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Literature summary for 1.2.1.46 extracted from

  • Sanghani, P.C.; Davis, W.I.; Zhai, L.; Robinson, H.
    Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism (2006), Biochemistry, 45, 4819-4830.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
for expression in Escherichia coli BL21 cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
formaldehyde dehydrogenase-adenosine 5'-diphosphate ribose and E67L-NADH binary complexes are determined Homo sapiens

Protein Variants

Protein Variants Comment Organism
E67L mutant shows, that Glu67 is critical for capturing the substrates for catalysis Homo sapiens
R368L mutant shows, that the predominant role of Arg-368 is in the binding of the coenzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
dodecanoic acid
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0017
-
S-hydroxymethylglutathione oxidation of S-hydroxymethylglutathione, formaldehyde dehydrogenase Homo sapiens
0.002
-
NADH oxidation of NADH, formaldehyde dehydrogenase Homo sapiens
0.0033
-
NAD+ reduction of NAD+, formaldehyde dehydrogenase Homo sapiens
0.0048
-
S-nitrosoglutathione reduction of S-nitrosoglutathione, formaldehyde dehydrogenase Homo sapiens
0.011
-
NADH oxidation of NADH, R368L mutant Homo sapiens
0.0144
-
NAD+ reduction of NAD+, R368L mutant Homo sapiens
0.038
-
S-hydroxymethylglutathione oxidation of S-hydroxymethylglutathione, R368L mutant Homo sapiens
0.116
-
NAD+ reduction of NAD+, E67L mutant Homo sapiens
0.16
-
S-nitrosoglutathione reduction of S-nitrosoglutathione, R368L mutant Homo sapiens
2.65
-
S-hydroxymethylglutathione oxidation of S-hydroxymethylglutathione, E67L mutant Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
formaldehyde + NAD+ + H2O Homo sapiens
-
formate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DE52, Q-sepharose and Sephacryl S-100HR chromatographic steps Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formaldehyde + NAD+ + H2O
-
Homo sapiens formate + NADH + H+
-
?
S-hydroxymethylglutathione + NAD+ + H2O
-
Homo sapiens S-formylglutathione + NADH + H+
-
?
S-nitrosoglutathione + NADH + H2O
-
Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
homodimer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
FDH
-
Homo sapiens
formaldehyde dehydrogenase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
S-nitrosoglutathione Homo sapiens
30
-
S-hydroxymethylglutathione Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH
-
Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.148
-
dodecanoic acid formaldehyde dehydrogenase Homo sapiens
0.161
-
dodecanoic acid R368L mutant Homo sapiens
0.617
-
dodecanoic acid E67L mutant Homo sapiens