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Literature summary for 4.6.1.1 extracted from

  • Diel, S.; Beyermann, M.; Navarro Llorens, J.M.; Wittig, B.; Kleuss, C.
    Two Interaction Sites on Mammalian Adenylyl Cyclase Type I and II: modulation by calmodulin and Gbetagamma (2008), Biochem. J., 411, 449-456.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin a second isoform- and regulator-specific contact site in C2 is necessary to render enzyme activity susceptible to calmodulin modulation. In addition to the PFAHL-motif in C1b of ACII, calmodulin requires not only the Ca2+-independent AC28-region in C1b but also a Ca2+-dependent domain in C2a of ACI with the VLG-loop to stimulate this adenylyl cyclase isoform Bos taurus
forskolin
-
Bos taurus
Galphas
-
Bos taurus
Gbetagamma a second isoform- and regulator-specific contact site in C2 is necessary to render enzyme activity susceptible to Gbetagamma modulation. In addition to the PFAHL-motif in C1b of ACII, Gbetagamma contacts the KF-loop in C2 Bos taurus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Sf9 cells Bos taurus

Protein Variants

Protein Variants Comment Organism
additional information ACI-deletion mutants ACI.lambda1057 with reduced catalytic activity and ACI.lambda1094, which like mutant ACIlambda1057 is active and stimulated by Ca/CaM as well as ACI. Mutant ACII.lambda928 is catalytically inactive, mutant ACII.AA930 shows diminished activity, mutants ACII.AA925 or ACII.AA932 show no significant change in Gbetagamma-regulation Bos taurus
V1027A/L1031A is not catalytically active under basal, Galphas- or forskolin-stimulated conditions Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P19754
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP
-
Bos taurus 3',5'-cAMP + diphosphate
-
?

Synonyms

Synonyms Comment Organism
ACI
-
Bos taurus
ACII
-
Bos taurus