title: CTP:phosphocholine cytidylyltransferase.
abstract: CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the synthesis of CDP-choline and is regulatory for phosphatidylcholine biosynthesis. This review focuses on recent developments in understanding the catalytic and regulatory mechanisms of this enzyme. Evidence for the nuclear localization of the enzyme is discussed, as well as evidence suggesting cytoplasmic localization. A comparison of the catalytic domains of CCTs from a wide variety of organisms is presented, highlighting a large number of completely conserved residues. Work implying a role for the conserved HXGH sequence in catalysis is described. The membrane-binding domain in rat CCT has been defined, and the role of lipids in activating the enzyme is discussed. The identification of the phosphorylation domain is described, as well as approaches to understand the role of phosphorylation in enzyme activity. Other possible control mechanisms such as enzyme degradation and gene expression are presented.
authors.affiliation: Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor 48109-0606, USA. ckent@umich.edu
authors.forename: C
authors.initials: C
authors.lastname: Kent
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019916:Choline-Phosphate Cytidylyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D019916:Choline-Phosphate Cytidylyltransferase