메뉴 건너뛰기




Volumn 19, Issue 4, 2007, Pages 139-150

Molecular recognition of Thermolysin and homologous zinc-metalloproteinases

Author keywords

Aspartame; Bacillus thermoproteolyticus; Thermolysin; Vibriolysin protein

Indexed keywords

ANTIHYPERTENSIVE AGENT; DIPEPTIDYL CARBOXYPEPTIDASE; ENZYME INHIBITOR; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; PEPTIDE; THERMOLYSIN; THERMOLYSIN INHIBITOR; ZINC METALLOPROTEINASE;

EID: 45149133111     PISSN: 11204826     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (3)

References (75)
  • 1
    • 0030864046 scopus 로고    scopus 로고
    • Blunting nature's Swiss army knife
    • Seife C. Blunting nature's Swiss army knife. Science 1997;277:1602-3.
    • (1997) Science , vol.277 , pp. 1602-1603
    • Seife, C.1
  • 2
    • 0001094555 scopus 로고
    • Studies on protease produced by thermophilic bacteria
    • Endo S. Studies on protease produced by thermophilic bacteria. J Ferment Technol 1962;40:346-53.
    • (1962) J Ferment Technol , vol.40 , pp. 346-353
    • Endo, S.1
  • 3
    • 77956941440 scopus 로고    scopus 로고
    • Matsubara H, Feder J. Other bacterial, mold, and yeast protease. 3rd ed. 3. In: Boyer PD, editor. The Enzymes New York, USA: Academic Press; 1971. p. 721-95.
    • Matsubara H, Feder J. Other bacterial, mold, and yeast protease. 3rd ed. Vol. 3. In: Boyer PD, editor. The Enzymes New York, USA: Academic Press; 1971. p. 721-95.
  • 4
    • 0024595625 scopus 로고
    • Computer Automated Structure Evaluatino (CASE): A Study of Inhibitor of the Thermolysin Enzyme
    • Klopman G, Bendale RD. Computer Automated Structure Evaluatino (CASE): A Study of Inhibitor of the Thermolysin Enzyme. J Theor Biol 1989;136:67-77.
    • (1989) J Theor Biol , vol.136 , pp. 67-77
    • Klopman, G.1    Bendale, R.D.2
  • 5
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings ND, Barrett AJ. Evolutionary families of metallopeptidases. Methods Enzymol 1995;248:183-228.
    • (1995) Methods Enzymol , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 6
    • 34548580171 scopus 로고    scopus 로고
    • Engineering, expression, purification, and production of recombinant thermolysin
    • Inouye K, Kusano M, Hashida Y, Minoda M, Yasukawa K. Engineering, expression, purification, and production of recombinant thermolysin. Biotechnol Annu Rev 2007;13:43-64.
    • (2007) Biotechnol Annu Rev , vol.13 , pp. 43-64
    • Inouye, K.1    Kusano, M.2    Hashida, Y.3    Minoda, M.4    Yasukawa, K.5
  • 7
    • 34748868292 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis of the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity
    • Tatsumi C, Hashida Y, Yasukawa K, Inouye K. Effects of site-directed mutagenesis of the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity. J Biochem 2007;141:835-42.
    • (2007) J Biochem , vol.141 , pp. 835-842
    • Tatsumi, C.1    Hashida, Y.2    Yasukawa, K.3    Inouye, K.4
  • 9
    • 45149125739 scopus 로고    scopus 로고
    • CLC BIO. (www.clcbio.com).
  • 10
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • Jongeneel CV, Bouvier J, Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett 1989;242:211-4.
    • (1989) FEBS Lett , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 11
    • 0029896448 scopus 로고    scopus 로고
    • Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism
    • Mock WL, Stanford DJ. Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism. Biochemistry 1996;35:7369-77.
    • (1996) Biochemistry , vol.35 , pp. 7369-7377
    • Mock, W.L.1    Stanford, D.J.2
  • 12
    • 0018232814 scopus 로고
    • Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases
    • Argos P, Garavito RM, Eventoff W, Rossmann MG, Branden CI. Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases. J Mol Biol 1978;126:141-58.
