CTP:phosphocholine cytidylyltransferase: insights into regulatory mechanisms and novel functions.
A key regulatory enzyme in phosphatidylcholine biosynthesis, CTP:cholinephosphate cytidylyltransferase (CCT), catalyzes the formation of CDP-choline. This review discusses the essential features of CCT and addresses intriguing new insights into the catalytic and regulatory properties of this complex enzyme. Characterization of a lipid-binding segment in rat CCT is described and the role of lipids in CCT activation is discussed. An analysis of the phosphorylation domain is presented and possible physiological rationales for reversible phosphorylation of CCT are discussed. The nuclear localization of CCT is examined in the context of multiple CCT isoforms, as is recent evidence establishing a potential link between CCT activity and vesicular transport.
Clement
J M
JM
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, 48109, USA.
Kent
C
C
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D019916:Choline-Phosphate Cytidylyltransferase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004789:Enzyme Activation; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D050356:Lipid Metabolism; D008969:Molecular Sequence Data; D010766:Phosphorylation
D007527:Isoenzymes; D019916:Choline-Phosphate Cytidylyltransferase