[en] The conditions of C---N bond breakage by the serine peptidases have been analysed. A two-way table has been generated where either formamide or protonated formamide serves as minimal model of the scissile C---N bond and where either methanol or the couple CH3O− H+ serves as minimal model of the attacking nucleophile. An addition-elimination reaction is proposed which links the enzyme acylation and deacylation steps.
Disciplines :
Microbiology Chemistry
Author, co-author :
Dive, Georges ; Université de Liège - ULiège > Institut de Chimie > Laboratoire de Chimie Pharmaceutique > Service de Microbiologie
Peeters, Daniel; Université Catholique de Louvain - UCL > Laboratoire de Chimie quantique
Leroy, Georges; Université Catholique de Louvain - UCL > Laboratoire de Chimie quantique
Ghuysen, Jean-Marie ; Université de Liège - ULiège > Institut de Chimie > Laboratoire de Chimie Pharmaceutique > Service de Microbiologie
Language :
English
Title :
Theoretical study of the C-N bond breakage catalyzed by the serine peptidases
Publication date :
February 1984
Journal title :
Journal of Molecular Structure: Theochem
ISSN :
0166-1280
Publisher :
Elsevier Science, Amsterdam, Netherlands
Volume :
16
Pages :
117-126
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
Walsh Enzymatic Reaction Mechanisms, W.H. Freeman and Co; 1979.
Blow, Birktoft, Hartley Nature 1969, 221:337-340.
Naray-Szabo (1983) Unusually large electrostatic field effect of the buried aspartate in serine proteinases: Source of catalytic power. International Journal of Quantum Chemistry 23:723-728.
Bachovchin, Roberts J. Am. Chem. Soc. 1978, 100:8041.
Kossiakoff, Spencer Nature 1980, 288:414.
Kollman, Hayes J. Am. Chem. Soc. 1981, 103:2955-2961.