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Information on EC 3.5.4.9 - methenyltetrahydrofolate cyclohydrolase and Organism(s) Thermoplasma acidophilum and UniProt Accession Q05213

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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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Thermoplasma acidophilum
UNIPROT: Q05213
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The taxonomic range for the selected organisms is: Thermoplasma acidophilum
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase
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methylenetetrahydrofolate dehydrogenase/cyclohydrolase
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5,10-methenyl-H4folate cyclohydrolase
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Citrovorum factor cyclodehydrase
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cyclohydrolase
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formyl-methenyl-methylenetetrahydrofolate synthetase (combined)
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methenyl-THF cyclohydrolase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
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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
additional information
?
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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
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the TaMTHFDC structure is a dimer with a polar interface, as well as a NADP+ binding site that shows minor conformational change, structure comparisons, overview
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme free and in complex with NADP+, sitting drop vapour diffusion method, mixing of 1.8 mg/ml protein in 10 mM Tris-HCl, 50 mM KCl, and 2 mM DTT, with 18% PEG 4000, 400 mM NaCl, and 100 mM Tris-HCl, pH 8.0 at 22°C, 5 mM NADP+ is added during crystallization, X-ray diffraction structure determination and analysis, molecular replacement
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally 6-His-tagged MTHFDC from Escherichia coli strain BL21(DE3) by heat-treatment, nickel affinity chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the N-terminally 6-His-tagged MTHFDC in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, W.H.; Sung, M.W.; Kim, J.H.; Kim, Y.K.; Han, A.; Hwang, K.Y.
Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum
Biochem. Biophys. Res. Commun.
406
459-463
2011
Thermoplasma acidophilum (Q05213), Thermoplasma acidophilum
Manually annotated by BRENDA team