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Literature summary extracted from

  • Swiatek, K.R.; Simon, L.N.; Chao, K.L.
    Nicotinamide methyltransferase and S-adenosylmethionine: 5-methylthioadenosine hydrolase. Control of transfer ribonucleic acid methylation (1973), Biochemistry, 12, 4670-4674.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.4 S-adenosyl-L-homocysteine
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.4 0.05
-
 S-adenosyl-L-methionine
-
 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.4 Homo sapiens
-
-
-
2.5.1.4 Rattus norvegicus
-
 Sprague-Dawley rat
-
2.5.1.4 Sus scrofa
-
 pig
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.4 KB cell cells Homo sapiens
-
2.5.1.4 liver
-
 Rattus norvegicus
-
2.5.1.4 liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.4 0.061
-
-
 Homo sapiens
2.5.1.4 0.099
-
 porcine liver homogenate supernatant Sus scrofa
2.5.1.4 0.108
-
 pH 5 preparation Sus scrofa
2.5.1.4 0.117
-
 ammonium sulfate-treated, pH 5 enzyme preparation Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.4 S-adenosyl-L-methionine
-
 Sus scrofa 5'-methylthioadenosine + 2-aminobutan-4-olide
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.4 0.05
-
 S-adenosyl-L-homocysteine competitive inhibitor to S-adenosylmethionine Sus scrofa