Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.3.2 0.0005
-
 5-formyltetrahydrofolate
-
 Oryctolagus cuniculus
6.3.3.2 0.3
-
 ATP
-
 Oryctolagus cuniculus

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.3.2 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

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.3.2
-
 Oryctolagus cuniculus

Reaction

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

Source Tissue

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

Storage Stability

EC Number Storage Stability Organism
6.3.3.2 -70°C, 0.1% Tween 20, stable for a long time Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.3.2 ATP + 5-formyltetrahydrofolate i.e. leucovorin, ir Oryctolagus cuniculus ADP + phosphate + 5,10-methylenetetrahydrofolate
-
 ?
6.3.3.2 ATP + 5-formyltetrahydrofolate ATP in form of MgATP2- Oryctolagus cuniculus ADP + phosphate + 5,10-methenyltetrahydrofolate
-
 ?
6.3.3.2 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 ?
-
 ?
6.3.3.2 CTP + 5-formyltetrahydrofolate as effective as ATP Oryctolagus cuniculus CDP + phosphate + 5,10-methylenetetrahydrofolate
-
 ?

Turnover Number [1/s]

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