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Literature summary extracted from

  • Yamazaki, A.; Tatsumi, M.; Bondarenko, V.A.; Kurono, S.; Komori, N.; Matsumoto, H.; Matsuura, I.; Hayashi, F.; Yamazaki, R.K.; Usukura, J.
    Mechanism for the regulation of mammalian cGMP phosphodiesterase6. 2: isolation and characterization of the transducin-activated form (2010), Mol. Cell. Biochem., 339, 235-251.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.35 membrane
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 Bos taurus 16020
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Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.35 retina
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 Bos taurus
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3.1.4.35 retinal rod
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 Bos taurus
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Subunits

EC Number Subunits Comment Organism
3.1.4.35 More rod photoreceptor cGMP phosphodiesterase consists of a catalytic subunit complex, Palphabeta, and two inhibitory subunits, Pgamma. Isolation of Palphalphabetagammaagammadelta and Palphabetagammadeltadelta suggests that one C-terminus of Palphabeta is involved in the Palphabetagammagamma interaction with membranes, and that Pgamma dissociation opens another C-terminus for Pdelta, a prenyl-binding protein, binding, which may lead to the expression of high PDE activity. Extraction, isolation and analysis of diverse subunit complexes, detailed overview Bos taurus
3.1.4.35 tetramer alphabeta(gamma)2 Bos taurus

Synonyms

EC Number Synonyms Comment Organism
3.1.4.35 cGMP phosphodiesterase6
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 Bos taurus
3.1.4.35 PDE6
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 Bos taurus

General Information

EC Number General Information Comment Organism
3.1.4.35 evolution mechanisms for PDE activation are similar in mammalian and amphibian photoreceptors as well as in rods and cones Bos taurus
3.1.4.35 malfunction identification of a Pgamma-depleted PDE as Palphabetagamma, detailed overview Bos taurus