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Inhibition of indolethylamine-N-methyltransferase by S-Adenosylhomocysteine

โœ Scribed by R.-L. Lin; N. Narasimhachari; H.E. Himwich

Book ID
118854655
Publisher
Elsevier Science
Year
1973
Tongue
English
Weight
387 KB
Volume
54
Category
Article
ISSN
0006-291X

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Affinity chromatography of an S-adenosylmethionine-dependent methyltransferase using immobilized S-adenosylhomocysteine : Purification of the indolethylamine N-methyltransferases of Phalaris Tuberosa
โœ J.P.G. Mack; M.B. Slaytor ๐Ÿ“‚ Article ๐Ÿ“… 1978 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 579 KB

In the cases that have been studied so far, S-adenosylhomocysteine (SAH) is a powerful inhibitor of S-adenosylmethionine (SAM) binding to SAM-dependent methyltransferases. We deduced, from the available data on the binding of SAM and SAH analogues to SAM dependent methyltransferases, that linkage of