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Information on EC 3.5.4.9 - methenyltetrahydrofolate cyclohydrolase and Organism(s) Escherichia coli and UniProt Accession P24186

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IUBMB 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.
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Escherichia coli
UNIPROT: P24186
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
mthfd2, cyclohydrolase, methenyltetrahydrofolate cyclohydrolase, 5,10-methenyltetrahydrofolate cyclohydrolase, mthfd2l, 5,10-methenyl-thf cyclohydrolase, nad-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase, methylenetetrahydrofolate dehydrogenase/cyclohydrolase, dhch1, methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-methenyl-H4folate cyclohydrolase
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-
-
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Citrovorum factor cyclodehydrase
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-
-
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cyclohydrolase
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-
-
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formyl-methenyl-methylenetetrahydrofolate synthetase (combined)
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-
-
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methenyl-THF cyclohydrolase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
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-
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-
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 hide
9027-97-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
5,10-methenyltetrahydrofolate + H2O
10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0045 - 0.04
5,10-methenyltetrahydrofolate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 57.4
5,10-methenyltetrahydrofolate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.67 - 2050
5,10-methenyltetrahydrofolate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
SDS-PAGE
31060
-
calculated from amino acid sequence
32000
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2 * 32000
35000
-
SDS-PAGE
70000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
small platelike crystals belong to body centered orthorhombic space group I222
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C58Y
kcat/Km for 5,10-methenyltetrahydrofolate is 13.2fold lower than wild-type value
D121A
kcat/Km for 5,10-methenyltetrahydrofolate is 2348fold lower than wild-type value
G122D
kcat/Km for 5,10-methenyltetrahydrofolate is 283fold lower than wild-type value
K54S
very low activity with 5,10-methenyltetrahydrofolate
Q98K
very low activity with 5,10-methenyltetrahydrofolate
R191E
kcat/Km for 5,10-methenyltetrahydrofolate is 1.3fold higher than wild-type value
Y50S
very low activity with 5,10-methenyltetrahydrofolate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C purified enzyme in 50% glycerol, 95% active after 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA fragment containing the bifunctional enzyme from Escherichia coli BE cloned and transformed into Escherichia coli BL21 for protein expression
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gene folD for bifunctional dehydrogenase/cyclohydrolase cloned and sequenced
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kirk, C.D.; Chen, L.; Imeson, H.C.; Cossins, E.A.
A 5,10-methylenetetrahydrofolate dehydrogenase: 5,10-methenyltetrahydrofolate cyclohydrolase protein from Pisum sativum
Phytochemistry
39
1309-1317
1995
Escherichia coli, Escherichia coli BE, Gottschalkia acidurici, Hordeum vulgare, Moorella thermoacetica, Neurospora sp., Pisum sativum, Spinacia oleracea, Triticum aestivum, Vicia faba, Zea mays
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Shen, B.W.; Dyer, D.H.; Huang, J.Y.; D'Ari, L.; Rabinowitz, J.; Stoddard, B.L.
The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase
Protein Sci.
8
1342-1349
1999
Escherichia coli
Manually annotated by BRENDA team
Sah, S.; Varshney, U.
Impact of mutating the key residues of a bifunctional 5,10-methylenetetrahydrofolate dehydrogenase-cyclohydrolase from Escherichia coli on its activities
Biochemistry
54
3504-3513
2015
Escherichia coli (P24186), Escherichia coli, Escherichia coli K12 (P24186)
Manually annotated by BRENDA team