    • (1978) J Mol Biol , vol.126 , pp. 141-158
    • Argos, P.1    Garavito, R.M.2    Eventoff, W.3    Rossmann, M.G.4    Branden, C.I.5
  • 13
    • 34748871409 scopus 로고    scopus 로고
    • Improving the activity and stability of thermolysin by site-directed mutagenesis
    • Yasukawa K, Inouye K. Improving the activity and stability of thermolysin by site-directed mutagenesis. Biochim Biophys Acta 2007;1774:1281-8.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1281-1288
    • Yasukawa, K.1    Inouye, K.2
  • 14
    • 33746883914 scopus 로고    scopus 로고
    • Engineering of the pH-dependence of thermolysin activity as examined by site-directed mutagenesis of Asn112 located at the active site of thermolysin
    • Kusano M, Yasukawa K, Hashida Y, Inouye K. Engineering of the pH-dependence of thermolysin activity as examined by site-directed mutagenesis of Asn112 located at the active site of thermolysin. J Biochem 2006;139:1017-23.
    • (2006) J Biochem , vol.139 , pp. 1017-1023
    • Kusano, M.1    Yasukawa, K.2    Hashida, Y.3    Inouye, K.4
  • 15
    • 17644368559 scopus 로고    scopus 로고
    • Mutational effect for stability in a conserved region of thermolysin
    • Matsumiya Y, Nishikawa K, Inouye K, Kubo M. Mutational effect for stability in a conserved region of thermolysin. Lett Appl Microbiol 2005;40:329-34.
    • (2005) Lett Appl Microbiol , vol.40 , pp. 329-334
    • Matsumiya, Y.1    Nishikawa, K.2    Inouye, K.3    Kubo, M.4
  • 16
    • 0008306775 scopus 로고
    • Enzyme kinetics in drug design: Implications of multiple forms of enzyme on substrate and inhibitor structure-activity correlations
    • Perun TJ, Propst CL, editors, New York: Marcel Dekker;
    • Rich DH, Northrop DB. Enzyme kinetics in drug design: Implications of multiple forms of enzyme on substrate and inhibitor structure-activity correlations. In: Perun TJ, Propst CL, editors. Computer-aided Drug Design. New York: Marcel Dekker; 1989. p. 185-250.
    • (1989) Computer-aided Drug Design , pp. 185-250
    • Rich, D.H.1    Northrop, D.B.2
  • 17
    • 0042683908 scopus 로고
    • Computer-aided design and evaluation of angiotensin converting enzyme inhibitor
    • Perun TJ, Propst CL, editors, New York: Marcel Dekker;
    • Hangauer DG. Computer-aided design and evaluation of angiotensin converting enzyme inhibitor. In: Perun TJ, Propst CL, editors. Computer-aided Drug Design. New York: Marcel Dekker; 1989. p. 253-326.
    • (1989) Computer-aided Drug Design , pp. 253-326
    • Hangauer, D.G.1
  • 18
    • 0025102454 scopus 로고
    • Design of inhibitors of articular cartilage destruction
    • Henderson B, Docherty AJP, Beeley NRA. Design of inhibitors of articular cartilage destruction. Drug Future 1990;15:495-507.
    • (1990) Drug Future , vol.15 , pp. 495-507
    • Henderson, B.1    Docherty, A.J.P.2    Beeley, N.R.A.3
  • 19
    • 0030803237 scopus 로고    scopus 로고
    • A theoretical investigation of tight-binding thermolysin inhibitors
    • Shen J. A theoretical investigation of tight-binding thermolysin inhibitors. J Med Chem 1997;40:2953-8.
    • (1997) J Med Chem , vol.40 , pp. 2953-2958
    • Shen, J.1
  • 20
    • 29244438204 scopus 로고    scopus 로고
    • Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin
    • Juers DH, Kim J, Matthews BW, Sieburth SM. Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin. Biochemistry 2005;44:16524-8.
    • (2005) Biochemistry , vol.44 , pp. 16524-16528
    • Juers, D.H.1    Kim, J.2    Matthews, B.W.3    Sieburth, S.M.4
  • 22
    • 0028905124 scopus 로고
    • Binding of phosphorus-containing inhibitors to thermolysin studied by the Poisson-Boltzmann method
    • Shen J, Wendoloski J. Binding of phosphorus-containing inhibitors to thermolysin studied by the Poisson-Boltzmann method. Protein Sci 1995;4:373-81.
