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Literature summary extracted from

  • Lee, H.S.; Schulz, A.R.; Fuller, R.W.
    The interaction of rabbit adrenal norepinephrine N-methyl transferase isozymes with substrates (1978), Arch. Biochem. Biophys., 185, 228-238.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.28 norepinephrine 4 distinct substrate inhibition patterns: enzyme form E1 is not subject to substrate inhibition, isoenzyme E-2 is inhibited by S-adenosyl-L-methionine and norepinephrine, isoenzyme E-3 and E-4 are inhibited by norepinephrine only, isoenzyme E5 is inhibited only by S-adenosyl-L-methionine Oryctolagus cuniculus
2.1.1.28 S-adenosyl-L-methionine 4 distinct substrate inhibition patterns: enzyme form E1 is not subject to substrate inhibition, isoenzyme E-2 is inhibited by S-adenosyl-L-methionine and norepinephrine, isoenzyme E-3 and E-4 are inhibited by norepinephrine only, isoenzyme E5 is inhibited only by S-adenosyl-L-methionine Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.28 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.28 adrenal gland
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.28 norepinephrine + S-adenosyl-L-methionine
-
 Oryctolagus cuniculus epinephrine + S-adenosyl-L-homocysteine
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.28 additional information
-
 additional information
-
 Oryctolagus cuniculus