• enzymology
  • In enzymology, a hexaprenyldihydroxybenzoate methyltransferase (EC 2.1.1.114) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-hexaprenyl-4,5-dihydroxybenzoate, whereas its two products are S-adenosylhomocysteine and 3-hexaprenyl-4-hydroxy-5-methoxybenzoate. (wikipedia.org)
  • In enzymology, an amine N-methyltransferase (EC 2.1.1.49) is an enzyme that is ubiquitously present in non-neural tissues and that catalyzes the N-methylation of tryptamine and structurally related compounds. (wikipedia.org)
  • In enzymology, a phenol O-methyltransferase (EC 2.1.1.25) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + phenol ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + anisole Thus, the two substrates of this enzyme are S-adenosyl methionine and phenol, whereas its two products are S-adenosylhomocysteine and anisole. (wikipedia.org)
  • In enzymology, a polysaccharide O-methyltransferase (EC 2.1.1.18) is an enzyme that catalyzes the chemical reaction S-adenosyl-L-methionine + 1,4-alpha-D-glucooligosaccharide ⇌ {\displaystyle \rightleftharpoons } S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D-glucose units Thus, the two substrates of this enzyme are S-adenosyl methionine and 1,4-alpha-D-glucooligosaccharide, whereas its two products are S-adenosylhomocysteine and oligosaccharide containing 6-methyl-D-glucose units. (wikipedia.org)
  • found primarily
  • MTases can be divided into three different groups on the basis of the chemical reactions they catalyze: m6A - those that generate N6-methyladenine EC 2.1.1.72 m4C - those that generate N4-methylcytosine EC 2.1.1.113 m5C - those that generate C5-methylcytosine EC 2.1.1.37 m6A and m4C methyltransferases are found primarily in prokaryotes. (wikipedia.org)
  • domain
  • Instead of SET, non-SET domain-containing histone methyltransferase utilizes the enzyme Dot1. (wikipedia.org)
  • The structure of HhaI methyltransferase (M.HhaI) has been resolved to 2.5 A: the molecule folds into 2 domains - a larger catalytic domain containing catalytic and cofactor binding sites, and a smaller DNA recognition domain. (wikipedia.org)
  • Histamine N-Methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal This article incorporates text from the United States National Library of Medicine, which is in the public domain. (wikipedia.org)