Article
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
Science (New York, N.Y.) - 29 Oct 2004
Frank René A W, Titman Christopher M, Pratap J Venkatesh, Luisi Ben F, Perham Richard N
Abstract excerpt
Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in...
Topics
- Amino Acid Substitution
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Dihydrolipoyllysine-Residue Acetyltransferase
- Geobacillus stearothermophilus
- Hydrogen-Ion Concentration
- Hydrophobic and Hydrophilic Interactions
- Kinetics
- Models, Molecular
- Mutation
- Phosphorylation