13C NMR study of how the oxyanion pK(a) values of subtilisin and chymotrypsin tetrahedral adducts are affected by different amino acid residues binding in enzyme subsites S1-S4

Biochemistry

Volumn 38, Issue 19, 1999, Pages 6187-6194

  O'Sullivan, Denis B ^c   O'Connell, Timothy P ^a,c   Mahon, Marrita M ^c   Koenig, Andreas ^b,c   Milne, John J ^c   Fitzpatrick, Teresa B ^c,d   Malthouse, J Paul G ^c  

^a MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

^b UNIVERSITY OF WITTEN HERDECKE   (Germany)

^c UNIVERSITY COLLEGE DUBLIN   (Ireland)

^d ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANION; CHYMOTRYPSIN; SUBTILISIN; CARBON; DRUG DERIVATIVE; METHYL CHLORIDE; PEPTIDE;

ALKYLATION; AMINO ACID SYNTHESIS; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROGEN BOND; PH MEASUREMENT; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY; BINDING SITE; CHEMISTRY; DRUG ANTAGONISM; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; SYNTHESIS;

ALKYLATION; AMINO ACIDS; BINDING SITES; CARBON ISOTOPES; CHYMOTRYPSIN; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; METHYL CHLORIDE; PEPTIDES; SUBTILISINS;

EID: 0033545727     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990126c     Document Type: Article

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