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Literature summary for 4.6.1.2 extracted from

  • Robinson, J.W.; Potter, L.R.
    Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain (2012), Sci. Signal., 5, ra65.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.2

Activating Compound

Activating Compound Comment Organism Structure
2'-deoxy-ATP poor allosteric activator Homo sapiens
2'-deoxy-GTP poor allosteric activator Homo sapiens
ATP ATP binding to the allosteric site is essential for the activation of isoform GC-B under physiologic condition. ATP increases the activities 2.4fold for isoform GC-A and 1.4fold for isoform GC-B Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP Homo sapiens
-
 3',5'-cyclic GMP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-deoxy-GTP effective substrate Homo sapiens ?
-
 ?
GTP
-
 Homo sapiens 3',5'-cyclic GMP + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
GC-A
-
 Homo sapiens
GC-B
-
 Homo sapiens
guanyl cyclase B
-
 Homo sapiens
guanylyl cyclase A
-
 Homo sapiens