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Literature summary for 1.1.1.284 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.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D267E kinetic properties identical to that of wild-type enzyme Saccharomyces cerevisiae
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
D269I highly unstable enzyme, kinetic properties identical to that of wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae