Literature summary for 1.1.1.284 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.

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Inhibitors

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
12-hydroxydodedecanoic acid + glutathione + NAD+	-	Homo sapiens	12-oxododecanoic acid + ?	-	?
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]

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Homo sapiens

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Release 2023.1 (January 2023)