Literature summary extracted from

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

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.6.1.18	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

EC Number	Organism	UniProt	Comment	Textmining
4.6.1.18	Bos taurus	-	-	-

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
4.6.1.18	ribonuclease A	-	Bos taurus
4.6.1.18	RnaseA	-	Bos taurus

General Information

EC Number	General Information	Comment	Organism
4.6.1.18	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)