Article
Genetic reconstruction and characterization of the recombinant transacylase (E2b) component of bovine branched-chain alpha-keto acid dehydrogenase complex. Implication of histidine 391 as an active site residue.
The Journal of biological chemistry - 5 Aug 1990
Griffin T A, Chuang D T
Abstract excerpt
Genetically altered transacylase (E2b) proteins of the bovine branched-chain alpha-keto acid dehydrogenase complex were overexpressed in Escherichia coli and characterized. Deletion by PstI or Bal31 digestion of the amino-terminal region of the inner-core domain (residues 175-421) beyond residue...
Topics
- 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
- Acyltransferases
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Blotting, Western
- Cattle
- Chromosome Deletion
- Cloning, Molecular
- Escherichia coli
- Genetic Vectors
- Histidine
- Hydrogen-Ion Concentration
- Ketone Oxidoreductases
- Kinetics
- Molecular Sequence Data
- Molecular Weight