The enzyme 3′,5′-cyclic-GMP phosphodiesterase (EC 3.1.4.35) catalyzes the reaction
3′,5′-cyclic-GMP phosphodiesterase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.4.35 | ||||||||
CAS no. | 9068-52-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- guanosine 3′,5′-cyclic phosphate + H2O guanosine 5′-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 3′,5′-cyclic-GMP 5'-nucleotidohydrolase. Other names in common use include guanosine cyclic 3',5'-phosphate phosphodiesterase, cyclic GMP phosphodiesterase, cyclic 3′,5′-GMP phosphodiesterase, cyclic guanosine 3′,5′-monophosphate phosphodiesterase, cyclic guanosine 3′,5′-phosphate phosphodiesterase, cGMP phosphodiesterase, cGMP-PDE, and cyclic guanosine 3′,5′-phosphate phosphodiesterase.
Structural studies
editAs of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1MC0, 2CHM, 2H40, 2H42, and 2H44.
References
edit- Marks F, Raab I (1974). "The second messenger system of mouse epidermis. IV. Cyclic AMP and cyclic GMP phosphodiesterase". Biochim. Biophys. Acta. 334: 368–377. doi:10.1016/0005-2744(74)90180-6.