CRAT
CRAT (carnitine O-acetyltransferase, also known as CAT1 and carnitine acetyltransferase) is a carnitine acyltransferase that catalyses the reversible transfer of acyl groups between carnitine and coenzyme A. It regulates the acyl-CoA/CoA ratio and contributes to energy homeostasis and fat metabolism. Browse Assay Genie's current range of CRAT research reagents below, or read on for the biology behind the target.
CRAT catalyses the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine, and in the reverse direction from carnitine to coenzyme A (CoA). In doing so it regulates the acyl-CoA/CoA ratio, a balance that matters for cellular energy metabolism. The enzyme also plays a crucial role in the transport of fatty acids for beta-oxidation, and it is responsible for the synthesis of short- and branched-chain acylcarnitines.
Substrate preferences have been characterised in some detail. CRAT is active towards certain intermediates of the branched-chain amino acid oxidation (BCAAO) pathway, whereas trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates. The protein belongs to the carnitine/choline acetyltransferase family, and the CRAT gene is classed by HGNC in the carnitine acyltransferases group. It is described by NCBI Gene as a key metabolic pathway enzyme with an important role in energy homeostasis and fat metabolism.
UniProt reports CRAT in the endoplasmic reticulum, peroxisome, mitochondrion and inner mitochondrial membrane, and NCBI Gene notes that it is found in both the mitochondria and the peroxisome. Alternative splicing produces transcript variants encoding different isoforms that may localise to different subcellular compartments. The enzyme was formerly named carnitine acetyltransferase, and CAT1 is a previous symbol for the gene. Mouse and rat both carry a Crat ortholog, which allows the enzyme to be studied in common rodent models.
CRAT contributes to the transport of fatty acids for beta-oxidation, making it a relevant enzyme for studies of lipid catabolism.
As a key metabolic enzyme in energy homeostasis and fat metabolism, CRAT is studied in work on how cells balance fuel use.
CRAT regulates the acyl-CoA/CoA ratio by shuttling acyl groups to and from carnitine, a point of control in metabolic studies.
CRAT acts on some branched-chain amino acid oxidation intermediates, linking it to studies of amino acid catabolism.
CRAT catalyses the reversible transfer of acyl groups between carnitine and coenzyme A, and so regulates the acyl-CoA/CoA ratio. It also plays a crucial role in the transport of fatty acids for beta-oxidation and synthesises short- and branched-chain acylcarnitines.
CRAT stands for carnitine O-acetyltransferase. Its previous name was carnitine acetyltransferase, and CAT1 is a previous gene symbol. Alternative splicing gives transcript variants that encode different isoforms, which may localise to different subcellular compartments.
CRAT is found in the mitochondria and the peroxisome, with UniProt also listing the endoplasmic reticulum and inner mitochondrial membrane. Mouse and rat each have a Crat ortholog; check the datasheet of any product for its validated reactivity.
Other carnitine acyltransferases and fatty acid metabolism enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P43155; product specifications from Assay Genie datasheets.