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BRENDA support 5,10-methylenetetrahydromethanopterin reductase

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

Word Map on EC


oxidized coenzyme F420
reduced coenzyme F420


5,10-methylene-H4MPT reductase, coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase, EC, 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


     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.98 With other, known, physiological acceptors
       5,10-methylenetetrahydromethanopterin reductase

General Stability

General Stability on EC - 5,10-methylenetetrahydromethanopterin reductase

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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