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

BRENDA support

Literature summary extracted from

  • Sanghani, P.C.; Stone, C.L.; Ray, B.D.; Pindel, E.V.; Hurley, T.D.; Bosron, W.F.
    Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase (2000), Biochemistry, 39, 10720-10729.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.284 12-oxododecanoic acid substrate inhibition Homo sapiens
1.1.1.284 NAD+ product inhibition Homo sapiens
1.1.1.284 NADH product inhibition Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.284 Zinc zinc-dependent enzyme Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.284 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.284
-
 Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.284 S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+ random bi-bi mechanism for oxidation of S-hydroxymethylglutathione and 12-hydroxydodecanoic acid Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.284 12-hydroxydodedecanoic acid + glutathione + NAD+
-
 Homo sapiens 12-oxododecanoic acid + ?
-
 ?
1.1.1.284 formaldehyde + glutathione + NAD+ the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione Homo sapiens S-formylglutathione + NADH + H+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.284 0.217
-
 12-Hydroxydodecanoic acid
-
 Homo sapiens
1.1.1.284 0.217
-
 NAD+ reaction with 12-hydroxydodecanoic acid Homo sapiens
1.1.1.284 1.04
-
 NAD+
-
 Homo sapiens
1.1.1.284 1.04
-
 S-hydroxymethyl glutathione
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.284 NAD+
-
 Homo sapiens