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1.5.98.1: methylenetetrahydromethanopterin dehydrogenase

This is an abbreviated version!
For detailed information about methylenetetrahydromethanopterin dehydrogenase, go to the full flat file.

Word Map on EC 1.5.98.1

Reaction

5,10-methylenetetrahydromethanopterin
+
oxidized coenzyme F420
 +
H+
=
5,10-methenyltetrahydromethanopterin
 +
reduced coenzyme F420

Synonyms

CBH37899, Coenzyme F420 dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase, coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase, coenzyme-F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase, Dehydrogenase, methylenetetrahydromethanopterin, EC 1.5.99.9, F420-dependent H4MPT dehydrogenase, F420-dependent methylene-tetrahydromethanopterin dehydrogenase, F420-dependent methylenetetrahydromethanopterin dehydrogenase, F420H2-dependent methylenetetrahydromethanopterin dehydrogenase, Methylene tetrahydromethanopterin:coenzyme F420 oxidoreductase, methylene-H(4)MPT dehydrogenase, Methylene-H4MPT:coenzyme F420 oxidoreductase, MTD, N5,N10-Methylenetetrahydromethanopterin dehydrogenase

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.98 With other, known, physiological acceptors
                1.5.98.1 methylenetetrahydromethanopterin dehydrogenase

Crystallization

Crystallization on EC 1.5.98.1 - methylenetetrahydromethanopterin dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization trials are performed with the hanging drop vapor diffusion method using a sparse matrix crystallization kit under anaerobic and red light conditions, determination the structures of the Mtd-5,10-methylenetetrahydromethanopterin-, Mtd-5,10-methenyltetrahydromethanopterin- and the Mtd-5,10-methenyltetrahydromethanopterin-F420H2 complexes at 2.1, 2.0, and 1.8 A resolution, both substrate and cofactor bind in a face to face arrangement to an active site cleft, thereby ensuring a direct hydride transfer between their C14a and C5 atoms
purified recombinant selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 0.001 ml protein solution containing 12 mg/ml enzyme and 10 mM MOPS-KOH, pH 7.0, mixed with 0.001 ml reservoir solution containing 13% v/v 2-methyl-2,4-pentanediol, 0.1 M sodium phosphate, pH 8.0, and 0.2 M magnesium acetate, X-ray diffraction structure determination and analysis at 1.54 A resolution by single wavelength anomalous dispersion method, or at 2.4 A resolution by multiwavelength anomalous dispersion method
-
selenomethionine-labeled enzyme: X-ray diffraction structure determination and analysis at 1.54 A resolution, atomic displacement B factor pattern, native enzyme: X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution, the native enzyme shows a crystallographic superstructure of the selenomethionine-labeled enzyme
-
the selenomethionine-labelled form of the enzyme is structurally characterized at 1.54 A resolution
hanging drop vapour diffusion method, crystal structure of the enzyme in complex with cytochrome F420 at 2.6 A resolution
-