RGD Reference Report - Cloning of human acetyl-CoA carboxylase-beta and its unique features. - Rat Genome Database

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Cloning of human acetyl-CoA carboxylase-beta and its unique features.

Authors: Ha, J  Lee, JK  Kim, KS  Witters, LA  Kim, KH 
Citation: Ha J, etal., Proc Natl Acad Sci U S A 1996 Oct 15;93(21):11466-70.
RGD ID: 1304210
Pubmed: PMID:8876158   (View Abstract at PubMed)
PMCID: PMC38080   (View Article at PubMed Central)

Acetyl-CoA carboxylase, which has a molecular mass of 265 kDa (ACC-alpha), catalyzes the rate-limiting step in the biosynthesis of long-chain fatty acids. In this study we report the complete amino acid sequence and unique features of an isoform of ACC with a molecular mass of 275 kDa (ACC-beta), which is primarily expressed in heart and skeletal muscles. In these tissues, ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. ACC-beta contains an amino acid sequence at the N terminus which is about 200 amino acids long and may be uniquely related to the role of ACC-beta in controlling carnitine palmitoyltransferase I activity and fatty acid oxidation by mitochondria. If we exclude this unique sequence at the N terminus the two forms of ACC show about 75% amino acid identity. All of the known functional domains of ACC are found in the homologous regions. Human ACC-beta cDNA has an open reading frame of 7,343 bases, encoding a protein of 2,458 amino acids, with a calculated molecular mass of 276,638 Da. The mRNA size of human ACC-beta is approximately 10 kb and is primarily expressed in heart and skeletal muscle tissues, whereas ACC-alpha mRNA is detected in all tissues tested. A fragment of ACC-beta cDNA was expressed in Escherichia coli and antibodies against the peptide were generated to establish that the cDNA sequence that we cloned is that for ACC-beta.

Objects referenced in this article
Gene Acacb acetyl-CoA carboxylase beta Rattus norvegicus

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