RGD Reference Report - Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization. - Rat Genome Database

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Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization.

Authors: He, D  Barnes, S  Falany, CN 
Citation: He D, etal., J Lipid Res. 2003 Dec;44(12):2242-9. Epub 2003 Sep 1.
RGD ID: 2312798
Pubmed: PMID:12951368   (View Abstract at PubMed)
DOI: DOI:10.1194/jlr.M300128-JLR200   (Journal Full-text)

Bile acid CoA:amino acid N-acyltransferase (BAT) is responsible for the amidation of bile acids with the amino acids taurine and glycine. Rat liver BAT (rBAT) cDNA was isolated from a rat liver lambdaZAP cDNA library and expressed in Sf9 insect cells using a baculoviral vector. rBAT displayed 65% amino acid sequence homology with human BAT (hBAT) and 85% homology with mouse BAT (mBAT). Similar to hBAT, expressed rBAT was capable of forming both taurine and glycine conjugates with cholyl-CoA. mBAT, which is highly homologous to rBAT, forms only taurine conjugated bile acids (Falany, C. N., H. Fortinberry, E. H. Leiter, and S. Barnes. 1997. Cloning and expression of mouse liver bile acid CoA: Amino acid N-acyltransferase. J. Lipid Res. 38: 86-95). Immunoblot analysis of rat tissues detected rBAT only in rat liver cytosol following homogenization and ultracentrifugation. Subcellular localization of rBAT detected activity and immunoreactive protein in both cytosol and isolated peroxisomes. Rat bile acid CoA ligase (rBAL), the enzyme responsible for the formation of bile acid CoA esters, was detected only in rat liver microsomes. Treatment of rats with clofibrate, a known peroxisomal proliferator, significantly induced rBAT activity, message, and immunoreactive protein in rat liver. Peroxisomal membrane protein-70, a marker for peroxisomes, was also induced by clofibrate, whereas rBAL activity and protein amount were not affected. In summary, rBAT is capable of forming both taurine and glycine bile acid conjugates and the enzyme is localized primarily in peroxisomes in rat liver.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
BaatRatbile acid conjugation involved_inIDA PMID:12951368UniProt 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
BaatRatcytosol located_inIDA PMID:12951368UniProt 
BaatRatperoxisome located_inIDA PMID:12951368UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Slc27a5Ratcholate-CoA ligase activity enablesIDA PMID:12951368UniProt 
BaatRatglycine N-choloyltransferase activity enablesIDA PMID:12951368UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Baat  (bile acid CoA:amino acid N-acyltransferase)
Slc27a5  (solute carrier family 27 member 5)


Additional Information