Literature summary for 4.6.1.18 extracted from

Moosavi-Movahedi, A.A.; Gharanfoli, M.; Jalili, S.; Ahmad, F.; Chamani, J.; Hakimelahi, G.H.; Sadeghi, M.; Amani, M.; Saboury, A.A.
The correlation of RNase A enzymatic activity with the changes in the distance between Nepsilon2-His12 and N delta1-His119 upon addition of stabilizing and destabilizing salts (2006), Protein J., 25, 117-125.

Search for more literature for 4.6.1.18

Activating Compound

Activating Compound	Comment	Organism	Structure
sulfate	decreases the distance between the catalytic His residues and increases the globular compactness	Bos taurus

Inhibitors

Inhibitors	Comment	Organism	Structure
thiocyanate	inactivation due to expansion of the enzyme surface and elongation of the catalytic center	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P61823	commercial preparation	-

Substrates and Products (Substrate)

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)