-dimensional structure of proteinase K at 0.15-nm resolution. Eur. J. Biochem. 178:155-171.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 155-171
    • Betzel, C.1    Pal, G.P.2    Saenger, W.3
  • 9
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry
    • Bode, W., E. Papamokos, and D. Musil. 1987. The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. Eur. J. Biochem. 166: 673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 10
    • 0034731382 scopus 로고    scopus 로고
    • Protein engineering of subtilisin
    • Bryan, P. N. 2000. Protein engineering of subtilisin. Biochim. Biophys. Acta 1543:203-222.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 203-222
    • Bryan, P.N.1
  • 12
    • 0030000685 scopus 로고    scopus 로고
    • Secretion of active subtilisin YaB by a simultaneous expression of separate pre-pro and pre-mature polypeptides in Bacillus subtilis
    • Chang, Y. C., H. Kadokura, K. Yoda, and M. Yamasaki. 1996. Secretion of active subtilisin YaB by a simultaneous expression of separate pre-pro and pre-mature polypeptides in Bacillus subtilis. Biochem. Biophys. Res. Commun. 219:463-468.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 463-468
    • Chang, Y.C.1    Kadokura, H.2    Yoda, K.3    Yamasaki, M.4
  • 13
    • 0033534477 scopus 로고    scopus 로고
    • Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization
    • Choi, I. G., W. G. Bang, S. H. Kim, and Y. G. Yu. 1999. Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization. J. Biol. Chem. 274:881-888.
    • (1999) J. Biol. Chem. , vol.274 , pp. 881-888
    • Choi, I.G.1    Bang, W.G.2    Kim, S.H.3    Yu, Y.G.4
  • 14
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41
    • Davail, S., G. Feller, E. Narinx, and C. Gerday. 1994. Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41. J. Biol. Chem. 269: 17448-17453.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 15
    • 0027464607 scopus 로고
    • Folding of subtilisin BPN′: Characterization of a folding intermediate
    • Eder, J., M. Rheinnecker, and A. R. Fersht. 1993. Folding of subtilisin BPN′: characterization of a folding intermediate. Biochemistry 32:18-26.
    • (1993) Biochemistry , vol.32 , pp. 18-26
    • Eder, J.1    Rheinnecker, M.2    Fersht, A.R.3
  • 16
    • 0032962740 scopus 로고    scopus 로고
    • Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase
    • Exterkate, F. A., and A. C. Alting. 1999. Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase. Appl. Environ. Microbiol. 65:1390-1396.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1390-1396
    • Exterkate, F.A.1    Alting, A.C.2
  • 17
    • 0034596066 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked
    • Fu, X., M. Inouye, and U. Shinde. 2000. Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked. J. Biol. Chem. 275:16871-16878.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16871-16878
    • Fu, X.1    Inouye, M.2    Shinde, U.3
  • 18
    • 0027164337 scopus 로고
    • Calcium-independent subtilisin by design
    • Gallagher, T., P. N. Bryan, and G. L. Gilliland. 1993. Calcium-independent subtilisin by design. Proteins 16:205-213.
    • (1993) Proteins , vol.16 , pp. 205-213
    • Gallagher, T.1    Bryan, P.N.2    Gilliland, G.L.3
  • 19
    • 0029645412 scopus 로고
    • The prosegment-subtilisin BPN′ complex: Crystal structure of a specific 'foldase.'
    • Gallagher, T., G. Gilliland, L. Wang, and P. N. Bryan. 1995. The prosegment-subtilisin BPN′ complex: crystal structure of a specific 'foldase.' Structure 3:907-914.
    • (1995) Structure , vol.3 , pp. 907-914
    • Gallagher, T.1    Gilliland, G.2    Wang, L.3    Bryan, P.N.4
  • 20
    • 84871693371 scopus 로고
    • The spectrophotometric determination of tyrosine and tryptophan in proteins
    • Goodwin, T. W., and R. A. Morton. 1946. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem. J. 40:628-632.
    • (1946) Biochem. J. , vol.40 , pp. 628-632
    • Goodwin, T.W.1    Morton, R.A.2
  • 21
    • 0024817865 scopus 로고
    • Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content
    • Gros, P., C. Betzel, Z. Dauter, K. S. Wilson, and W. G. Hol. 1988. Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content. J. Mol. Biol. 210:347-367.
