Literature summary for 4.6.1.18 extracted from

Almarza, J.; Rincon, L.; Bahsas, A.; Brito, F.
Molecular mechanism for the denaturation of proteins by urea (2009), Biochemistry, 48, 7608-7613.

Search for more literature for 4.6.1.18

Inhibitors

Inhibitors	Comment	Organism	Structure
Urea	mechanism of inhibition, urea inhibits ribonuclease A competitively over a concentration range from 100 mM to 4.0 M, urea with its high dipolar moment is a competitive inhibitor and a very high concentration (more than 4.0 M) of it could denature the enzyme, beginning the interaction with the protein at the active center	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cytidine 2',3'-cyclic monophosphate + H2O	-	Bos taurus	cytidine 3'-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
ribonuclease A	-	Bos taurus
RnaseA	-	Bos taurus

General Information

General Information	Comment	Organism
malfunction	mechanistic model for the denaturation of bovine pancreatic ribonuclease A in urea, a direct interaction between urea and protonated histidine as the initial step for protein inactivation followed by hydrogen bond formation with polar residues, and the breaking of hydrophobic collapse as the final steps for protein denaturation	Bos taurus

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Release 2023.1 (January 2023)