doi: 10.1016/0014-5793(84)80498-6.
Aspartic acid-121 functions at the active site of bovine pancreatic ribonuclease
- PMID: 6427012
- DOI: 10.1016/0014-5793(84)80498-6
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Aspartic acid-121 functions at the active site of bovine pancreatic ribonuclease
FEBS Lett.
.
Free article
Abstract
The fully active semisynthetic enzyme formed by the non-covalent interaction of residues 1-118 of bovine pancreatic ribonuclease and a synthetic tetradecapeptide containing residues 111-124 of the enzyme has allowed a direct test of the role of aspartic acid-121 in the functioning of the molecule. Replacement of this residue by asparagine results in a derivative that is 4.5% active against cytidine 2',3'-cyclic phosphate at pH 7.0 under standard assay conditions. Further studies with the same substrate at pH 5.8 reveal that the reduced activity results entirely from a diminished catalytic efficiency and not from a decreased affinity for substrate.
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