Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.4 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
Search for more literature for 2.5.1.4

Inhibitors

Inhibitors Comment Organism Structure
S-adenosyl-L-homocysteine
-
 Sus scrofa

KM Value [mM]

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

Organism

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

Source Tissue

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Ki Value [mM]

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