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Literature summary for 6.3.3.2 extracted from

  • Stover, P.; Huang, T.; Schirch, V.; Maras, B.; Valiante,S.; Barra, D.
    Purification and properties of rabbit liver 5,10-methenyltetrahydrofolate synthetase (1993), Chemistry and Biology of Pteridines and Folates (J. A. Ayling et al., eds., Plenum Press New York), , 723-726.
No PubMed abstract available

General Stability

General Stability Organism
stabilized by non-ionic detergent Tween 20 Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0005
-
5-formyltetrahydrofolate
-
Oryctolagus cuniculus
0.3
-
ATP
-
Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Oryctolagus cuniculus 5829
-
mitochondrion small amounts Oryctolagus cuniculus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ as effective as Mg2+ Oryctolagus cuniculus
Co2+ as effective as Mg2+ Oryctolagus cuniculus
Mg2+ required in equivalent concentration with ATP, its only role is to form a complex with ATP Oryctolagus cuniculus
Mn2+ as effective as Mg2+ Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 5-formyltetrahydrofolate Oryctolagus cuniculus it is proposed that methenyltetrahydrofolate synthetase is a salvage enzyme which converts the nonenzymatically formed and nonmetabolically active 5-formyltetrahydropteroyl-(Glu)n back into the one-carbon donor folate pool. It is also possible that methenyltetrahydrofolate synthetase is part of a regulation system in the cell in which its substrate 5-formyl-tetrahydropteroyl-(Glu)n plays a role as a regulator of one-carbon metabolism by inhibiting other folate requiring enzymes ?
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate random sequential mechanism Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oryctolagus cuniculus
-

Storage Stability

Storage Stability Organism
-70°C, 0.1% Tween 20, stable for a long time Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-formyltetrahydrofolate i.e. leucovorin, ir Oryctolagus cuniculus ADP + phosphate + 5,10-methylenetetrahydrofolate
-
?
ATP + 5-formyltetrahydrofolate ATP in form of MgATP2- Oryctolagus cuniculus ADP + phosphate + 5,10-methenyltetrahydrofolate
-
?
ATP + 5-formyltetrahydrofolate it is proposed that methenyltetrahydrofolate synthetase is a salvage enzyme which converts the nonenzymatically formed and nonmetabolically active 5-formyltetrahydropteroyl-(Glu)n back into the one-carbon donor folate pool. It is also possible that methenyltetrahydrofolate synthetase is part of a regulation system in the cell in which its substrate 5-formyl-tetrahydropteroyl-(Glu)n plays a role as a regulator of one-carbon metabolism by inhibiting other folate requiring enzymes Oryctolagus cuniculus ?
-
?
CTP + 5-formyltetrahydrofolate as effective as ATP Oryctolagus cuniculus CDP + phosphate + 5,10-methylenetetrahydrofolate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Oryctolagus cuniculus