    • (1988) J. Mol. Biol. , vol.210 , pp. 347-367
    • Gros, P.1    Betzel, C.2    Dauter, Z.3    Wilson, K.S.4    Hol, W.G.5
  • 22
    • 0025828307 scopus 로고
    • Calcium binding to thermitase. Crystallographic studies of thermitase at O, 5, and 100 mM calcium
    • Gros, P., K. H. Kalk, and W. G. Hol. 1991. Calcium binding to thermitase. Crystallographic studies of thermitase at O, 5, and 100 mM calcium. J. Biol. Chem. 266:2953-2961.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2953-2961
    • Gros, P.1    Kalk, K.H.2    Hol, W.G.3
  • 23
    • 0028103878 scopus 로고
    • Renaturation of the mature subtilisin BPN′ immobilized on agarose beads
    • Hayashi, T., M. Matsubara, D. Nohara, S. Kojima, K. Miura, and T. Sakai. 1994. Renaturation of the mature subtilisin BPN′ immobilized on agarose beads. FEBS Lett. 350:109-112.
    • (1994) FEBS Lett. , vol.350 , pp. 109-112
    • Hayashi, T.1    Matsubara, M.2    Nohara, D.3    Kojima, S.4    Miura, K.5    Sakai, T.6
  • 24
    • 0031471409 scopus 로고    scopus 로고
    • Kinetic studies of the inhibitory effects of propeptides subtilisin BPN′ and Carlsberg to bacterial serine proteases
    • Huang, H. W., W. C. Chen, C. Y. Wu, H. C. Yu, W. Y. Lin, S. T. Chen, and K. T. Wang. 1997. Kinetic studies of the inhibitory effects of propeptides subtilisin BPN′ and Carlsberg to bacterial serine proteases. Protein Eng. 10:1227-1233.
    • (1997) Protein Eng. , vol.10 , pp. 1227-1233
    • Huang, H.W.1    Chen, W.C.2    Wu, C.Y.3    Yu, H.C.4    Lin, W.Y.5    Chen, S.T.6    Wang, K.T.7
  • 25
    • 0022429781 scopus 로고
    • Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis
    • Jacobs, M., M. Eliasson, M. Uhlen, and J. I. Flock. 1985. Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis. Nucleic Acids Res. 13:8913-8926.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8913-8926
    • Jacobs, M.1    Eliasson, M.2    Uhlen, M.3    Flock, J.I.4
  • 26
    • 0032553556 scopus 로고    scopus 로고
    • The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 Å resolution
    • Jain, S. C., U. Shinde, Y. Li, M. Inouye, and H. M. Berman. 1998. The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 Å resolution. J. Mol. Biol. 284:137-144.
    • (1998) J. Mol. Biol. , vol.284 , pp. 137-144
    • Jain, S.C.1    Shinde, U.2    Li, Y.3    Inouye, M.4    Berman, H.M.5
  • 27
    • 0037200990 scopus 로고    scopus 로고
    • Two flexible loops in subtilisin-like thermophilic protease, thermicin, from Thermoanaerobacter yonseiensis
    • Jang, H. J., C. H. Lee, W. Lee, and Y. S. Kim. 2002. Two flexible loops in subtilisin-like thermophilic protease, thermicin, from Thermoanaerobacter yonseiensis. J. Biochem. Mol. Biol. 35:498-507.
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 498-507
    • Jang, H.J.1    Lee, C.H.2    Lee, W.3    Kim, Y.S.4
  • 29
    • 0032975313 scopus 로고    scopus 로고
    • Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain ac10: Gene cloning and enzyme purification and characterization
    • Kulakova, L., A. Calkin, T. Kurihara, T. Yoshimura, and N. Esaki. 1999. Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain ac10: gene cloning and enzyme purification and characterization. Appl. Environ. Microbiol. 65:611-617.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 611-617
    • Kulakova, L.1    Calkin, A.2    Kurihara, T.3    Yoshimura, T.4    Esaki, N.5
  • 30
    • 0028067179 scopus 로고
    • Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine
    • Li, Y., and M. Inouye. 1994. Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine. J. Biol. Chem. 269:4169-4174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 31
    • 0028846035 scopus 로고
    • Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants
    • Li, Y., Z. Hu, F. Jordan, and M. Inouye. 1995. Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. J. Biol. Chem. 270:25127-25132.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25127-25132
    • Li, Y.1    Hu, Z.2    Jordan, F.3    Inouye, M.4
  • 32
    • 11844291967 scopus 로고    scopus 로고
    • The propeptide is not required to produce catalytically active neutral protease from Bacillus stearothermophilus
    • Mansfeld, J., E. Petermann, P. Durrschmidt, and R. Ulbrich-Hoftnann. 2005. The propeptide is not required to produce catalytically active neutral protease from Bacillus stearothermophilus. Protein Expr. Purif. 39:219-228.