    • (1995) Protein Sci , vol.4 , pp. 373-381
    • Shen, J.1    Wendoloski, J.2
  • 23
    • 0026770573 scopus 로고
    • Crystallographic analysis of transition-state mimics bound to penicillopepsin: Phosphorus-containing peptide analogues
    • Fraser ME, Strynadka NC, Bartlett PA, Hanson JE, James MN. Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues. Biochemistry 1992;31:5201-14.
    • (1992) Biochemistry , vol.31 , pp. 5201-5214
    • Fraser, M.E.1    Strynadka, N.C.2    Bartlett, P.A.3    Hanson, J.E.4    James, M.N.5
  • 24
    • 0027030121 scopus 로고
    • Inhibition of human skin fibroblast collagenase by phosphorus-containing peptides
    • Galardy RE, Grobelny D, Kortylewicz ZP, Poncz L. Inhibition of human skin fibroblast collagenase by phosphorus-containing peptides. Matrix Suppl 1992;1:259-62.
    • (1992) Matrix Suppl , vol.1 , pp. 259-262
    • Galardy, R.E.1    Grobelny, D.2    Kortylewicz, Z.P.3    Poncz, L.4
  • 25
    • 0025102395 scopus 로고
    • Inhibition of thermolysin by phosphonamidate transition-state analogues: Measurement of 31P-15N bond lengths and chemical shifts in two enzyme-inhibitor complexes by solid-state nuclear magnetic resonance
    • Copie V, Kolbert AC, Drewry DH, Bartlett PA, Oas TG, Griffin RG. Inhibition of thermolysin by phosphonamidate transition-state analogues: measurement of 31P-15N bond lengths and chemical shifts in two enzyme-inhibitor complexes by solid-state nuclear magnetic resonance. Biochemistry 1990;29:9176-84.
    • (1990) Biochemistry , vol.29 , pp. 9176-9184
    • Copie, V.1    Kolbert, A.C.2    Drewry, D.H.3    Bartlett, P.A.4    Oas, T.G.5    Griffin, R.G.6
  • 26
    • 0024413687 scopus 로고
    • Binding energetics of phosphorus-containing inhibitors of thermolysin
    • Grobelny D, Goli UB, Galardy RE. Binding energetics of phosphorus-containing inhibitors of thermolysin. Biochemistry 1989;28:4948-51.
    • (1989) Biochemistry , vol.28 , pp. 4948-4951
    • Grobelny, D.1    Goli, U.B.2    Galardy, R.E.3
  • 27
    • 0023786536 scopus 로고
    • Thermolysin-inhibitor complexes examined by 31P and 113Cd NMR spectroscopy
    • Gettins P. Thermolysin-inhibitor complexes examined by 31P and 113Cd NMR spectroscopy. J Biol Chem 1988;263:10208-11.
    • (1988) J Biol Chem , vol.263 , pp. 10208-10211
    • Gettins, P.1
  • 28
    • 0023667707 scopus 로고
    • Possible role for water dissociation in the slow binding of phosphorus-containing transition-state-analogue inhibitors of thermolysin
    • Bartlett PA, Marlowe CK. Possible role for water dissociation in the slow binding of phosphorus-containing transition-state-analogue inhibitors of thermolysin. Biochemistry 1987;26:8553-61.
    • (1987) Biochemistry , vol.26 , pp. 8553-8561
    • Bartlett, P.A.1    Marlowe, C.K.2
  • 29
    • 0023667724 scopus 로고
    • Slow- and fast-binding inhibitors of thermolysin display different modes of binding: Crystallographic analysis of extended phosphonamidate transition-state analogues
    • Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW. Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues. Biochemistry 1987;26:8542-53.
    • (1987) Biochemistry , vol.26 , pp. 8542-8553
    • Holden, H.M.1    Tronrud, D.E.2    Monzingo, A.F.3    Weaver, L.H.4    Matthews, B.W.5
  • 30
    • 0023105721 scopus 로고
    • Evaluation of intrinsic binding energy from a hydrogen bonding group in an enzyme inhibitor
    • Bartlett PA, Marlowe CK. Evaluation of intrinsic binding energy from a hydrogen bonding group in an enzyme inhibitor. Science 1987;235:569-71.
