Structural highlights
Function
IDH_ECOLI
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
Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.
Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.,Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL Science. 1995 Jun 2;268(5215):1312-8. PMID:7761851[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL. Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Science. 1995 Jun 2;268(5215):1312-8. PMID:7761851
