메뉴 건너뛰기




Volumn 125, Issue 6, 1999, Pages 1016-1021

Identification and designing of the S3 site of aqualysin I, a thermophilic subtilisin-related serine protease

Author keywords

Aqualysin I; P3 specificity; S3 subsite; Serine protease; Subtilsin

Indexed keywords

ALANINE; GLYCINE; HYDROLASE; MUTANT PROTEIN; PHENYLALANINE; POLYAMINE; SERINE; SERINE PROTEINASE; SUBTILISIN; SUCCINIC ACID;

EID: 0032809035     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022380     Document Type: Article
Times cited : (3)

References (46)
  • 1
    • 0024384198 scopus 로고
    • Protein engineering of disulfide bonds in subtilisin BPN′
    • Mitchinson, C. and Wells, J.A. (1989) Protein engineering of disulfide bonds in subtilisin BPN′. Biochemistry 28, 4807-4815
    • (1989) Biochemistry , vol.28 , pp. 4807-4815
    • Mitchinson, C.1    Wells, J.A.2
  • 2
    • 0022998684 scopus 로고
    • In vivo formation and stability of engineered disulfide bonds in subtilisin
    • Wells, J.A. and Powers, D.B. (1986) In vivo formation and stability of engineered disulfide bonds in subtilisin. J. Biol. Chem. 261, 6564-6570
    • (1986) J. Biol. Chem. , vol.261 , pp. 6564-6570
    • Wells, J.A.1    Powers, D.B.2
  • 3
    • 0023034995 scopus 로고
    • The crystallographically determined structures of a typical strained disulfides engineered into subtilisin
    • Katz, B.A. and Kassiakoff, A. (1986) The crystallographically determined structures of a typical strained disulfides engineered into subtilisin. J. Biol. Chem. 261, 15480-15485
    • (1986) J. Biol. Chem. , vol.261 , pp. 15480-15485
    • Katz, B.A.1    Kassiakoff, A.2
  • 4
    • 0023661636 scopus 로고
    • Protein engineering of subtilisin BPN′: Enhanced stabilization through the introduction of two cysteins to form a disulfide bond
    • Pantoliano, M.W., Ladner, R.C., Bryan, P.N., Rollence, M.L., Wood, J.F., and Poulos, T.L. (1987) Protein engineering of subtilisin BPN′: enhanced stabilization through the introduction of two cysteins to form a disulfide bond. Biochemistry 26, 2077-2082
    • (1987) Biochemistry , vol.26 , pp. 2077-2082
    • Pantoliano, M.W.1    Ladner, R.C.2    Bryan, P.N.3    Rollence, M.L.4    Wood, J.F.5    Poulos, T.L.6
  • 5
    • 0024564552 scopus 로고
    • Control of enzyme activity by an engineered disulfude bond
    • Matsumura, M. and Matthews, B.W. (1989) Control of enzyme activity by an engineered disulfude bond. Science 243, 792-794
    • (1989) Science , vol.243 , pp. 792-794
    • Matsumura, M.1    Matthews, B.W.2
  • 7
    • 0022445901 scopus 로고
    • Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering
    • Estell, D.A., Graycar, T.P., Miller, J.V., Powers, D.B., Burnier, J.P., Ng, P.G., and Wells, J.A. (1986) Probing steric and hydrophobic effects on enzyme-substrate interactions by protein engineering. Science 233, 659-663
    • (1986) Science , vol.233 , pp. 659-663
    • Estell, D.A.1    Graycar, T.P.2    Miller, J.V.3    Powers, D.B.4    Burnier, J.P.5    Ng, P.G.6    Wells, J.A.7
  • 8
  • 9
    • 0023384982 scopus 로고
    • Engineered enzyme specificity by "substrate-assisted catalysis."
