A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment

Science

Volumn 278, Issue 5340, 1997, Pages 1128-1132

  Ash, Elissa L ^a   Sudmeier, James L ^a   De Fabo, Edward C ^b   Bachovchin, William W ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b GEORGE WASHINGTON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SERINE PROTEINASE;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; EXPERIMENT; FRACTIONATION; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; THEORY;

ASPARTIC ACID; BINDING SITES; BORONIC ACIDS; CATALYSIS; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; OLIGOPEPTIDES; PROTONS; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; SUBTILISINS; TEMPERATURE; UROCANIC ACID;

EID: 0030723218     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5340.1128     Document Type: Article

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41. We thank R. M. Day for supplying the subtilisin BPN' NMR sample, C. A. Kettner for supplying boronic acid inhibitors, and N. I. Krinsky for helpful discussions. Supported in part by NIH grant GM27927.