Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a rate-limited product complex formed during a single initial round of turnover by isocitrate dehydrogenase has been determined. Photolytic liberation of either caged substrate or caged cofactor and Laue X-ray data collection were used to visualize the complex, which has a minimum half-life of approximately 10 milliseconds. The experiment was conducted with three different photoreactive compounds, each possessing a unique mechanism leading to the formation of the enzyme-substrate (ES) complex. Photoreaction efficiency and subsequent substrate affinities and binding rates in the crystal are critical parameters for these experiments. The structure suggests that CO2 dissociation is a rapid event that may help drive product formation, and that small conformational changes may contribute to slow product release.
Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs.,Stoddard BL, Cohen BE, Brubaker M, Mesecar AD, Koshland DE Jr Nat Struct Biol. 1998 Oct;5(10):891-7. PMID:9783749[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stoddard BL, Cohen BE, Brubaker M, Mesecar AD, Koshland DE Jr. Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogs. Nat Struct Biol. 1998 Oct;5(10):891-7. PMID:9783749 doi:10.1038/2331
