Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1981-10-25
pubmed:abstractText
Acetyl-CoA carboxylase, a major rate-limiting enzyme for fatty acid synthesis, is subject to acute regulation by both allosteric modulation and covalent enzyme phosphorylation. Because citrate activation of the enzyme in vitro requires citrate concentrations far in excess of intracellular levels, we have attempted to identify other ligands which might mediate carboxylase activity. Heated liver extracts contain a potent endogenous activator of carboxylase assayed in dialyzed high speed liver supernatant; the activator elutes behind the salt volume of a Bio-Gel P-6 gel filtration column, is destroyed by alkaline phosphatase, and is adsorbed by charcoal. This activator activity is shared by several guanine nucleotides (5'-GTP, 5'-GDP, 5'-GMP, and 3':5'-cyclic GMP). Further separation of the endogenous activator by high pressure liquid chromatography reveals a carboxylase-activating compound which co-elutes with 5'-GMP. The guanine nucleotides are potent activators of carboxylase activity at intracellular nucleotide concentrations and permit expression of maximal enzyme velocity at cytosolic citrate concentrations. However, we have been unable to document any effects of guanine nucleotides on isolated rat liver acetyl-CoA carboxylase. While the mechanisms of these effects remain to be elucidated, they suggest that the guanine nucleotides may be important intracellular regulators of carboxylase activity and of fatty acid synthesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8573-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Regulation of acetyl-CoA carboxylase by guanine nucleotides.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.