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Literature summary for 2.1.1.28 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

Inhibitors Comment Organism Structure
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
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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
adrenal gland
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Ki Value [mM]

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