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Choline Kinase (Crude Enzyme)

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  Post Date: Aug 18,2022
  Expiry Date: Feb 14,2023
  Detailed Description: Cas No. :9026-67-9 Choline kinase (also known as CK,ChoK and choline phosphokinase) is an enzyme which catalyzes the first reaction in the choline pathway for phosphatidylcholine (PC) biosynthesis. This reaction involves the transfer of a phosphate group from adenosine triphosphate (ATP) to choline in order to form phosphocholine. Thus, the two substrates of this enzyme are ATP and choline, whereas its two products are adenosine diphosphate (ADP) and O-phosphocholine. Choline kinase requires magnesium ions (+2) as a cofactor for this reaction. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The first detailed investigation of the enzyme was conducted by McCamen in 1962, where it was shown that the brain is the richest source of the enzyme in mammalian tissue. A related enzyme, ethanolamine kinase, tends to co-purify with choline kinase leading to a suggestion that the two activities are mediated by two distinct active sites on a single protein. These enzymes participate in glycine, serine and threonine metabolism and glycerophospholipid metabolism. In mammalian cells, the enzyme exists as three isoforms: CKα-1,CKα-2 and CKβ. These isoforms are encoded by two separate genes, CHKA and CHKB and are only active in their homodimeric, heterodimeric and oligomeric forms. This product with the indicated enzyme activity was briefly purified from engineered E. coli. https://www.creative-enzymes.com/product/Choline-Kinase-Crude-Enzyme-_16223.html

  CAS Registry Number:

9026-67-9


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