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Information on EC 1.5.1.5 - methylenetetrahydrofolate dehydrogenase (NADP+) and Organism(s) Thermoplasma acidophilum and UniProt Accession Q05213

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IUBMB Comments
In eukaryotes, occurs as a trifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) and formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes occurs as a bifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase activity (EC 3.5.4.9).
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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
methylenetetrahydrofolate dehydrogenase, 5,10-methylenetetrahydrofolate dehydrogenase, mthfd2 protein, ch2-thf dehydrogenase, mthfd1 protein, mitochondrial methylenetetrahydrofolate dehydrogenase, methylenetetrahydrofolate dehydrogenase (nadp+ dependent), bmmthfd, n5,n10-methylenetetrahydrofolate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase
bifunctional enzyme
5,10-methylenetetrahydrofolate dehydrogenase
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5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase
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methylenetetrahydrofolate dehydrogenase
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N5,N10-methylenetetrahydrofolate dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:NADP+ oxidoreductase
In eukaryotes, occurs as a trifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) and formate---tetrahydrofolate ligase (EC 6.3.4.3) activity. In some prokaryotes occurs as a bifunctional enzyme also having methenyltetrahydrofolate cyclohydrolase activity (EC 3.5.4.9).
CAS REGISTRY NUMBER
COMMENTARY hide
9029-14-5
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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-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
show the reaction diagram
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?
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
show the reaction diagram
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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
5,10-methylenetetrahydrofolate + NADP+
5,10-methenyltetrahydrofolate + NADPH + H+
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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prefers NADP+ as a cofactor, rather than NAD+
NADP+
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prefers NADP+ as a cofactor, rather than NAD+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30600
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SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
monomer
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1 * 30600, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native form and as a NADP complex, hanging drop vapor diffusion method, at 22°C in 18% PEG 4000, 400 mM NaCl, and 100 mM Tris-HCl (pH 8.0)
hanging drop vapour diffusion method, in the presence of its cofactor NADP+, at 22°C using polyethylene glycol 4000 as a precipitant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heat treatment, Ni-affinity column chromatography, and Superdex-200 gel filtration
His-Trap affinity column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, J.H.; Sung, M.W.; Lee, E.H.; Nam, K.H.; Hwang, K.Y.
Crystallization and preliminary X-ray diffraction analysis of 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum DSM 1728
J. Microbiol. Biotechnol.
18
283-286
2008
Thermoplasma acidophilum
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team