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Literature summary for 3.5.4.9 extracted from

  • 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 (2011), Biochem. Biophys. Res. Commun., 406, 459-463.
    View publication on PubMed
Search for more literature for 3.5.4.9

Cloned(Commentary)

Cloned (Comment) Organism
expression of the N-terminally 6-His-tagged MTHFDC in Escherichia coli strain BL21(DE3) Thermoplasma acidophilum

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Thermoplasma acidophilum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermoplasma acidophilum the enzyme is a bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase, cf. EC 1.5.1.5 ?
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 ?

Organism

Organism UniProt Comment Textmining
Thermoplasma acidophilum Q05213
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally 6-His-tagged MTHFDC from Escherichia coli strain BL21(DE3) by heat-treatment, nickel affinity chromatography, and gel filtration Thermoplasma acidophilum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is a bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase, cf. EC 1.5.1.5 Thermoplasma acidophilum ?
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 ?
additional information tetrahydrofolate binding pocket structure analysis, residues 157-163 form a GXGXXXG motif and interact with the substrate, residues Asn157 and highly conserved Ser159 are important, overview Thermoplasma acidophilum ?
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 ?

Subunits

Subunits Comment Organism
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 Thermoplasma acidophilum
More structure of the TaMTHFDC-NADP+ complex dimer, overview Thermoplasma acidophilum

Synonyms

Synonyms Comment Organism
5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase
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 Thermoplasma acidophilum
methylenetetrahydrofolate dehydrogenase/cyclohydrolase
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 Thermoplasma acidophilum
MTHFDC
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 Thermoplasma acidophilum

General Information

General Information Comment Organism
additional information structure of the TaMTHFDC-NADP+ complex dimer, overview Thermoplasma acidophilum