Literature summary for 3.1.4.35 extracted from

Kotera, J.; Francis, S.H.; Grimes, K.A.; Rouse, A.; Blount, M.A.; Corbin, J.D.
Allosteric sites of phosphodiesterase-5 sequester cyclic GMP (2004), Front. Biosci., 9, 378-386.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3',5'-cGMP + H2O	Bos taurus	allosteric cGMP-binding sites of PDE5 could regulate cGMP signaling by sequestering cGMP from cGMP-dependent protein kinase and perhaps from the PDE5 catalytic site as well. The cGMP sequestered by binding of cGMP to PDE5 R domain significantly dampens activation of cGMP-dependent protein kinase and hydrolysis of cGMP by PDE5 C domain	5'-GMP	-	?

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3',5'-cGMP + H2O	-	Bos taurus	5'-GMP	-	?
3',5'-cGMP + H2O	allosteric cGMP-binding sites of PDE5 could regulate cGMP signaling by sequestering cGMP from cGMP-dependent protein kinase and perhaps from the PDE5 catalytic site as well. The cGMP sequestered by binding of cGMP to PDE5 R domain significantly dampens activation of cGMP-dependent protein kinase and hydrolysis of cGMP by PDE5 C domain	Bos taurus	5'-GMP	-	?

Synonyms

Synonyms	Comment	Organism
PDE5	-	Bos taurus
phosphodiesterase-5	-	Bos taurus

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Release 2023.1 (January 2023)