    • Carter, P. and Wells, J.A. (1987) Engineered enzyme specificity by "substrate-assisted catalysis." Science 237, 394-399
    • (1987) Science , vol.237 , pp. 394-399
    • Carter, P.1    Wells, J.A.2
  • 10
    • 0023646665 scopus 로고
    • Rational modification of enzyme catalysis by engineering surface charge
    • Russell, A.J. and Fersht, A.R. (1987) Rational modification of enzyme catalysis by engineering surface charge. Nature 328, 496-500
    • (1987) Nature , vol.328 , pp. 496-500
    • Russell, A.J.1    Fersht, A.R.2
  • 11
    • 0024273064 scopus 로고
    • Mutant subtilisin E with enhanced protease activity obtained by site-directed mutagensis
    • Takagi, H., Morinaga, Y., Ikemura, H., and Inouye, M. (1988) Mutant subtilisin E with enhanced protease activity obtained by site-directed mutagensis. J. Biol. Chem. 263, 19592-19596
    • (1988) J. Biol. Chem. , vol.263 , pp. 19592-19596
    • Takagi, H.1    Morinaga, Y.2    Ikemura, H.3    Inouye, M.4
  • 12
    • 0027479593 scopus 로고
    • Engineering a novel specificity in subtilisin BPN′
    • Rheinnecker, M., Baker, G., Eder, J., and Fersht, A.R. (1993) Engineering a novel specificity in subtilisin BPN′. Biochemistry 32, 1199-1203
    • (1993) Biochemistry , vol.32 , pp. 1199-1203
    • Rheinnecker, M.1    Baker, G.2    Eder, J.3    Fersht, A.R.4
  • 13
    • 0028874551 scopus 로고
    • Designing subtilisin BPN′ to cleave substrates containing dibasic residues
    • Ballinger, M.D., Tom, J., and Wells, J.A. (1995) Designing subtilisin BPN′ to cleave substrates containing dibasic residues. Biochemistry 34, 13312-13319
    • (1995) Biochemistry , vol.34 , pp. 13312-13319
    • Ballinger, M.D.1    Tom, J.2    Wells, J.A.3
  • 14
    • 0014409072 scopus 로고
    • Subtilisin Carlsberg. V. The complete sequence; comaprison with subtilisin BPN′; evolutionary relationships
    • Smith, E.L., Delange, R.J., Evans, W.H., Landon, M., and Markland, F.S. (1968) Subtilisin Carlsberg. V. The complete sequence; comaprison with subtilisin BPN′; evolutionary relationships. J. Biol. Chem. 243, 2184-2191
    • (1968) J. Biol. Chem. , vol.243 , pp. 2184-2191
    • Smith, E.L.1    Delange, R.J.2    Evans, W.H.3    Landon, M.4    Markland, F.S.5
  • 15
    • 0024191755 scopus 로고
    • Three-dimensional structure of proteinase K at 0.15-nm resolution
    • Betzel, C., Pal, G.P., and Saenger, W. (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
  • 16
    • 0022553273 scopus 로고
    • Active-site geometry of proteinase K. Crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor
    • Betzel, C., Pal, G.P., Struck, M., Jany, K.-D., and Saenger, W. (1986) Active-site geometry of proteinase K. Crystallographic study of its complex with a dipeptide chloromethyl ketone inhibitor. FEBS Lett. 197, 105-110
    • (1986) FEBS Lett. , vol.197 , pp. 105-110
    • Betzel, C.1    Pal, G.P.2    Struck, M.3    Jany, K.-D.4    Saenger, W.5
  • 17
    • 0015505885 scopus 로고
    • Comparison of the active site stereochemistry and substrate conformation in α-chymotrypsin and subtilisin BPN′
    • Wright, C.S. (1972) Comparison of the active site stereochemistry and substrate conformation in α-chymotrypsin and subtilisin BPN′. J. Mol. Biol. 67, 151-163
    • (1972) J. Mol. Biol. , vol.67 , pp. 151-163
    • Wright, C.S.1
  • 18
    • 0015505837 scopus 로고
    • Crystal structure of a subtilisin BPN′ complex with N-benzyl-L-arginine
    • Wright, C.S., Alden, E.A., and Kraut, J. (1972) Crystal structure of a subtilisin BPN′ complex with N-benzyl-L-arginine. J. Mol. Biol. 66, 283-289
