Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.5 expressed in Escherichia coli BL21(DE3) cells Thermoplasma acidophilum
3.5.4.9 expression of the N-terminally 6-His-tagged MTHFDC in Escherichia coli strain BL21(DE3) Thermoplasma acidophilum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.5 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) Thermoplasma acidophilum
3.5.4.9 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.5 Thermoplasma acidophilum Q05213
-
-
3.5.4.9 Thermoplasma acidophilum Q05213
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.5 heat treatment, Ni-affinity column chromatography, and Superdex-200 gel filtration Thermoplasma acidophilum
3.5.4.9 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.5 5,10-methylenetetrahydrofolate + NADP+
-
Thermoplasma acidophilum 5,10-methenyltetrahydrofolate + NADPH + H+
-
?
3.5.4.9 additional information the enzyme is a bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase, cf. EC 1.5.1.5 Thermoplasma acidophilum ?
-
?
3.5.4.9 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 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.5.1.5 homodimer x-ray crystallography Thermoplasma acidophilum
3.5.4.9 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
3.5.4.9 More structure of the TaMTHFDC-NADP+ complex dimer, overview Thermoplasma acidophilum

Synonyms

EC Number Synonyms Comment Organism
1.5.1.5 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase bifunctional enzyme Thermoplasma acidophilum
1.5.1.5 MTHFDC
-
Thermoplasma acidophilum
3.5.4.9 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase
-
Thermoplasma acidophilum
3.5.4.9 methylenetetrahydrofolate dehydrogenase/cyclohydrolase
-
Thermoplasma acidophilum
3.5.4.9 MTHFDC
-
Thermoplasma acidophilum

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.5 NADP+
-
Thermoplasma acidophilum

General Information

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