Literature summary extracted from

Kloor, D.; Hermes, M.; Kirschler, J.; Mueller, M.; Hagen, N.; Kalbacher, H.; Stevanovic, S.; Osswald, H.
Determinants for the cAMP-binding site at the S-adenosylhomocysteine-hydrolase (2009), Naunyn Schmiedebergs Arch. Pharmacol., 380, 215-222.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
3.13.2.1	cAMP	cAMP at 0.010 mM enhances the hydrolytic activity of native AdoHcy-hydrolase by 35%, whereas the activity of the enzyme in its NAD+ form is not stimulated by cAMP. The cAMP-binding site at the AdoHcy-hydrolase is independent of the NAD+/NADH ratio of the enzyme and is identical with the high affinity-binding site of adenosine. cAMP does not interact with the catalytic site of AdoHcyhydrolase and does not act as an allosteric effector	Bos taurus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.13.2.1	additional information	not inhibitory: azido-cAMP	Bos taurus

Organism

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

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.13.2.1	kidney	-	Bos taurus	-

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Release 2023.1 (January 2023)