    • (1972) J. Mol. Biol. , vol.66 , pp. 283-289
    • Wright, C.S.1    Alden, E.A.2    Kraut, J.3
  • 19
    • 0015517292 scopus 로고
    • An X-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN′
    • Robertus, J.D., Alden, R.A., Birktoft, J.J., Kraut, J., Powers, J.C., and Wilcox, P.E. (1972) An X-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN′. Biochemistry 11, 2439-2449
    • (1972) Biochemistry , vol.11 , pp. 2439-2449
    • Robertus, J.D.1    Alden, R.A.2    Birktoft, J.J.3    Kraut, J.4    Powers, J.C.5    Wilcox, P.E.6
  • 20
    • 0017253438 scopus 로고
    • Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin
    • Poulos, T.L., Alden, R.A., Freer, S.T., Birktoft, J.J., and Kraut, J. (1976) Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin. J. Biol. Chem. 261, 1097-1103
    • (1976) J. Biol. Chem. , vol.261 , pp. 1097-1103
    • Poulos, T.L.1    Alden, R.A.2    Freer, S.T.3    Birktoft, J.J.4    Kraut, J.5
  • 21
    • 0022701771 scopus 로고
    • Refined 1.2 Å crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin c and its detailed interaction with subtilisin
    • Bode, W., Papamokos, E., Musil, D., Seemueller, U., and Fritz, H. (1986) Refined 1.2 Å crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin c and its detailed interaction with subtilisin. EMBO J. 5, 813-818
    • (1986) EMBO J. , vol.5 , pp. 813-818
    • Bode, W.1    Papamokos, E.2    Musil, D.3    Seemueller, U.4    Fritz, H.5
  • 22
    • 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
    • Bode, W., Papamokos, E., and Musil, D. (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. Eur. J. Biochem. 166, 673-692
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 23
    • 0015525674 scopus 로고
    • Subtilisin Novo. The three-dimensional structure and its comparison with subtilisin BPN′
    • Drenth, J., Hol, W.G.J., Jansonius, J.N., and Koekoek, R. (1972) Subtilisin Novo. The three-dimensional structure and its comparison with subtilisin BPN′. Eur. J. Biochem. 26, 177-181
    • (1972) Eur. J. Biochem. , vol.26 , pp. 177-181
    • Drenth, J.1    Hol, W.G.J.2    Jansonius, J.N.3    Koekoek, R.4
  • 25
    • 0026029144 scopus 로고
    • Refined crystal structures of subtilisin Novo in complex with wild-type and two mutant eglins
    • Heinz, D.W., Priestle, J.P., Rahuel, J., Wilson, K.S., and Grütter, M.G. (1991) Refined crystal structures of subtilisin Novo in complex with wild-type and two mutant eglins. J. Mol. Biol. 217, 353-371
    • (1991) J. Mol. Biol. , vol.217 , pp. 353-371
    • Heinz, D.W.1    Priestle, J.P.2    Rahuel, J.3    Wilson, K.S.4    Grütter, M.G.5
  • 26
    • 0023729499 scopus 로고
    • Structural comparison of two serine proteinase-protein inhibitor complexes: Eglin c-aubtilisin Carlsberg and CI-2-subtilisin Novo
    • McPhalen, C.A. and James, M.N. (1988) Structural comparison of two serine proteinase-protein inhibitor complexes: eglin c-aubtilisin 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
  • 27
    • 0025882132 scopus 로고
    • Neutron structure of subtilisin BPN′: Effects of chemical environment on hydrogen-bonding geometries and the pattern of hydrogen-deuterilum exchange in secondary structure elements
    • Kossiakoff, A.A., White, M.U., and Eigenbrot, C. (1991) Neutron structure of subtilisin BPN′: effects of chemical environment on hydrogen-bonding geometries and the pattern of hydrogen-deuterilum exchange in secondary structure elements. Biochemistry 30, 1211-1221
    • (1991) Biochemistry , vol.30 , pp. 1211-1221
