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Literature summary for 1.5.1.6 extracted from

  • Chang, W.N.; Lin, H.C.; Fu, T.F.
    Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties (2010), Protein Expr. Purif., 72, 217-222.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli and Pichia pastoris Danio rerio

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0127
-
10-formyltetrahydrofolate 30°C, pH not specified in the publication, recombinant N-terminal domain Danio rerio
0.0156
-
10-formyltetrahydrofolate 30°C, pH not specified in the publication, full-length recombinant enzyme Danio rerio

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
4 * 100000, calculated Danio rerio
400000
-
gel fitlration Danio rerio

Organism

Organism UniProt Comment Textmining
Danio rerio E3NZ06
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Danio rerio

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.04
-
30°C, pH not specified in the publication, recombinant enzyme expressed in Pichia pastoris Danio rerio

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
10-formyltetrahydrofolate + NADP+ + H2O
-
Danio rerio tetrahydrofolate + CO2 + NADPH + H+
-
?
additional information enzyme does not catalyze the oxidation of 10-formyltetrahydrofolate or propanal Danio rerio ?
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 100000, calculated Danio rerio

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
97
-
10-formyltetrahydrofolate 30°C, pH not specified in the publication, full-length recombinant enzyme Danio rerio