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Literature summary extracted from

  • Schirch, D.; Villar, E.; Maras, B.; Barra, D.; Schirch, V.
    Domain structure and function of 10-formyltetrahydrofolate dehydrogenase (1994), J. Biol. Chem., 269, 24728-24735.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.5.1.6 NADPH activates Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.6 chymotrypsin cleavage between the two domains, inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase and aldehyde dehydrogenase activity Oryctolagus cuniculus
1.5.1.6 Subtilisin cleavage between the two domains, inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase and aldehyde dehydrogenase activity Oryctolagus cuniculus
1.5.1.6 tetrahydrofolate
-
 Oryctolagus cuniculus
1.5.1.6 Trypsin cleavage between the two domains, inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase and aldehyde dehydrogenase activity Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.6 0.001
-
 NADP+
-
 Oryctolagus cuniculus
1.5.1.6 0.013
-
 10-formyltetrahydrofolate
-
 Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.6 99000
-
 4 * 99000, SDS-PAGE Oryctolagus cuniculus
1.5.1.6 440000
-
 gel filtration Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O Oryctolagus cuniculus regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate in the cell in response to yet unknown aldehyde and thiol metabolites tetrahydrofolate + CO2 + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.6 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.6
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.6 liver
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.6 additional information
-
-
 Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
1.5.1.6 -20°C, 20% glycerol, several months, stable Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O structure of enzyme domains and of catalytic centers Oryctolagus cuniculus tetrahydrofolate + CO2 + NADPH + H+ high affinity for tetrahydrofolate ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O enzyme requires Cys-707 to form a thiohemiacetal with the formyl group of 10-formyltetrahydrofolate Oryctolagus cuniculus tetrahydrofolate + CO2 + NADPH + H+ high affinity for tetrahydrofolate ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O enzyme binds one molecule of tetrahydrofolate and two molecules of NADP+ per tetramer, tetrahydrofolate and NADP+ bind to separate domains, higher affinity for NADP+ at lower enzyme concentrations Oryctolagus cuniculus tetrahydrofolate + CO2 + NADPH + H+ high affinity for tetrahydrofolate ?
1.5.1.6 10-formyltetrahydrofolate + NADP+ + H2O regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate in the cell in response to yet unknown aldehyde and thiol metabolites Oryctolagus cuniculus tetrahydrofolate + CO2 + NADPH + H+
-
 ?
1.5.1.6 additional information enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate Oryctolagus cuniculus ?
-
 ?
1.5.1.6 additional information enzyme consists of two independent folded domains connected by a linker sequence: a 32 kDa N-terminal domain with 10-formyltetrahydrofolate binding site shows hydrolase activity and a 63 kDa C-terminal domain with NADP+ binding site and Cys-707 shows aldehyde dehydrogenase activity, native structure of enzyme is necessary for 10-formyltetrahydrofolate dehydrogenase activity Oryctolagus cuniculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.6 homotetramer 4 * 99000, SDS-PAGE Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.6 30
-
 assay at Oryctolagus cuniculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.6 0.967
-
 10-formyltetrahydrofolate
-
 Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.6 8
-
 broad pH-maximum at pH 8.0 Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.6 10-formyltetrahydrofolate 10-formyltetrahydrofolate Oryctolagus cuniculus
1.5.1.6 NADP+ NADP+-dependent Oryctolagus cuniculus
1.5.1.6 tetrahydrofolate
-
 Oryctolagus cuniculus