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Volumn 5, Issue 6, 2001, Pages 559-565+VIII

Specificity pocket water network and its role in the activity of proteolytic enzymes: Revealed by crystal structures of trypsin

Author keywords

Active site geometry; Activity of trypsin; Autolysate; Network of water molecules; Recognition amino acid water interaction

Indexed keywords

ALPHA TRYPSIN; AMINO ACID; ASPARTIC ACID; BETA TRYPSIN; EPSILON TRYPSIN; HISTIDINE; PROTEINASE; SERINE; THROMBIN; TRYPSIN; UNCLASSIFIED DRUG;

EID: 0035761657     PISSN: 10258140     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (14)
  • 1
    • 0027941821 scopus 로고
    • Refined 1.8 Å resolution crystal structure of the porcine ε trypsin
    • Huang Q, Wang Z, Li Y, Liu S, Tang Y. Refined 1.8 Å resolution crystal structure of the porcine ε trypsin, Biochemica et Biophysica Acta 1994; 1209: 77-82.
    • (1994) Biochemica et Biophysica Acta , vol.1209 , pp. 77-82
    • Huang, Q.1    Wang, Z.2    Li, Y.3    Liu, S.4    Tang, Y.5
  • 2
    • 0030954450 scopus 로고    scopus 로고
    • The first crystal structure at 1.8 Å resolution of an active autolysate form of porcine α trypsin
    • Johnson A, Krishnaswamy S, Sundaram P.V, Pattabhi V. The first crystal structure at 1.8 Å resolution of an active autolysate form of porcine α trypsin, Acta Cryst. 1997; D53: 311-315.
    • (1997) Acta Cryst. , vol.D53 , pp. 311-315
    • Johnson, A.1    Krishnaswamy, S.2    Sundaram, P.V.3    Pattabhi, V.4
  • 3
    • 0014670506 scopus 로고
    • Pseudotrypsin, a modified bovine trypsin produced by limited autodigestion
    • Smith RL, Shaw E. Pseudotrypsin, A modified bovine trypsin produced by limited autodigestion, J. Biol. Chem. 1969; 244: 4704-4707.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4704-4707
    • Smith, R.L.1    Shaw, E.2
  • 4
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the comples formed between porcine β trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with the bovine β trypsin and its complexes
    • Huang, Q, Liu S. Tang Y. Refined 1.6 Å resolution crystal structure of the comples formed between porcine β trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with the bovine β trypsin and its complexes, J. Mol. Biol. 1993; 229: 1022-1036.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 5
    • 0028519286 scopus 로고
    • Prediction of novel serine protease inhibitor
    • Kurinov I, Harrison R.W. Prediction of novel serine protease inhibitor Nature Struct. Biol. 1994; 1: 735-743.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 735-743
    • Kurinov, I.1    Harrison, R.W.2
  • 6
    • 0024791521 scopus 로고
    • Crystal structure of bovine β trypsin at 1.5 Å resolution in a crystal form with low molecular packing density
    • Bartunik H.D, Summers L.J, Bartsch H.H. Crystal structure of bovine β trypsin at 1.5 Å resolution in a crystal form with low molecular packing density, J. Mol. Biol. 1989; 210: 813-828.
    • (1989) J. Mol. Biol. , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3
  • 7
    • 0017585038 scopus 로고
    • Reexamination of the charge relay system in subtilisin comparison with other serine proteases
    • Mathews D.A, Alden R.A, Birkroft J.J, Freer S.T, Kraut J. Reexamination of the charge relay system in subtilisin comparison with other serine proteases, J. Biol. Chem. 1977; 252: 8875-8883.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8875-8883
    • Mathews, D.A.1    Alden, R.A.2    Birkroft, J.J.3    Freer, S.T.4    Kraut, J.5
  • 8
    • 0032724963 scopus 로고    scopus 로고
    • Crystal structure at 1.63 Å resolution of the native form of porcine β-trypsin: Revealing an acetate ion binding site and functional water network
    • Johnson A, Gautham N, Pattabhi V. Crystal structure at 1.63 Å resolution of the native form of porcine β-trypsin: revealing an acetate ion binding site and functional water network, Biochimica et Biophysica acta 1999; 1435: 7-21.
    • (1999) Biochimica et Biophysica Acta , vol.1435 , pp. 7-21
    • Johnson, A.1    Gautham, N.2    Pattabhi, V.3
  • 9
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R, Bode W. Structural basis of the activation and action of trypsin, Acc. Chem. Res. 1978; 11: 114-122.
    • (1978) Acc. Chem. Res. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 10
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in Trypsin, Trypsinogen and its complexes with inhibitors
    • Marquart M, Walter J, Deisennofer J, Bode W, Huber R. The geometry of the reactive site and of the peptide groups in Trypsin, Trypsinogen and its complexes with inhibitors, Acta Cryst. 1983; B39: 480-490.
    • (1983) Acta Cryst. , vol.B39 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Deisennofer, J.3    Bode, W.4    Huber, R.5
  • 11
    • 0033574398 scopus 로고    scopus 로고
    • The crystal structures of the complexes between bovine β trypsin and ten P1 varients of BPTI
    • Helland R, Otlewski J, Sundheim O, Dadlez M, Smalåas A.O. The crystal structures of the complexes between bovine β trypsin and ten P1 varients of BPTI. J. Mol. Biol. 1999; 287: 923-942.
    • (1999) J. Mol. Biol. , vol.287 , pp. 923-942
    • Helland, R.1    Otlewski, J.2    Sundheim, O.3    Dadlez, M.4    Smalåas, A.O.5
  • 12
    • 0017305810 scopus 로고
    • On the correlation between three-dimensional structure and reactivity for a series of locked substrates of chymotrypsin
    • Rodgers P.S, Goaman L.C.G, Blow D.M. On the correlation between three-dimensional structure and reactivity for a series of locked substrates of chymotrypsin, J. Am. Chem. Soc. 1976; 98: 6690-6695.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 6690-6695
    • Rodgers, P.S.1    Goaman, L.C.G.2    Blow, D.M.3
  • 13
    • 0001261435 scopus 로고
    • A source for the special catalytic power of enzymes
    • Strom D.R. Koshland D.E, Jr. A source for the special catalytic power of enzymes, Proc. Natl. Acad. Sci. 1970; 66: 445-452.
    • (1970) Proc. Natl. Acad. Sci. , vol.66 , pp. 445-452
    • Strom, D.R.1    Koshland D.E., Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.