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Crat-mediated acetyl group buffering is essential for optimal exercise performance.
structural model for L-CPT I (show CPT1A Proteins) (liver CPT I (show CPT1A Proteins)), based on the similarity of this enzyme to the recently crystallized mouse carnitine acetyltransferase
The predicted full length cDNA sequence of the porcine CRAT gene was characterised and a new 5' variant for dog, rat and mouse was proposed.
CrAT turned out to be active towards some but not all the BCAAO intermediates tested and no activity was found with dicarboxylic acyl-CoA (show GNPAT Proteins) esters.
the purification, crystallization and preliminary X-ray crystallographic studies of human carnitine acetyltransferase are reported
structure of a binary complex of human peroxisomal carnitine acetyltransferase and the substrate l-carnitine, refined to a resolution of 1.8; site-directed mutagenesis and kinetic characterization
Data show that CrAT overexpression in primary human skeletal myocytes increased glucose uptake and attenuated lipid-induced suppression of glucose oxidation.
Human CPT1A (show CPT1A Proteins), CPT1B (show CPT1B Proteins), CPT2 (show CPT2 Proteins), CROT (show CROT Proteins) and CRAT are known to encode active carnitine acyltransferases. Earlier pfam annotations refer to the non-existing compound CARNITATE. In 2000 this has been changed to CARNITINE.
This gene encodes carnitine acetyltransferase (CRAT), which is a key enzyme in the metabolic pathway in mitochondria, peroxisomes and endoplasmic reticulum. CRAT catalyzes the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine and regulates the ratio of acylCoA/CoA in the subcellular compartments. Two transcript variants encoding different isoforms have been found for this gene.
, Carnitine acetyltransferase
, carnitine O-acetyltransferase
, carnitine acetylase
, carnitine acetyl transferase