Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1990-6-27
pubmed:databankReference
pubmed:abstractText
Complementary DNAs encoding rat long-chain acyl-CoA synthetase have been isolated. The cDNAs were identified using synthetic oligonucleotide probes based on partial amino acid sequences of lysyl endopeptidase peptides of the purified enzyme. Rat long-chain acyl-CoA synthetase is predicted to contain 699 amino acid residues and to have a calculated molecular weight of 78,177. Significant sequence similarity was found between parts of long-chain acyl-CoA synthetase and firefly luciferase. Based on the similarity of the reaction mechanisms of the two enzymes, we propose a function for the similar region. The long-chain acyl-CoA synthetase mRNA is expressed in liver, heart, and epididymal adipose tissues and, to a much lesser extent, in brain, small intestine, and lung. The level of long-chain acyl-CoA synthetase mRNA is increased 7-8-fold in rat liver by feeding a diet high in carbohydrate or fat, consistent with the physiological significance of the enzyme in fatty acid metabolism.
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
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8681-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2341402-Amino Acid Sequence, pubmed-meshheading:2341402-Animals, pubmed-meshheading:2341402-Base Sequence, pubmed-meshheading:2341402-Beetles, pubmed-meshheading:2341402-Cloning, Molecular, pubmed-meshheading:2341402-Coenzyme A Ligases, pubmed-meshheading:2341402-DNA, pubmed-meshheading:2341402-Gene Expression Regulation, pubmed-meshheading:2341402-Gene Library, pubmed-meshheading:2341402-Luciferases, pubmed-meshheading:2341402-Microsomes, Liver, pubmed-meshheading:2341402-Molecular Sequence Data, pubmed-meshheading:2341402-Oligonucleotide Probes, pubmed-meshheading:2341402-Organ Specificity, pubmed-meshheading:2341402-Plasmids, pubmed-meshheading:2341402-RNA, Messenger, pubmed-meshheading:2341402-Rats, pubmed-meshheading:2341402-Repressor Proteins, pubmed-meshheading:2341402-Restriction Mapping, pubmed-meshheading:2341402-Saccharomyces cerevisiae Proteins, pubmed-meshheading:2341402-Sequence Homology, Nucleic Acid
pubmed:year
1990
pubmed:articleTitle
Structure and regulation of rat long-chain acyl-CoA synthetase.
pubmed:affiliation
Tohoku University Gene Research Center, Sendai, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't