    • (2005) Protein Expr. Purif. , vol.39 , pp. 219-228
    • Mansfeld, J.1    Petermann, E.2    Durrschmidt, P.3    Ulbrich-Hoftnann, R.4
  • 33
    • 0033524956 scopus 로고    scopus 로고
    • The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli
    • Marie-Claire, C., E. Ruffet, A. Beaumont, and B. P. Roques. 1999. The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli. J. Mol. Biol. 285:1911-1915.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1911-1915
    • Marie-Claire, C.1    Ruffet, E.2    Beaumont, A.3    Roques, B.P.4
  • 34
    • 0035808308 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: The structural and functional characterization of the aqualysin I propeptide
    • Marie-Claire, C., Y. Yabuta, K. Suefuji, H. Matsuzawa, and U. Shinde. 2001. Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide. J. Mol. Biol. 305:151-165.
    • (2001) J. Mol. Biol. , vol.305 , pp. 151-165
    • Marie-Claire, C.1    Yabuta, Y.2    Suefuji, K.3    Matsuzawa, H.4    Shinde, U.5
  • 35
    • 0023958951 scopus 로고
    • Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1
    • Matsuzawa, H., K. Tokugawa, M. Hamaoki, M. Mizoguchi, H. Taguchi, I. Terada, S. T. Kwon, and T. Ohta. 1988. Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1. Eur. J. Biochem. 171:441-447.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 441-447
    • Matsuzawa, H.1    Tokugawa, K.2    Hamaoki, M.3    Mizoguchi, M.4    Taguchi, H.5    Terada, I.6    Kwon, S.T.7    Ohta, T.8
  • 36
    • 0023729499 scopus 로고
    • Structural comparison of two serine proteinase-protein inhibitor complexes: Eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo
    • McPhalen, C. A., and M. N. James. 1988. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. Biochemistry 27:6582-6598.
    • (1988) Biochemistry , vol.27 , pp. 6582-6598
    • McPhalen, C.A.1    James, M.N.2
  • 37
    • 0031415284 scopus 로고    scopus 로고
    • Subtilisin from psychrophilic antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold
    • Narinx, E., E. Baisem, and C. Gerdaym. 1997. Subtilisin from psychrophilic antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng. 10:1271-1279.
    • (1997) Protein Eng. , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baisem, E.2    Gerdaym, C.3
  • 38
    • 0033166285 scopus 로고    scopus 로고
    • Intramolecular chaperone and inhibitor activities of a propeptide from a bacterial zinc aminopeptidase
    • Nirasawa, S., Y. Nakajima, Z. Z. Zhang, M. Yoshida, and K. Hayashi. 1999. Intramolecular chaperone and inhibitor activities of a propeptide from a bacterial zinc aminopeptidase. Biochem. J. 341:25-31.
    • (1999) Biochem. J. , vol.341 , pp. 25-31
    • Nirasawa, S.1    Nakajima, Y.2    Zhang, Z.Z.3    Yoshida, M.4    Hayashi, K.5
  • 39
    • 0029956778 scopus 로고    scopus 로고
    • The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro
    • O'Donohue, M. J., and A. Beaumont. 1996. The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro. J. Biol. Chem. 271: 26477-26481.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26477-26481
    • O'Donohue, M.J.1    Beaumont, A.2
  • 40
    • 0026168310 scopus 로고
    • Pro-peptide as an intramolecular chaperone: Renaturation of denatured subtilisin e with a synthetic pro-peptide
    • Ohta, Y., H. Hojo, S. Aimoto, T. Kobayashi, X. Zhu, F. Jordan, and M. Inouye. 1991. Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide. Mol. Microbiol. 5:1507-1510.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1507-1510
    • Ohta, Y.1    Hojo, H.2    Aimoto, S.3    Kobayashi, T.4    Zhu, X.5    Jordan, F.6    Inouye, M.7
  • 41
    • 0023691688 scopus 로고
    • The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: Subtilisin as a test case
    • Pantoliano, M. W., M. Whitlow, J. F. Wood, M. L. Rollence, B. C. Finzel, G. L. Gilliland, T. L. Poulos, and P. N. Bryan. 1988. The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. Biochemistry 27:8311-8317.
