Covalent reactivity of phosphonate monophenyl esters with serine proteinases: An overlooked feature of presumed transition state analogs

Archives of Biochemistry and Biophysics

Volumn 402, Issue 2, 2002, Pages 281-288

  Nishiyama, Yasuhiro ^a   Taguchi, Hiroaki ^a   Luo, Jin Quan ^a   Zhou, Yong Xin ^a   Burr, Gary ^a   Karle, Sangeeta ^a   Paul, Sudhir ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

Catalytic antibody; Covalent reactivity; Phosphonate monoester; Serine proteinase

Indexed keywords

CATALYTIC ANTIBODY; DYFLOS; ESTER; PEPTIDASE; PHOSPHONATE PHENYL ESTER DERIVATIVE; PHOSPHONIC ACID DERIVATIVE; REAGENT; SERINE PROTEINASE; THROMBIN; TRYPSIN; UNCLASSIFIED DRUG;

ACYLATION; ARTICLE; CATALYSIS; CHEMICAL REACTION; COVALENT BOND; ENZYME ACTIVE SITE; HYDROLYSIS; KINETICS; MASS SPECTROMETRY; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ANTIBODIES; BINDING SITES; CATALYSIS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESTERS; MASS SPECTROMETRY; PHOSPHONIC ACIDS; PROTEASE INHIBITORS; PROTEIN BINDING; SERINE ENDOPEPTIDASES; THROMBIN;

EID: 0037098449     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-9861(02)00087-5     Document Type: Article

References (25)