A four-proton-families model for pH-dependent enzyme activation: Application to intestinal brush border sucrase
DOI10.1016/0025-5564(92)90011-KzbMATH Open0761.92017OpenAlexW2016596466WikidataQ52420997 ScholiaQ52420997MaRDI QIDQ1194458FDOQ1194458
Authors: Monique Vasseur, Guy van Melle, Regine Frangne, Francisco Alvarado
Publication date: 27 September 1992
Published in: Mathematical Biosciences (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1016/0025-5564(92)90011-k
Recommendations
- A method for writing enzyme rate equations: Application to the estimation of the number and size of key proton families
- Kinetics of a general model for enzyme activation through a limited proteolysis
- Reduction of intrinsic kinetic and thermodynamic barriers for enzyme-catalysed proton transfers from carbon acid substrates
- Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
- Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation
acid ionization reactionfour-proton- families modelpH-dependent enzyme functionthree-proton-families
Cites Work
This page was built for publication: A four-proton-families model for pH-dependent enzyme activation: Application to intestinal brush border sucrase
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q1194458)