Structural highlights
Evolutionary Conservation
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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.
See Also
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
