Literature summary for 4.6.1.1 extracted from

Ritt, M.; Sivaramakrishnan, S.
Correlation between activity and domain complementation in adenylyl cyclase demonstrated with a novel fluorescence resonance energy transfer sensor (2016), Mol. Pharmacol., 89, 407-412 .

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Activating Compound

Activating Compound	Comment	Organism	Structure
forskolin	forskolin binds cyclase relatively weakly in the absence of the Galphas subunit. The presence of Galphas substantially increases the ability of forskolin to complement and activate the cyclase	Homo sapiens

Application

Application	Comment	Organism
analysis	development of a fluorescence resonance energy transfer (FRET) sensor that functions both as a soluble cyclase and a reporter of complementation within the catalytic domain. There is a strong linear correlation between catalytic domain complementation and cyclase activity upon stimulation with forskolin and the Galphas subunit. The sensor is functional in live cells	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
transfection of Sf9 cell	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
2'-d3'-AMP	P-site inhibitor, uncompetitive. A complemented state of the enzyme is strongly stabilized by the presence of the inhibitor and diphosphate; P-site inhibitor, uncompetitive. A complemented state of the enzyme is strongly stabilized by the presence of the inhibitor and diphosphate	Homo sapiens
additional information	presence of diphosphate does not have a significant effect on either cyclase activity or FRET; presence of diphosphate does not have a significant effect on either cyclase activity or FRET	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O95622	isoform Adcy5	-
Homo sapiens	Q08462	isoform Adcy2	-

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Release 2023.1 (January 2023)