    • (1988) Biochemistry , vol.27 , pp. 8311-8317
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Rollence, M.L.4    Finzel, B.C.5    Gilliland, G.L.6    Poulos, T.L.7    Bryan, P.N.8
  • 42
    • 0024962392 scopus 로고
    • Large increases in general stability for subtilisin BPN′ through incremental changes in the free energy of unfolding
    • Pantoliano, M. W., M. Whitlow, J. F. Wood, S. W. Dodd, K. D. Hardman, M. L. Rollence, and P. N. Bryan. 1989. Large increases in general stability for subtilisin BPN′ through incremental changes in the free energy of unfolding. Biochemistry 28:7205-7213.
    • (1989) Biochemistry , vol.28 , pp. 7205-7213
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Dodd, S.W.4    Hardman, K.D.5    Rollence, M.L.6    Bryan, P.N.7
  • 43
    • 0028949981 scopus 로고
    • Folding mediated by an intramolecular chaperone: Autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism
    • Shinde, U., and M. Inouye. 1995. Folding mediated by an intramolecular chaperone: autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism. J. Mol. Biol. 247:390-395.
    • (1995) J. Mol. Biol. , vol.247 , pp. 390-395
    • Shinde, U.1    Inouye, M.2
  • 44
    • 0029123798 scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Characterization of the structural changes in pro-subtilisin e coincident with autoprocessing
    • Shinde, U., and M. Inouye. 1995. Folding pathway mediated by an intramolecular chaperone: characterization of the structural changes in pro-subtilisin E coincident with autoprocessing. J. Mol. Biol. 252:25-30.
    • (1995) J. Mol. Biol. , vol.252 , pp. 25-30
    • Shinde, U.1    Inouye, M.2
  • 45
    • 0029543755 scopus 로고    scopus 로고
    • Propeptide-mediated folding in subtilisin: The intramolecular chaperone concept
    • Shinde, U., and M. Inouye. 1996. Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept. Adv. Exp. Med. Biol. 379:147-154.
    • (1996) Adv. Exp. Med. Biol. , vol.379 , pp. 147-154
    • Shinde, U.1    Inouye, M.2
  • 46
    • 0030756534 scopus 로고    scopus 로고
    • Protein memory through altered folding mediated by intramolecular chaperones
    • Shinde, U. P., J. J. Liu, and M. Inouye. 1997. Protein memory through altered folding mediated by intramolecular chaperones. Nature 389:520-522.
    • (1997) Nature , vol.389 , pp. 520-522
    • Shinde, U.P.1    Liu, J.J.2    Inouye, M.3
  • 47
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisin-like serine proteases
    • Siezen, R. J., and J. A. Leunissen. 1997. Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6:501-523.
    • (1997) Protein Sci. , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.2
  • 48
    • 0025998717 scopus 로고
    • Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases
    • Siezen, R. J., W. M. de Vos, J. A. Leunissen, and B. W. Dijkstra. 1991. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 4:719-737.
    • (1991) Protein Eng. , vol.4 , pp. 719-737
    • Siezen, R.J.1    De Vos, W.M.2    Leunissen, J.A.3    Dijkstra, B.W.4
  • 49
    • 0024425004 scopus 로고
    • The α-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
    • Silen, J. L., and D. A. Agard. 1989. The α-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature 341:462-464.
    • (1989) Nature , vol.341 , pp. 462-464
    • Silen, J.L.1    Agard, D.A.2
  • 50
    • 0033544694 scopus 로고    scopus 로고
    • Calcium-mediated thermostability in the subtilisin superfamily: The crystal structure of Bacillus Ak. 1 protease at 1.8 Å resolution
    • Smith, C. A., H. S. Toogood, H. M. Baker, R. M. Daniel, and E. N. Baker. 1999. Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak. 1 protease at 1.8 Å resolution. J. Mol. Biol. 294:1027-1040.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1027-1040
    • Smith, C.A.1    Toogood, H.S.2    Baker, H.M.3    Daniel, R.M.4    Baker, E.N.5
  • 51
    • 0024331466 scopus 로고
    • Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli
    • Smith, S. M., and M. M. Gottesman. 1989. Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli. J. Biol. Chem. 264:20487-20495.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20487-20495
    • Smith, S.M.1    Gottesman, M.M.2
  • 52
    • 0021337529 scopus 로고
    • Replacement of the Bacillus subtilis subtilisin structural gene with an in vitro-derived deletion mutation
    • Stahl, M. L., and E. Ferrari. 1984. Replacement of the Bacillus subtilis subtilisin structural gene with an in vitro-derived deletion mutation. J. Bacteriol. 158:411-418.