    • Kossiakoff, A.A.1    White, M.U.2    Eigenbrot, C.3
  • 28
    • 0025828307 scopus 로고
    • Calcium binding to thermitase
    • Gros, P., Kalk, K.H., and Hol, W.G.J. (1991) Calcium binding to thermitase. 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.J.3
  • 29
    • 0025998717 scopus 로고
    • Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases
    • Siezen, R.J., Vos, W.M., Leunissen, J.A.M., and Dijkstra, B.W. (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    Vos, W.M.2    Leunissen, J.A.M.3    Dijkstra, B.W.4
  • 30
    • 0002639249 scopus 로고
    • Production of thermophilic extracellular proteases (aqualysin I and II) by Thermus aquaticus YT-1, an extreme thermophile
    • Matsuzawa, H., Hamaoki, M., and Ohta, T. (1983) Production of thermophilic extracellular proteases (aqualysin I and II) by Thermus aquaticus YT-1, an extreme thermophile. Agric. Biol. Chem. 47, 25-28
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 25-28
    • Matsuzawa, H.1    Hamaoki, M.2    Ohta, T.3
  • 31
    • 0023958951 scopus 로고
    • Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1
    • Matsuzawa, H., Tokugawa, K., Hamaoki, M., Mizoguchi, M., Taguchi, H., Terada, I., Kwon, S.-T., and Ohta, T. (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
  • 32
    • 0024276069 scopus 로고
    • Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteritics of the deduced primary structure of the enzyme
    • Kwon, S.-T., Terada, I., Matsuzawa, H., and Ohta, T. (1988) Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteritics of the deduced primary structure of the enzyme. Eur. J. Biochem. 173, 491-497
    • (1988) Eur. J. Biochem. , vol.173 , pp. 491-497
    • Kwon, S.-T.1    Terada, I.2    Matsuzawa, H.3    Ohta, T.4
  • 33
    • 0024099136 scopus 로고
    • Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1
    • Kwon, S.-T., Matsuzawa, H., and Ohta, T. (1988) Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1. J. Biochem. 104, 557-559
    • (1988) J. Biochem. , vol.104 , pp. 557-559
    • Kwon, S.-T.1    Matsuzawa, H.2    Ohta, T.3
  • 35
    • 0026265551 scopus 로고
    • 2-terminal pro-sequence in the position of active aqualysin I (a thermophilic serine protease) in Escherichia coli
    • 2-terminal pro-sequence in the position of active aqualysin I (a thermophilic serine protease) in Escherichia coli. Agric. Biol. Chem. 55, 3027-3032
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 3027-3032
    • Lee, Y.-C.1    Miyata, Y.2    Terada, I.3    Ohta, T.4    Matsuzawa, H.5
  • 36
    • 0026846393 scopus 로고
    • 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli
    • 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli. FEMS Microbiol. Lett. 92, 73-78
    • (1992) FEMS Microbiol. Lett. , vol.92 , pp. 73-78
    • Lee, Y.-C.1    Ohta, T.2    Matsuzawa, H.3
  • 37
    • 85009597173 scopus 로고    scopus 로고
    • Stability of thermostable enzyme, aqualysin I; a subtilisin-type serine protease from Thermus aquaticus YT-1
    • Tanaka, T., Matsuzawa, H., and Ohta, T. (1998) Stability of thermostable enzyme, aqualysin I; a subtilisin-type serine protease from Thermus aquaticus YT-1. Biosci. Biotechnol. Biochem. 62, 1806-1808
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1806-1808
    • Tanaka, T.1    Matsuzawa, H.2    Ohta, T.3
  • 38
    • 0032174682 scopus 로고    scopus 로고
    • P1-specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor
    • Tanaka, T., Matsuzawa, H., Kojima, S., Kumagai, I., Miura, K., and Ohta, T. (1998) P1-specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor. Biosci. Biotechnol. Biochem. 62, 2035-2038
