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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.

Wordmap for 1.5.98.2

Word Map on EC 1.5.98.2 Wordmap for 1.5.98.2

Reaction

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5-methyltetrahydromethanopterin
+
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oxidized coenzyme F420
=
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5,10-methylenetetrahydromethanopterin
 +
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reduced coenzyme F420

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
                EC 1.5.98.21.5.98.2 5,10-methylenetetrahydromethanopterin reductase

General Stability

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

for references in articles please use BRENDA:EC1.5.98.2

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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
is of less importance
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
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