Article
Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis.
Nature - 1 Jan 2000
Clarke A R, Wigley D B, Chia W N, Barstow D, Atkinson T, Holbrook J J
Abstract excerpt
The binding of substrates to lactate dehydrogenases induces a marked rearrangement of the protein structure in which a 'loop' of polypeptide (residues 98-110) closes over the active site of the enzyme. In this rearrangement, arginine 109 (a basic residue conserved in all known lactate dehydrogenase sequences and in the homologous malate dehydrogenases) moves 0.8 nm from a position in the solvent to one in the...
Topics
- Arginine
- Genes
- Genes, Bacterial
- Geobacillus stearothermophilus
- Kinetics
- L-Lactate Dehydrogenase
- Mutation
- Protein Binding
- Protein Conformation