Linked Life Data

8631912

Source:http://linkedlifedata.com/resource/pubmed/id/8631912

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1996-7-1
pubmed:abstractText
Mammalian adenylyl cyclases have two homologous cytoplasmic domains (C1 and C2). The first cytoplasmic domain of type I enzyme (IC1) and the second cytoplasmic domain of type II enzyme (IIC2-delta 3, a construct in which 36 N-terminal amino acids of the C2 region are deleted) were expressed and purified to homogeneity. Alone, each had no adenylyl cyclase activity; however, mixing of the two domains in vitro resulted in Gs alpha- and forskolin-activated enzyme activity. The turnover number for Gs alpha- and forskolin-stimulated enzyme activity of the complex between IC1 and IIC2-delta 3 was 8.2 s-1. The concentration of IIC2-delta 3 to achieve half-maximal activation of IC1 was 0.8 and 1.3 microM when stimulated by forskolin and Gs alpha, respectively. The concentration of IIC2-delta 3 needed to complex with IC1 was reduced 10-fold (0.08 microM) when the enzyme was activated by both forskolin and Gs alpha, suggesting that Gs alpha and forskolin increased the affinity of the two cytoplasmic domains for each other.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10941-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Two cytoplasmic domains of mammalian adenylyl cyclase form a Gs alpha- and forskolin-activated enzyme in vitro.
pubmed:affiliation
Department of Pharmacological and Physiological Sciences, University of Chicago, Illinois 60637, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't