    • (1984) J. Bacteriol. , vol.158 , pp. 411-418
    • Stahl, M.L.1    Ferrari, E.2
  • 54
    • 0027196077 scopus 로고
    • Crystal structure of selenosubtilisin at 2.0-Å resolution
    • Syed, R., Z. P. Wu, J. M. Hogle, and D. Hilvert. 1993. Crystal structure of selenosubtilisin at 2.0-Å resolution. Biochemistry 32:6157-6164.
    • (1993) Biochemistry , vol.32 , pp. 6157-6164
    • Syed, R.1    Wu, Z.P.2    Hogle, J.M.3    Hilvert, D.4
  • 55
    • 0027502878 scopus 로고
    • Protein engineering on subtilisin
    • Takagi, H. 1993. Protein engineering on subtilisin. Int. J. Biochem. 25:307-312.
    • (1993) Int. J. Biochem. , vol.25 , pp. 307-312
    • Takagi, H.1
  • 56
    • 0024273064 scopus 로고
    • Mutant subtilisin E with enhanced protease activity obtained by site-directed mutagenesis
    • Takagi, H., Y. Morinaga, H. Ikeura, and M. Inouye. 1988. Mutant subtilisin E with enhanced protease activity obtained by site-directed mutagenesis. J. Biol Chem. 263:19592-19596.
    • (1988) J. Biol Chem. , vol.263 , pp. 19592-19596
    • Takagi, H.1    Morinaga, Y.2    Ikeura, H.3    Inouye, M.4
  • 58
    • 0030580110 scopus 로고    scopus 로고
    • Evidence for intramolecular processing of prosubtilisin sequestered on a solid support
    • Volkov, A., and F. Jordan. 1996. Evidence for intramolecular processing of prosubtilisin sequestered on a solid support. J. Mol. Biol. 262:595-599.
    • (1996) J. Mol. Biol. , vol.262 , pp. 595-599
    • Volkov, A.1    Jordan, F.2
  • 59
    • 0017075046 scopus 로고
    • Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability
    • Voordouw, G., C. Milo, and R. S. Roche. 1976. Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability. Biochemistry 15:3716-3724.
    • (1976) Biochemistry , vol.15 , pp. 3716-3724
    • Voordouw, G.1    Milo, C.2    Roche, R.S.3
  • 60
    • 0023783073 scopus 로고
    • Subtilisin-an enzyme designed to be engineered
    • Wells, J. A., and D. A. Estell. 1988. Subtilisin-an enzyme designed to be engineered. Trends Biochem. Sci. 13:291-297.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 291-297
    • Wells, J.A.1    Estell, D.A.2
  • 61
    • 0021112782 scopus 로고
    • Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis
    • Wells, J. A., E. Ferrari, D. J. Henner, D. A. Estell, and E. Y. Chen. 1983. Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis. Nucleic Acids Res. 11:7911-7925.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 7911-7925
    • Wells, J.A.1    Ferrari, E.2    Henner, D.J.3    Estell, D.A.4    Chen, E.Y.5
  • 62
    • 0026004831 scopus 로고
    • Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity
    • Winther, J. R., and P. Sorensen. 1991. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proc. Natl. Acad. Sci. USA 88:9330-9334.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9330-9334
    • Winther, J.R.1    Sorensen, P.2
  • 63
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., O. Kandler, and M. L. Wheelis. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl Acad. Sci. USA 87:4576-4579.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 64
    • 0014682668 scopus 로고
    • Structure of subtilisin BPN′ at 2.5 angstrom resolution
    • Wright, C. S., R. A. Alden, and J. Kraut. 1969. Structure of subtilisin BPN′ at 2.5 angstrom resolution. Nature 221:235-242.
    • (1969) Nature , vol.221 , pp. 235-242
    • Wright, C.S.1    Alden, R.A.2    Kraut, J.3
  • 65
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin
    • Yabuta, Y., H. Takagi, M. Inouye, and U. Shinde. 2001. Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. J. Biol Chem. 276:44427-44434.
    • (2001) J. Biol Chem. , vol.276 , pp. 44427-44434
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3    Shinde, U.4
  • 67
    • 0037674588 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases
    • Yabuta, Y., E. Subbian, C. Oiry, and U. Shinde. 2003. Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases. J. Biol. Chem. 278:15246-15251.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15246-15251
    • Yabuta, Y.1    Subbian, E.2    Oiry, C.3    Shinde, U.4
  • 68
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • Zhu, X. L., Y. Ohta, F. Jordan, and M. Inouye. 1989. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature 339:483-484.
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.L.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4


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