Journal article
ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit
FEBS letters, Vol.580(28), pp.6741-6748
2006
Handle:
https://hdl.handle.net/2376/110792
PMID: 17137579
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.
Metrics
10 Record Views
Details
- Title
- ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit
- Creators
- Seon-Kap Hwang - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USAShigeki Hamada - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USAThomas W Okita - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA
- Publication Details
- FEBS letters, Vol.580(28), pp.6741-6748
- Academic Unit
- Biological Chemistry, Institute of
- Publisher
- Elsevier B.V
- Identifiers
- 99900547258301842
- Language
- English
- Resource Type
- Journal article