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 2035-2038
    • Tanaka, T.1    Matsuzawa, H.2    Kojima, S.3    Kumagai, I.4    Miura, K.5    Ohta, T.6
  • 39
    • 0000285358 scopus 로고    scopus 로고
    • Substrate specificity of aqualysin I, a bacterial thermophilic alkaline serine protease from Thermus aquaticus YT-1: Comparison with proteinase K, subtilisin BPN′ and subtilisin Carlsberg
    • Tanaka, T., Matsuzawa, H., and Ohta, T. (1998) Substrate specificity of aqualysin I, a bacterial thermophilic alkaline serine protease from Thermus aquaticus YT-1: comparison with proteinase K, subtilisin BPN′ and subtilisin Carlsberg. Biosci. Biotechnol. Biochem. 62, 2161-2165
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 2161-2165
    • Tanaka, T.1    Matsuzawa, H.2    Ohta, T.3
  • 40
    • 0043286619 scopus 로고    scopus 로고
    • Substrate specificity of aqualysin I altered by an organic solvent, DMSO
    • Tanaka, T., Matsuzawa, H., and Ohta, T. (1999) Substrate specificity of aqualysin I altered by an organic solvent, DMSO. Biosci. Biotechnol. Biochem. 63, 446-448
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 446-448
    • Tanaka, T.1    Matsuzawa, H.2    Ohta, T.3
  • 41
    • 0032535232 scopus 로고    scopus 로고
    • Engineering of S2 site of aqualysin I; alteration of P2-specificity by excluding P2 side chain
    • Tanaka, T., Matsuzawa, H., and Ohta, T. (1998) Engineering of S2 site of aqualysin I; alteration of P2-specificity by excluding P2 side chain. Biochemistry 37, 17402-17407
    • (1998) Biochemistry , vol.37 , pp. 17402-17407
    • Tanaka, T.1    Matsuzawa, H.2    Ohta, T.3
  • 42
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotype selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotype selection. Methods Enzymol. 154, 367-382
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 43
    • 0014802965 scopus 로고
    • Subtilisin BPN′: Inactivation by chloromethyl ketone derivatives of peptide substrate
    • Morihara, K. and Oka, T. (1970) Subtilisin BPN′: Inactivation by chloromethyl ketone derivatives of peptide substrate. Arch. Biochem. Biophys. 138, 526-531
    • (1970) Arch. Biochem. Biophys. , vol.138 , pp. 526-531
    • Morihara, K.1    Oka, T.2
  • 44
    • 0015848152 scopus 로고
    • Effect of secondary interaction on the enzymatic activity of subtilisin BPN7prime;: Comparison with α-chymotrypsin, trypsin, and elastase
    • Morihara, K. and Oka, T. (1973) Effect of secondary interaction on the enzymatic activity of subtilisin BPN7prime;: Comparison with α-chymotrypsin, trypsin, and elastase. FEBS Lett. 33, 54-56
    • (1973) FEBS Lett. , vol.33 , pp. 54-56
    • Morihara, K.1    Oka, T.2
  • 45
    • 0016333650 scopus 로고
    • Comparative study of various serine alkaline proteinases from microorganisms
    • Morihara, K., Oka, T., and Tsuzuki, H. (1974) Comparative study of various serine alkaline proteinases from microorganisms. Arch. Biochem. Biophys. 165, 72-79
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 72-79
    • Morihara, K.1    Oka, T.2    Tsuzuki, H.3
  • 46
    • 0345177872 scopus 로고
    • Specificity of proteinase K from Tritirachium album limber for synthetic peptides
    • Morihara, K. and Tsuzuki, H. (1975) Specificity of proteinase K from Tritirachium album Limber for synthetic peptides. Agric. Biol. Chem. 39, 1489-1492
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 1489-1492
    • Morihara, K.1    Tsuzuki, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.