Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine. | Zendy

Fusao Hirata | Zendy; O. Humberto Viveros | Zendy; Emanuel J. Diliberto | Zendy; J Axelrod | Zendy

Open Access

Identification and properties of two methyltransferases in conversion of phosphatidylethanolamine to phosphatidylcholine.

Author(s) -

Fusao Hirata,

O. Humberto Viveros,

Emanuel J. Diliberto,

J Axelrod

Publication year - 1978

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.75.4.1718

Subject(s) - methyltransferase , phosphatidylethanolamine , phosphatidylcholine , methylation , biochemistry , chemistry , methionine , enzyme , microsome , phospholipid , dna , amino acid , membrane

Two methyltransferases involved in the methylation of phosphatidylethanolamine to form phosphatidylcholine were demonstrated in a microsomal fraction of bovine adrenal medulla. The first methyltransferase catalyzes the methylation of phosphatidylethanolamine to form phosphatidyl-N-monomethylethanolamine. This enzyme has an optimum pH of 6.5, a low Km for S-adenosyl-L-methionine (1.4 micron), and an absolute requirement for Mg2+. The second methyltransferase catalyzes the two successive methylations of phodphatidyl-N-monomethylethanolamine to phosphatidyl-N,N-dimethylethanolamine and phosphatidylcholine. In contrast to the first methyltransferase, it has an optimum pH of 10 and a high Km for S-adenosyl-L-methionine (0.1 mM) and does not require Mg2+.

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