Structure of Human Carnitine Acetyltransferase
نویسندگان
چکیده
منابع مشابه
Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer.
Carnitine acyltransferases are a family of ubiquitous enzymes that play a pivotal role in cellular energy metabolism. We report here the x-ray structure of human carnitine acetyltransferase to a 1.6-A resolution. This structure reveals a monomeric protein of two equally sized alpha/beta domains. Each domain is shown to have a partially similar fold to other known but oligomeric enzymes that are...
متن کاملCarnitine acetyltransferase in nervous tissue.
Some of the kinetic properties of carnitine acetyltransferase in brain homogenates have been reported with the use of a new, sensitive radiometric method for the determination of acetylcarnitine. Those properties and the distribution pattern of carnitine acetyltransferase in various rat tissues, subcellular fractions, and discrete areas of the brain have been compared with those obtained for ch...
متن کاملStructural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase.
We report the crystal structure of a binary complex of human peroxisomal carnitine acetyltransferase and the substrate l-carnitine, refined to a resolution of 1.8 Angstrom with an R(factor) value of 18.9% (R(free)=22.3%). L-carnitine binds to a preformed pocket in the active site tunnel of carnitine acetyltransferase aligned with His(322). The quaternary nitrogen of carnitine forms a pi-cation ...
متن کاملCytochemical localization of transferase activities: carnitine acetyltransferase.
Two methods for the cytochemical detection of free CoA and their utilization in the finestructural localization of carnitine acetyltransferase in rat heart are described. The first utilizes the reducing property of the SH group of CoA to reduce potassium ferricyanide to potassium ferrocyanide, which in the presence of uranyl ions forms an electron-dense precipitate of uranyl ferrocyanide. The s...
متن کاملThe substrate specificity of carnitine acetyltransferase.
1. A study of the acyl group specificity of the carnitine acetyltransferase reaction [acyl-(-)carnitine+CoASH right harpoon over left harpoon (-)-carnitine+acyl-CoA] has been made with the enzyme from pigeon breast muscle. Acyl groups containing up to 10 carbon atoms are transferred and detailed kinetic investigations with a range of acyl-CoA and acylcarnitine substrates are reported. 2. Acyl-C...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m212356200