    • (1987) Science , vol.235 , pp. 569-571
    • Bartlett, P.A.1    Marlowe, C.K.2
  • 31
    • 0023040231 scopus 로고
    • Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin
    • Tronrud DE, Monzingo AF, Matthews BW. Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin. Eur J Biochem 1986;157:261-8.
    • (1986) Eur J Biochem , vol.157 , pp. 261-268
    • Tronrud, D.E.1    Monzingo, A.F.2    Matthews, B.W.3
  • 32
    • 0021683965 scopus 로고
    • Differential effects of proteolysis and protein modification on the activities of 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase
    • El-Maghrabi MR, Pate TM, Murray KJ, Pilkis SJ. Differential effects of proteolysis and protein modification on the activities of 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase. J Biol Chem 1984;259:13096-103.
    • (1984) J Biol Chem , vol.259 , pp. 13096-13103
    • El-Maghrabi, M.R.1    Pate, T.M.2    Murray, K.J.3    Pilkis, S.J.4
  • 33
    • 0021113924 scopus 로고
    • Phosphonamidates as transition-state analogue inhibitors of thermolysin
    • Bartlett PA, Marlowe CK. Phosphonamidates as transition-state analogue inhibitors of thermolysin. Biochemistry 1983;22:4618-24.
    • (1983) Biochemistry , vol.22 , pp. 4618-4624
    • Bartlett, P.A.1    Marlowe, C.K.2
  • 34
    • 0016279108 scopus 로고
    • The accessibility of bovine rhodopsin in photoreceptor membranes
    • Saari JC. The accessibility of bovine rhodopsin in photoreceptor membranes. J Cell Biol 1974;63:(2 Pt 1)480-91.
    • (1974) J Cell Biol , vol.63 , Issue.2 PART 1 , pp. 480-491
    • Saari, J.C.1
  • 35
    • 0016165471 scopus 로고
    • The amino acid sequences of the phosphorylated sites in troponin-I from rabbit skeletal muscle
    • Huang TS, Bylund DB, Stull JT, Krebs EG. The amino acid sequences of the phosphorylated sites in troponin-I from rabbit skeletal muscle. FEBS Lett 1974;42:249-52.
    • (1974) FEBS Lett , vol.42 , pp. 249-252
    • Huang, T.S.1    Bylund, D.B.2    Stull, J.T.3    Krebs, E.G.4
  • 36
    • 0015984215 scopus 로고
    • Properties of rat brain tubulin
    • Eipper BA. Properties of rat brain tubulin. J Biol Chem 1974;249:1407-16.
    • (1974) J Biol Chem , vol.249 , pp. 1407-1416
    • Eipper, B.A.1
  • 37
    • 0015493788 scopus 로고
    • Structural studies of calf thymus F3 histone. II. Occurrence of phosphoserine and -N-acetyllysine in thermolysin peptides
    • Marzluff WF Jr, McCarty KS. Structural studies of calf thymus F3 histone. II. Occurrence of phosphoserine and -N-acetyllysine in thermolysin peptides. Biochemistry 1972;11:2677-81.
    • (1972) Biochemistry , vol.11 , pp. 2677-2681
    • Marzluff Jr, W.F.1    McCarty, K.S.2
  • 38
    • 0014876701 scopus 로고
    • Modification of histories during spermiogenesis in trout: A molecular mechanism for altering histone binding to DNA
    • Sung MT, Dixon GH. Modification of histories during spermiogenesis in trout: a molecular mechanism for altering histone binding to DNA. Proc Natl Acad Sci U S A 1970;67:1616-23.
    • (1970) Proc Natl Acad Sci U S A , vol.67 , pp. 1616-1623
    • Sung, M.T.1    Dixon, G.H.2
  • 39
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews BW. Structural basis of the action of thermolysin and related zinc peptidases. Acc Chem Res 1988;21:333-40.
    • (1988) Acc Chem Res , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 40
    • 0023106632 scopus 로고
    • Calculation of the relative change in binding free energy of a protein-inhibitor complex
    • Bash PA, Singh UC, Brown FK, Langridge R, Kollman PA. Calculation of the relative change in binding free energy of a protein-inhibitor complex. Science 1987;235:574-6.
