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Literature summary for 4.6.1.1 extracted from

  • Yoshimura, M.; Pearson, S.; Kadota, Y.; Gonzalez, C.E.
    Identification of ethanol responsive domains of adenylyl cyclase (2006), Alcohol. Clin. Exp. Res., 30, 1824-1832.
    View publication on PubMed
Search for more literature for 4.6.1.1

Activating Compound

Activating Compound Comment Organism Structure
ethanol AC2 is less responsive to ethanol than rat AC3 or human AC7, N-terminal 28-amino-acid region of the C1a domain and the C-terminal region of the AC molecule are important for the enhancement of AC activity by ethanol Rattus norvegicus
ethanol AC3 is far less responsive, AC2 is less responsive to ethanol than human AC7, N-terminal 28-amino-acid region of the C1a domain and the C-terminal region of the adenylate cyclase molecule are important for the enhancement of adenylate cyclase activity by ethanol Rattus norvegicus
ethanol AC7 is the most ethanol responsive isoform, N-terminal 28-amino-acid region of the C1a domain and the C-terminal region of the AC molecule are important for the enhancement of AC activity by ethanol Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
chimeras inserted into the mammalian expression vector pCMV-SK, wild-type and chimeric mutants expressed in HEK-293 cells Homo sapiens
chimeras inserted into the mammalian expression vector pCMV-SK, wild-type and chimeric mutants expressed in HEK-293 cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information AC7-AC2 chimeric mutants, regardless of the origin of the N-terminal tail, C1b, M1, and M2 domains, the ethanol response of the mutant is similar to that of the parent isoform of AC, from which the C1a and C2 domains are derived Rattus norvegicus
additional information AC7–AC3 chimeric mutants, exchange of the putative transmembrane domains, M1 and M2 or of the N-terminal tail has no effect on the ethanol response of enzyme activity Homo sapiens
additional information AC7–AC3 chimeric mutants, exchange of the putative transmembrane domains, M1 and M2 or of the N-terminal tail has no effect on the ethanol response of enzyme activity Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Homo sapiens P51828
-
-
Rattus norvegicus P21932
-
-
Rattus norvegicus P26769
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP
-
 Homo sapiens 3',5'-cAMP + diphosphate
-
 ?
ATP
-
 Rattus norvegicus 3',5'-cAMP + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
AC2
-
 Rattus norvegicus
AC3
-
 Rattus norvegicus
AC7
-
 Homo sapiens