We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit
- Authors
Hwang, Seon-Kap; Hamada, Shigeki; Okita, Thomas W.
- Abstract
Abstract: The ATP binding region in the catalytically inactive large subunit (LS) of the potato tuber ADP-glucose pyrophosphorylase was identified and investigated. Mutations at the ATP binding significantly affected not only the apparent affinities for ATP and Glc-1-P, and catalytic rate but also in many instances, sensitivity to 3-phosphoglycerate. The catalytic rates of the LS mutant enzymes correlated most strongly with changes in the affinity toward ATP, a relationship substantiated by photoaffinity labeling studies with azido-ATP analog. These results indicate that the LS, although catalytically defective, interacts cooperatively with the catalytic small subunit in binding substrates and effectors and, in turn, influencing net catalysis.
- Subjects
GLUCOSE; SUCROSE; ENZYME kinetics; CHEMICAL kinetics
- Publication
FEBS Letters, 2006, Vol 580, Issue 28/29, p6741
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.11.029