    • (1987) Science , vol.235 , pp. 574-576
    • Bash, P.A.1    Singh, U.C.2    Brown, F.K.3    Langridge, R.4    Kollman, P.A.5
  • 42
    • 0024365686 scopus 로고
    • Free energy perturbation simulations of the inhibition of thermolysin: Prediction of the free energy of binding of a new inhibitors
    • Merz KM, Kollman PA. Free energy perturbation simulations of the inhibition of thermolysin: Prediction of the free energy of binding of a new inhibitors. J Am Chem Soc 1989;111:5649-58.
    • (1989) J Am Chem Soc , vol.111 , pp. 5649-5658
    • Merz, K.M.1    Kollman, P.A.2
  • 44
    • 0028905124 scopus 로고
    • Binding of phosphoruscontaining inhibitors to thermolysin studied by the Poisson-Boltzmann Method
    • Shen J, Wendoloski JJ. Binding of phosphoruscontaining inhibitors to thermolysin studied by the Poisson-Boltzmann Method. Protein Sci 1995;4:373-81.
    • (1995) Protein Sci , vol.4 , pp. 373-381
    • Shen, J.1    Wendoloski, J.J.2
  • 45
    • 0029995624 scopus 로고    scopus 로고
    • Validate: A new method for the receptorbased prediction of binding affinities of novel ligands
    • Head RD, Smythe ML, Oprea TI, Waller CL, Green SM, Marshall GR, Validate: A new method for the receptorbased prediction of binding affinities of novel ligands. J Am Chem Soc 1996;118:3959-69.
    • (1996) J Am Chem Soc , vol.118 , pp. 3959-3969
    • Head, R.D.1    Smythe, M.L.2    Oprea, T.I.3    Waller, C.L.4    Green, S.M.5    Marshall, G.R.6
  • 46
    • 0029979312 scopus 로고    scopus 로고
    • Fitting an inhibitor into the active site of thermolysin: A molecular dynamics case study
    • Wasserman ZR, Hodge CN. Fitting an inhibitor into the active site of thermolysin: A molecular dynamics case study. Protein Eng 1996;24:227-37.
    • (1996) Protein Eng , vol.24 , pp. 227-237
    • Wasserman, Z.R.1    Hodge, C.N.2
  • 47
    • 0026799337 scopus 로고
    • Effects of salts on thermolysin: Activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylaladne methyl ester, and a unique change in the absorption spectrum of thermolysin
    • Inouye K. Effects of salts on thermolysin: activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylaladne methyl ester, and a unique change in the absorption spectrum of thermolysin. J Biochem 1992;112:335-40.
    • (1992) J Biochem , vol.112 , pp. 335-340
    • Inouye, K.1
  • 48
    • 0032517347 scopus 로고    scopus 로고
    • Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity
    • Inouye K, Kuzuya K, Tonomura B. Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity. Biochim Biophys Acta 1998;1388:209-14.
    • (1998) Biochim Biophys Acta , vol.1388 , pp. 209-214
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 49
    • 0030772527 scopus 로고    scopus 로고
    • Effects of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts
    • Inouye K, Lee SB, Nambu K, Tonomura B. Effects of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts. J Biochem 1997;122:358-64,
    • (1997) J Biochem , vol.122 , pp. 358-364
    • Inouye, K.1    Lee, S.B.2    Nambu, K.3    Tonomura, B.4
  • 50
    • 4644307860 scopus 로고    scopus 로고
    • Substrate-dependent activation of thermolysin by salt
    • Oneda H, Muta Y, Inouye K. Substrate-dependent activation of thermolysin by salt. Biosci Biotechnol Biochem 2004;68:1811-3.
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 1811-1813
    • Oneda, H.1    Muta, Y.2    Inouye, K.3
  • 51
    • 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 SB, Tonomura B. Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem J 1996:315 (Pt 1)133-8.
    • (1996) Biochem J , vol.315 , Issue.PART 1 , pp. 133-138
    • Inouye, K.1    Lee, S.B.2    Tonomura, B.3
  • 52
    • 34548801455 scopus 로고    scopus 로고
    • A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli
    • Yasukawa K, Kusano M, Inouye K. A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli. Protein Eng Des Sel 2007;20:375-83.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 375-383
    • Yasukawa, K.1    Kusano, M.2    Inouye, K.3
  • 53
    • 0021314461 scopus 로고
    • Structural and functional aspects of domain motions in proteins
    • Bennett WS, Huber R. Structural and functional aspects of domain motions in proteins. CRC Crit Rev Biochem 1984;15:291-384.
