1.5.98.2: 5,10-methylenetetrahydromethanopterin reductase

This is an abbreviated version!
For detailed information about 5,10-methylenetetrahydromethanopterin reductase, go to the full flat file.

Reaction

Synonyms

5,10-methylene-H4MPT reductase, coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase, EC 1.5.99.11, H(2)-dependent methylene-H(4)MPT dehydrogenase, H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase, H2-dependent methylenetetrahydromethanopterin dehydrogenase, Hmd, Mer, MK0524, MTBMA_c03270, N5,N10-methylenetetrahydromethanopterin reductase, N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent), N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase

ECTree

     1 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.98 With other, known, physiological acceptors

                1.5.98.2 5,10-methylenetetrahydromethanopterin reductase

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Results	in table
6	Activating Compound
1297	AA Sequence
1	CAS Registry Number
2	Cloned(Commentary)
1	Cofactor
2	Crystallization (Commentary)
12	General Information
4	General Stability
2	Inhibitors
9	KM Value [mM]
2	Localization
9	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
115	Organism
1	Oxidation Stability
8	Pathway
8	pH Optimum
9	Purification (Commentary)
2	Reaction
3	Reaction Type
27	Reference
4	Source Tissue
9	Specific Activity [micromol/min/mg]
27	Substrates and Products (Substrate)
10	Subunits
23	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
2	Temperature Stability [°C]
2	Turnover Number [1/s]

General Stability

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General Stability on EC 1.5.98.2 - 5,10-methylenetetrahydromethanopterin reductase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

efficiency of salts in protecting the reductase from inactivation decreased in the following order: K2HPO4, KCl, (NH4)2SO4, NH4Cl, Na2HPO4, NaCl

Methanopyrus kandleri

Q8TXY4

726826

is of less importance

Methanopyrus kandleri

Q8TXY4

726826

salt concentrations between 0.1 M and 1.5 M are required for maximal stability. Potassium salts are more effective than ammonium salts, and the latter more effective than sodium salts in stabilizing the enzyme activity. The anion

Methanopyrus kandleri

Q8TXY4

726826

thermostability of the reductase is very low in the absence of salts. In their presence, however, the reductase is highly thermostable. Salt concentrations between 0.1 M and 1.5 M are required for maximal stability. Potassium salts prove more effective than ammonium salts

Methanopyrus kandleri

Q8TXY4

726826