Back to Results
First PageMeta Content
Enzyme kinetics / Enzymes / Metabolism / Catalysis / Hexokinase / Glucokinase / Enzyme / Adenosine triphosphate / Uncompetitive inhibitor / Chemistry / Biology / Enzyme inhibitors


29 Biochem. J[removed], 29–38 (Printed in Great Britain) Kinetic studies of rat liver hexokinase D (‘ glucokinase ’) in non-co-operative conditions show an ordered mechanism with MgADP as the last product to
Add to Reading List

Document Date: 2009-10-20 06:55:40


Open Document

File Size: 197,46 KB

Share Result on Facebook

City

Phillips / Santiago / /

Company

Oxford University Press / ADP / AKm / Wilson / Merck / John Wiley and Sons / AMP / Knight / Liver Metabolism / Springer-Verlag/RG Landes Company / Marseille Laboratory / Scheme 1 / /

Country

France / United States / United Kingdom / Chile / /

Currency

USD / /

Event

Business Partnership / /

Facility

Marseille Laboratory / The complex / E dGlc CrATP complex / E GlcNAc complex / /

IndustryTerm

active site / similar solution / buffer solution / nucleotide site / active-site / allosteric site / Chemical modification / /

Organization

Centre National / Universidad de Chile / †Institut Fe / Biochemical Society / Oxford University / Functional / /

Person

Austin Matschinsky / Athel Cornish-Bowden / Ulrike Heberlein / Eliana Rabajille / Erika Lang / Hermann Niemeyer / Van Schaftingen / Moukil Schaftingen / /

Position

Professor / co-operative / /

Product

Skullcandy G.I. Headphone/Headset / MgATP / studied using MgATP# / /

ProvinceOrState

N. F. / /

TVStation

Kapp / /

Technology

ion exchange / directed mutagenesis / /

SocialTag