Any feedback?
Information on EC 3.5.4.9 - methenyltetrahydrofolate cyclohydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07245
for references in articles please use BRENDA:EC3.5.4.9Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.4.9 methenyltetrahydrofolate cyclohydrolaseIUBMB Comments
In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
Specify your search results
Word Map
- 3.5.4.9
- gtp
- purine
-
one-carbon
- guanosine
- tetrahydrobiopterin
-
trifunctional
- bh4
- 5,10-methylenetetrahydrofolate
- mthfd1
- 10-formyltetrahydrofolate
- aicar
-
c1-tetrahydrofolate
- 5-aminoimidazole-4-carboxamide
-
folate-dependent
-
10-formyl-thf
-
c1-thf
-
transformylase
-
6.3.4.3
- sepiapterin
-
formyltransferase
- dihydroneopterin
-
dopa-responsive
-
5,10-methylene-thf
- gtpch1
- 2,4-diamino-6-hydroxypyrimidine
-
folate-mediated
- biopterins
- drug development
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mthfd2, cyclohydrolase, methenyltetrahydrofolate cyclohydrolase, 5,10-methenyltetrahydrofolate cyclohydrolase, mthfd2l, 5,10-methenyl-thf cyclohydrolase, methylenetetrahydrofolate dehydrogenase/cyclohydrolase, nad-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase, dhch1, methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-methenyl-H4folate cyclohydrolase
-
-
-
-
Citrovorum factor cyclodehydrase
-
-
-
-
cyclohydrolase
-
-
-
-
formyl-methenyl-methylenetetrahydrofolate synthetase (combined)
-
-
-
-
methenyl-THF cyclohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing)
In eukaryotes, the enzyme occurs as a trifunctional enzyme that also has methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes, it occurs as a bifunctional enzyme that also has dehydrogenase (EC 1.5.1.5) activity or formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
CAS REGISTRY NUMBER
COMMENTARY
9027-97-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyl-tetrahydrofolate + H2O
10-formyltetrahydrofolate + H+
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
5,10-methenyl-tetrahydrofolate + H2O
10-formyltetrahydrofolate + H+
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
-
-
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methenyl-tetrahydrofolate + H2O
10-formyltetrahydrofolate + H+
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
5,10-methenyl-tetrahydrofolate + H2O
10-formyltetrahydrofolate + H+
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
-
r
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
-
-
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paukert, J.L.; Rabinowitz, J.C.
Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): a multifunctional protein in eukaryotic folate metabolism
Methods Enzymol.
66
616-626
1980
Saccharomyces cerevisiae, Ovis aries, Sus scrofa
Ljungdahl, L.G.; Clark, J.E.
Purification of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum
Methods Enzymol.
122
385-391
1986
Acetobacterium woodii, Saccharomyces cerevisiae, Clostridium formicaceticum, Moorella thermoacetica, Moorella thermoautotrophica, Escherichia coli
Clark, J.E.; Ljungdahl, L.G.
Purification and properties of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum
J. Biol. Chem.
257
3833-3836
1982
Acetobacterium woodii, Clostridium formicaceticum, Escherichia coli, Gallus gallus, Gottschalkia acidurici, Moorella thermoacetica, Ovis aries, Saccharomyces cerevisiae, Sus scrofa
Cohen, L.; MacKenzie, R.E.
Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from porcine liver. Interaction between the dehydrogenase and cyclohydrolase activities of the multifunctional enzyme
Biochim. Biophys. Acta
522
311-317
1978
Ovis aries, Saccharomyces cerevisiae, Sus scrofa
D'Ari, L.; Rabinowitz, J.C.
Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli
J. Biol. Chem.
266
23953-23958
1991
Clostridium cylindrosporum, Columba sp., Escherichia coli, Escherichia coli BE, Gallus gallus, Homo sapiens, Moorella thermoacetica, Mus musculus, Oryctolagus cuniculus, Ovis aries, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa
Tremblay, G.B.; Mejia, N.R.; MacKenzie, R.E.
The NADP-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase is not expressed in Spodoptera frugiperda cells
J. Biol. Chem.
267
8281-8285
1992
Rattus norvegicus, Saccharomyces cerevisiae, Spodoptera frugiperda, Spodoptera frugiperda Sf9
Pelletier, J.N.; MacKenzie, R.E.
Binding to the 2',5'-ADP subsite stimulates cyclohydrolase activity of human NADP+-dependent methylenetetrahydrofolate dehydrogenase/cyclohydrolase
Biochemistry
33
1900-1906
1994
Saccharomyces cerevisiae, Homo sapiens, Sus scrofa
Pawelek, P.D.; MacKenzie, R.E.
Methylenetetrahydrofolate dehydrogenase-cyclohydrolase from Photobacterium phosphoreum shares properties with a mammalian mitochondrial homologue
Biochim. Biophys. Acta
1296
47-54
1996
Acetobacterium woodii, Clostridium formicaceticum, Drosophila melanogaster, Escherichia coli, Homo sapiens, Mus musculus, Photobacterium phosphoreum, Rattus norvegicus, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium, Spodoptera frugiperda, Spodoptera frugiperda Sf9
Cheung, E.; D'Ari, L.; Rabinowitz, J.C.; Dyer, D.H.; Huang, J.Y.; Stoddard, B.L.
Purification, crystallization, and preliminary X-ray studies of a bifunctional 5,10-methenyl/methylene tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli
Proteins
27
322-324
1997
Saccharomyces cerevisiae, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus, Escherichia coli BE
Pawelek, P.D.; MacKenzie, R.E.
Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes
Biochemistry
37
1109-1115
1998
Homo sapiens, Mus musculus, Photobacterium phosphoreum, Saccharomyces cerevisiae, Sus scrofa
EXTERNAL LINKS (specific for EC-Number 3.5.4.9)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
