메뉴 건너뛰기




Volumn 20, Issue 2, 1994, Pages 149-166

Cold adaption of enzymes: Structural comparison between salmon and bovine trypsins

Author keywords

anionic; catalytic efficiency; cold adaption; crystal structure; ectotherm; protein stability

Indexed keywords

TRYPSIN;

EID: 0028033122     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340200205     Document Type: Article
Times cited : (135)

References (61)
  • 10
    • 0027516857 scopus 로고
    • Refined 1.6 Å resolution crystal structure of the complex formed between porcine β‐trypsin and MCTI‐A, a trypsin inhibitor of the squash family. Detailed comparison with bovine β‐trypsin and its complex
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 33
    • 0000359399 scopus 로고
    • On the purification and characterization of three anionic, serine‐type peptide hydrolases from antarctic Krill, Euphausia superba
    • (1985) Comp. Biochem. Physiol. , vol.82 B , pp. 607-619
    • Osnes1    Mohr, V.2
  • 34
    • 0016271762 scopus 로고
    • Temperature adaption of enzymes: A proposed molecular basis for the different catalytic efficiencies of enzymes from ectoterms and endoterms
    • (1974) Comp. Biochem. Physiol. , vol.49 B , pp. 307-312
    • Low, P.S.1    Somero, G.N.2
  • 41
    • 0001099937 scopus 로고
    • Traitement Statistique des Erreurs dans al Determination des Structures Cristallines
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzatti, P.V.1
  • 44
    • 0015518520 scopus 로고
    • Structure of crystalline α‐chymotrypsin V. The atomic structure of tosyl‐α‐chymotrypsin at 2 Å resolution
    • (1972) J. Mol. Biol. , vol.68 , pp. 187-220
    • Birktoft, J.J.1    Blow, D.M.2
  • 48
    • 0001666380 scopus 로고
    • On the mechanism of enzyme action. XLVI. The effect of certain ions on crystalline trypsin and reinvestigation of its isoelectric point
    • (1951) Arch. Biochem. Biophys. , vol.33 , pp. 320-332
    • Bier, M.1    Nord, F.F.2
  • 56
    • 0016771378 scopus 로고
    • The refined crystal structure of bovine β‐trypsin at 1.8 Å resolution. I. Crystallization, data collection and application of Patterson search techniques
    • (1975) J. Mol. Biol. , vol.98 , pp. 683-692
    • Fehlhammer, H.1    Bode, W.2
  • 57
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine β‐trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site and active site at pH 7.0
    • (1975) J. Mol. Biol. , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 61
    • 0019889789 scopus 로고
    • Direct determination of protonation states of aspartic acid‐102 and histidine‐57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin
    • (1981) Biochemistry , vol.20 , pp. 6462-6474
    • Kossiakoff, A.A.1    Spencer, S.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.