Literature summary for 3.1.4.35 extracted from

Heikaus, C.C.; Stout, J.R.; Sekharan, M.R.; Eakin, C.M.; Rajagopal, P.; Brzovic, P.S.; Beavo, J.A.; Klevit, R.E.
Solution structure of the cGMP binding GAF domain from phosphodiesterase 5: insights into nucleotide specificity, dimerization, and cGMP-dependent conformational change (2008), J. Biol. Chem., 283, 22749-22759.

Search for more literature for 3.1.4.35

Cloned(Commentary)

Cloned (Comment)	Organism
-	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
D196A	the mutation disrupts cGMP binding and increases cAMP affinity in constructs containing only GAF (mammalian cGMP-dependent PDEs, Anabaena adenylyl cyclases, and Escherichia coli FhlA), causing an altered cAMP-bound structural conformation	Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
sildenafil	potent PDE5 inhibitor	Mus musculus
tadalafil	potent PDE5 inhibitor	Mus musculus
vardenafil	potent PDE5 inhibitor	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8CG03	-	-

Purification (Commentary)

Purification (Comment)	Organism
purified without addition of cAMP or cGMP by Superose-12 gel filtration	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3',5'-cGMP + H2O	PDE5A has a higher selectivity for cGMP due to much lower cAMP binding affinity	Mus musculus	5'-GMP	-	?

Synonyms

Synonyms	Comment	Organism
3',5'-cyclic nucleotide phosphodiesterase 5	-	Mus musculus
PDE5	-	Mus musculus
PDE5A	isoform	Mus musculus
phosphodiesterase 5	-	Mus musculus

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Release 2023.1 (January 2023)