Literature summary extracted from

Fernandez, M.R.; Biosca, J.A.; Torres, D.; Crosas, B.; Pares, X.
A double residue substitution in the coenzyme-binding site accounts for the different kinetic properties between yeast and human formaldehyde dehydrogenases (1999), J. Biol. Chem., 274, 37869-37875.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.1.1.284	D267E	kinetic properties identical to that of wild-type enzyme	Saccharomyces cerevisiae
1.1.1.284	D267E/T269I	Km-value for S-hydroxymethylglutathione is about 11fold lower than that of the wild-type enzyme, turnover-number for S-hydroxymethylglutathione is about 8fold lower than that of wild-type enzyme	Saccharomyces cerevisiae
1.1.1.284	D269I	highly unstable enzyme, kinetic properties identical to that of wild-type enzyme	Saccharomyces cerevisiae

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.1.1.284	0.0025	-	S-hydroxymethyl glutathione	mutant D267E/T269I	Saccharomyces cerevisiae
1.1.1.284	0.03	-	S-hydroxymethylglutathione	wild-type enzyme	Saccharomyces cerevisiae
1.1.1.284	0.045	-	NAD+	wilde-type enzyme	Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.1.1.284	80000	-	non-denaturing PAGE	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.1.1.284	formaldehyde + glutathione + NAD+	Saccharomyces cerevisiae	enzyme is not essential but enhances the resistance against formaldehyde	S-formylglutathione + NADH + H+	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.284	Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.1.1.284	-	Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.284	formaldehyde + glutathione + NAD+	the true substrate is a hemimercaptal, S-hydroxymethylglutathione, spontaneously formed from formaldehyde and glutathione	Saccharomyces cerevisiae	S-formylglutathione + NADH + H+	-	?
1.1.1.284	formaldehyde + glutathione + NAD+	enzyme is not essential but enhances the resistance against formaldehyde	Saccharomyces cerevisiae	S-formylglutathione + NADH + H+	-	?
1.1.1.284	formaldehyde + S-hydroxymethyl glutathione + NAD+	-	Saccharomyces cerevisiae	?	-	?

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.1.1.284	4.75	-	S-hydroxymethyl glutathione	mutant D267E/T269I	Saccharomyces cerevisiae
1.1.1.284	51.7	-	S-hydroxymethylglutathione	wild-type enzyme	Saccharomyces cerevisiae

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.284	NAD+	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)