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PMID:12810727

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Citation

O'Byrne, J, Hunt, MC, Rai, DK, Saeki, M and Alexson, SE (2003) The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J. Biol. Chem. 278:34237-44

Abstract

Bile acid-CoA:amino acid N-acyltransferase (BACAT) catalyzes the conjugation of bile acids to glycine and taurine for excretion into bile. By use of site-directed mutagenesis and sequence comparisons, we have identified Cys-235, Asp-328, and His-362 as constituting a catalytic triad in human BACAT (hBACAT) and identifying BACAT as a member of the type I acyl-CoA thioesterase gene family. We therefore hypothesized that hBACAT may also hydrolyze fatty acyl-CoAs and/or conjugate fatty acids to glycine. We show here that recombinant hBACAT also can hydrolyze long- and very long-chain saturated acyl-CoAs (mainly C16:0-C26:0) and by mass spectrometry verified that hBACAT also conjugates fatty acids to glycine. Tissue expression studies showed strong expression of BACAT in liver, gallbladder, and the proximal and distal intestine. However, BACAT is also expressed in a variety of tissues unrelated to bile acid formation and transport, suggesting important functions also in the regulation of intracellular levels of very long-chain fatty acids. Green fluorescent protein localization experiments in human skin fibroblasts showed that the hBACAT enzyme is mainly cytosolic. Therefore, the cytosolic BACAT enzyme may play important roles in protection against toxicity by accumulation of unconjugated bile acids and non-esterified very long-chain fatty acids.

Links

PubMed Online version:10.1074/jbc.M300987200

Keywords

Acyltransferases/chemistry; Amino Acid Sequence; Animals; Aspartic Acid/chemistry; Bile Acids and Salts/metabolism; Catalysis; Cloning, Molecular; Cysteine/chemistry; Cytosol/metabolism; DNA, Complementary/metabolism; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fatty Acids/chemistry; Fibroblasts/enzymology; Gallbladder/enzymology; Glycine/chemistry; Green Fluorescent Proteins; Histidine/chemistry; Humans; Intestines/enzymology; Kinetics; Liver/enzymology; Luminescent Proteins/metabolism; Mass Spectrometry; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Recombinant Fusion Proteins/metabolism; Recombinant Proteins/metabolism; Taurine/chemistry; Tissue Distribution

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:BAAT

involved_in

GO:0002152: bile acid conjugation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:BAAT

located_in

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:BAAT

involved_in

GO:0006699: bile acid biosynthetic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:BAAT

involved_in

GO:0006637: acyl-CoA metabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:BAAT

enables

GO:0047963: glycine N-choloyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:BAAT

enables

GO:0052815: medium-chain acyl-CoA hydrolase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:BAAT

enables

GO:0052816: long-chain acyl-CoA hydrolase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:BAAT

enables

GO:0052817: very long chain acyl-CoA hydrolase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:BAAT

located_in

GO:0005829: cytosol

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete


See also

References

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