    • (1984) CRC Crit Rev Biochem , vol.15 , pp. 291-384
    • Bennett, W.S.1    Huber, R.2
  • 54
    • 0036618346 scopus 로고    scopus 로고
    • Hausrath AC, Matthews BW. Thermolysin in the absence of substrate has an open conformation. Acta Crystallogr D Biol Crystallogr 2002;58(Pt 6 Pt 2):1002-7.
    • Hausrath AC, Matthews BW. Thermolysin in the absence of substrate has an open conformation. Acta Crystallogr D Biol Crystallogr 2002;58(Pt 6 Pt 2):1002-7.
  • 55
    • 0000050728 scopus 로고
    • Flexible friends
    • Dobson CM. Flexible friends. Curr Biol 1993;3:530-2.
    • (1993) Curr Biol , vol.3 , pp. 530-532
    • Dobson, C.M.1
  • 56
    • 0021902413 scopus 로고
    • Mapping protein dynamics by X-ray diffraction
    • Ringe D, Petsko GA. Mapping protein dynamics by X-ray diffraction. Prog Biophys Mol Biol 1985;45:197-235.
    • (1985) Prog Biophys Mol Biol , vol.45 , pp. 197-235
    • Ringe, D.1    Petsko, G.A.2
  • 57
    • 0028934005 scopus 로고
    • The importance of being floppy
    • Wagner G. The importance of being floppy. Nat Struct Biol 1995;2:255-7.
    • (1995) Nat Struct Biol , vol.2 , pp. 255-257
    • Wagner, G.1
  • 58
    • 0026489329 scopus 로고
    • Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
    • Holland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN et al. Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochemistry 1992;31:11310-6.
    • (1992) Biochemistry , vol.31 , pp. 11310-11316
    • Holland, D.R.1    Tronrud, D.E.2    Pley, H.W.3    Flaherty, K.M.4    Stark, W.5    Jansonius, J.N.6
  • 59
    • 0033613193 scopus 로고    scopus 로고
    • Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: Structural parameters for a Zn monodentation or bidentation in metalloendopeptidases
    • Gaucher JF, Selkti M, Tiraboschi G, Prange T, Roques BP, Tomas A et al. Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases. Biochemistry 1999;38:12569-76.
    • (1999) Biochemistry , vol.38 , pp. 12569-12576
    • Gaucher, J.F.1    Selkti, M.2    Tiraboschi, G.3    Prange, T.4    Roques, B.P.5    Tomas, A.6
  • 60
    • 0021744255 scopus 로고
    • An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides
    • Hangauer DG, Monzingo AF, Matthews BW. An interactive computer graphics study of thermolysin-catalyzed peptide cleavage and inhibition by N-carboxymethyl dipeptides. Biochemistry 1984;23:5730-41.
    • (1984) Biochemistry , vol.23 , pp. 5730-5741
    • Hangauer, D.G.1    Monzingo, A.F.2    Matthews, B.W.3
  • 61
    • 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 ion-dependent inactivation of thermolysin
    • Hashida Y, Inouye K. Molecular mechanism of the inhibitory effect of cobalt ion on thermolysin activity and the suppressive effect of calcium ion on the cobalt ion-dependent inactivation of thermolysin. J Biochem 2007;141:879-88.
    • (2007) J Biochem , vol.141 , pp. 879-888
    • Hashida, Y.1    Inouye, K.2
  • 62
    • 0023839658 scopus 로고
    • The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis
    • Holden HM, Matthews BW. The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis. J Biol Chem 1988;263:3256-60.
    • (1988) J Biol Chem , vol.263 , pp. 3256-3260
    • Holden, H.M.1    Matthews, B.W.2
  • 63
    • 0028158656 scopus 로고
    • Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex
    • Holland DR, Barclay PL, Danilewicz JC, Matthews BW, James K. Inhibition of thermolysin and neutral endopeptidase 24.11 by a novel glutaramide derivative: X-ray structure determination of the thermolysin-inhibitor complex. Biochemistry 1994;33:51-6.
