Article
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Biochemistry - 24 Sept 1996
Lee H J, Wang M, Paschke R, Nandy A, Ghisla S, Kim J J
Abstract excerpt
Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active center base-arrangement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr255Glu, have been determined by X-ray crystallography at 2.75 and 2.4 A resolution, respectively. The catalytic base responsible for the alpha-proton abstraction from the thioester...
Topics
- Acyl Coenzyme A
- Acyl-CoA Dehydrogenase
- Acyl-CoA Dehydrogenase, Long-Chain
- Animals
- Binding Sites
- Crystallography, X-Ray
- Glutamic Acid
- Humans
- Hydrogen Bonding
- Kinetics
- Models, Molecular
- Mutation
- Oxidation-Reduction