메뉴 건너뛰기




Volumn 11, Issue 4, 2002, Pages 965-973

Direct proton magnetic resonance determination of the pKa of the active center histidine in thiolsubtilisin

Author keywords

Catalytic triad; Protein dielectric constant; Serine protease; Thiolsubtilisin

Indexed keywords

ASPARTIC ACID; BORONIC ACID DERIVATIVE; CHYMOTRYPSIN; HISTIDINE; IMIDAZOLE DERIVATIVE; PHOSPHOSERINE; SERINE; SUBTILISIN; THIOL DERIVATIVE; THIOLACID; TRYPSIN;

EID: 0036130134     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.3890102     Document Type: Article
Times cited : (18)

References (49)
  • 7
    • 0033583716 scopus 로고    scopus 로고
    • Hydrogen bonding to active-site histidine in peptidyl boronic acid inhibitor complexes of chymotrypsin and subtilisin: Proton magnetic resonance assignments and H/D fractionation factors
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4684-4689
    • Bao, D.1    Huskey, W.P.2    Kettner, C.3    Jordan, F.4
  • 17
    • 0023280069 scopus 로고
    • Calculation of electrostatic potentials in an enzyme active site
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.1    Honig, B.2
  • 21
    • 48749149745 scopus 로고
    • Solvent suppression in Fourier transform nuclear magnetic resonance
    • (1983) J. Magn. Reson. , vol.55 , pp. 283-300
    • Hore, P.J.1
  • 22
    • 0024293878 scopus 로고
    • Why ion-pair charge reversal by protein engineering is unlikely to succeed
    • (1988) Nature , vol.334 , pp. 270-272
    • Hwang, J.K.1    Warshel, A.2
  • 23
    • 0019889802 scopus 로고
    • Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and its presence in thiolsubtilisins
    • (1981) Biochemistry , vol.20 , pp. 6366-6370
    • Jordan, F.1    Polgár, L.2
  • 25
    • 0033580678 scopus 로고    scopus 로고
    • Remarkable stabilization of zwitterionic intermediates may account for a billion-fold rate acceleration by thiamin diphosphate-dependent decarboxylases
    • (1999) Biochemistry , vol.38 , pp. 6369-6373
    • Jordan, F.1    Li, H.2    Brown, A.3
  • 29
    • 0028067179 scopus 로고
    • Autoprocessing of prothiolsubtilisin E in which the active site serine 221 is altered to cysteine
    • (1994) J. Biol. Chem. , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 30
    • 0023463943 scopus 로고
    • Complex of α-chymotrypsin and N-acetyl-L-leucyl-L-phenylalanyl trifluoromethyl ketone inhibitor complexes: Structural studies with NMR spectroscopy
    • (1987) Biochemistry , vol.26 , pp. 7603-7608
    • Liang, T.-C.1    Abeles, R.H.2
  • 31
    • 0032566351 scopus 로고    scopus 로고
    • Correlations of the basicity of His57 with transition state analogue binding, substrate reactivity, and the strength of the low-barrier hydrogen bond in chymotrypsin
    • (1998) Biochemistry , vol.37 , pp. 11940-11948
    • Lin, J.1    Cassidy, C.S.2    Frey, P.A.3
  • 32
    • 2042505525 scopus 로고
    • Varian Associates, Palo Alto, CA
    • (1992) Magnetic Moments , vol.2 , pp. 12
  • 34
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive overrelaxation to solve the Poisson-Boltzmann equation
    • (1991) J. Comp. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 35
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • (1995) Science , vol.268 , pp. 1144-1149
  • 45
    • 0023660015 scopus 로고
    • Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering
    • (1987) J. Mol. Biol. , vol.193 , pp. 803-813


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.