    • (1994) Biochemistry , vol.33 , pp. 51-56
    • Holland, D.R.1    Barclay, P.L.2    Danilewicz, J.C.3    Matthews, B.W.4    James, K.5
  • 64
    • 0022632152 scopus 로고
    • Binding between thermolysin and its specific inhibitor, N-phosphoryl-L-leucyl-L-tryptophan (PIT)
    • Kitagishi K, Hiromi K. Binding between thermolysin and its specific inhibitor, N-phosphoryl-L-leucyl-L-tryptophan (PIT). J. Biochem 1986;99:191-7.
    • (1986) J. Biochem , vol.99 , pp. 191-197
    • Kitagishi, K.1    Hiromi, K.2
  • 66
    • 0021680137 scopus 로고
    • Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: A novel class of transition-state analogues for zinc peptidases
    • Monzingo AF, Matthews BW. Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases. Biochemistry 1984;23:5724-9.
    • (1984) Biochemistry , vol.23 , pp. 5724-5729
    • Monzingo, A.F.1    Matthews, B.W.2
  • 67
    • 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, Inouye K. Characterization of Gly-D-Phe, Gly-L-Leu, and D-Phe as affinity ligands to thermolysin. Protein Expr Purif 2006;46:332-6.
    • (2006) Protein Expr Purif , vol.46 , pp. 332-336
    • Yasukawa, K.1    Kusano, M.2    Nakamura, K.3    Inouye, K.4
  • 68
    • 0026093346 scopus 로고
    • Differential binding energy: A detailed evaluation of the influence of hydrogen-bonding and hydrophobic groups on the inhibition of thermolysin by phosphorus-containing inhibitors
    • Morgan B, Scholtz JM, Ballinger MD, Zipkin ID, Bartlett PA. Differential binding energy: a detailed evaluation of the influence of hydrogen-bonding and hydrophobic groups on the inhibition of thermolysin by phosphorus-containing inhibitors. J Am Chem Soc 1991;113:297-307.
    • (1991) J Am Chem Soc , vol.113 , pp. 297-307
    • Morgan, B.1    Scholtz, J.M.2    Ballinger, M.D.3    Zipkin, I.D.4    Bartlett, P.A.5
  • 70
    • 2142710121 scopus 로고    scopus 로고
    • A silanediol inhibitor of the metalloprotease thermolysin: Synthesi and comparison with a phosphinic acid inhibitor
    • Kim J, Sieburth SM. A silanediol inhibitor of the metalloprotease thermolysin: synthesi and comparison with a phosphinic acid inhibitor. J Org Chem 2004;69:3008-14.
    • (2004) J Org Chem , vol.69 , pp. 3008-3014
    • Kim, J.1    Sieburth, S.M.2
  • 71
    • 0018786945 scopus 로고
    • Inhibition of thermolysin and carboxypeptidase A by phosphoramidates
    • Kam CM, Nishino N, Powers JC. Inhibition of thermolysin and carboxypeptidase A by phosphoramidates. Biochemistry 1979;18:3032-8.
    • (1979) Biochemistry , vol.18 , pp. 3032-3038
    • Kam, C.M.1    Nishino, N.2    Powers, J.C.3
  • 72
    • 0017810151 scopus 로고
    • Peptide hydroxamic acids as inhibitors of thermolysin
    • Nishino N, Powers JC. Peptide hydroxamic acids as inhibitors of thermolysin. Biochemistry 1978;17:2846-50.
    • (1978) Biochemistry , vol.17 , pp. 2846-2850
    • Nishino, N.1    Powers, J.C.2
  • 73
    • 0018780188 scopus 로고
    • Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography
    • Nishino N, Powers JC. Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography. Biochemistry 1979;18:4340-7.
    • (1979) Biochemistry , vol.18 , pp. 4340-4347
    • Nishino, N.1    Powers, J.C.2
  • 74
    • 0017400132 scopus 로고
    • A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances
    • Weaver LH, Kester WR, Matthews BW. A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances. J Mol Biol 1977;114:119-32.
    • (1977) J Mol Biol , vol.114 , pp. 119-132
    • Weaver, L.H.1    Kester, W.R.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.