Roles of Lysine1 and Lysine7 Residues of Bovine Pancreatic Ribonuclease in the Enzymatic Activity

1) In order to investigate the roles of Lys1 and Lys7 of RNase A in the enzymatic activity, four S-peptide derivatives were prepared and their abilities to activate S-protein were measured. They are 1-norleucine-S-peptide, 7-norleucine S-peptide, 1,7-di-norleucine-S-peptide, and tri-N-acetyl S-pepti...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1986-10, Vol.100 (4), p.1057-1063
Main Authors: IRIE, Masachika, OHGI, Kazuko, YOSHINAGA, Makiko, YANAGIDA, Tamami, OKADA, Yoshio, TENO, Naoki
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cattle
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Kinetics
Lysine
Peptides - metabolism
Ribonuclease, Pancreatic - metabolism
RNA, Fungal
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Summary:1) In order to investigate the roles of Lys1 and Lys7 of RNase A in the enzymatic activity, four S-peptide derivatives were prepared and their abilities to activate S-protein were measured. They are 1-norleucine-S-peptide, 7-norleucine S-peptide, 1,7-di-norleucine-S-peptide, and tri-N-acetyl S-peptide. 2) From the analyses of the relative activity and kinetic parameters of RNase S' derivatives with UpU, UpU> p, and UpUpU> p, it was concluded that Lys7 of RNase A is a binding site for 3′-phosphate of UpU > p and the modification or substitution of Lys1 affects the binding of trinucleotide substrate.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a121785