1. Homologies in the active site regions of lactate dehydrogenases
- Author
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Susan S. Taylor and Susanna S. Oxley
- Subjects
Protein Conformation ,Biophysics ,Biochemistry ,Species Specificity ,Animals ,Coenzyme binding ,Trypsin ,Amino Acid Sequence ,Amino Acids ,Binding site ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,Binding Sites ,L-Lactate Dehydrogenase ,biology ,Muscles ,Myocardium ,Maleates ,Substrate (chemistry) ,Active site ,Molecular biology ,Peptide Fragments ,Nephropidae ,Enzyme ,chemistry ,Organ Specificity ,biology.protein ,Cattle ,Rabbits ,Lactate dehydrogenases ,Chickens ,Protein Binding ,Cysteine - Abstract
Peptides isolated from several lactate dehydrogenases (EC 1.1.1.27) have been characterized and sequenced. These peptides include much of the substrate binding site as well as the loop of polypeptide chain which shows major conformational changes following coenzyme binding. Despite significant differences in catalytic properties, the amino acid sequence in these two active site regions of the molecule is highly conserved in most cases. A noteable exception is cysteine 165 which at one time was thought to be essential for enzymatic activity. The lactate dehydrogenases investigated were isolated from rabbit muscle, chicken heart, beef heart, and lobster tail.
- Published
- 1976
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