Literature summary extracted from
Gladyshev, V.N.; Boyington, J.C.; Khangulov, S.V.; Grahame, D.A.; Stadtman, T.C.; Sun, P.D.
Characterization of crystalline formate dehydrogenase H from Escherichia coli (1996), J. Biol. Chem., 271, 8095-8100.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.17.98.4 |
crystals diffract to 2.6 A resolution and belong to a space group of P4(1)2(1)2 or P4(3)2(1)2 with unit cell dimensions a = b = 146.1 A and c = 82.7 A. There is one monomer of FDH per crystallographic asymmetric unit. Similar diffraction quality crystals of oxidized FDH can be obtained by oxidation of crystals of formate-reduced enzyme with benzyl viologen. Mo(IV)- and the reduced FeS cluster containing form of the enzyme was crystallized and this can be converted into Mo(VI)- and oxidized FeS cluster form upon oxidation |
Escherichia coli |
General Stability
EC Number |
General Stability |
Organism |
---|
1.17.98.4 |
enzyme in dilute solutions (30 mg/ml) is rapidly inactivated at basic pH or in the presence of formate under anaerobic conditions, but at higher enzyme concentrations (3 mg/ml) the enzyme is relatively stable |
Escherichia coli |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.17.98.4 |
Fe |
Mo(IV)- and the reduced FeS cluster-containing form of the enzyme is crystallized and this can be converted into Mo(VI)- and oxidized FeS cluster form upon oxidation |
Escherichia coli |
|
1.17.98.4 |
Mo |
Mo(IV)- and the reduced FeS cluster-containing form of the enzyme is crystallized and this can be converted into Mo(VI)- and oxidized FeS cluster form upon oxidation |
Escherichia coli |
|
1.17.98.4 |
Se |
selenocysteine-containing enzyme. The molybdenum-coordinated selenocysteine is essential for catalytic activity of the native enzyme |
Escherichia coli |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.17.98.4 |
80000 |
- |
gel filtration |
Escherichia coli |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.17.98.4 |
Escherichia coli |
- |
- |
- |
Oxidation Stability
EC Number |
Oxidation Stability |
Organism |
---|
1.17.98.4 |
the formate-reduced enzyme is extremely sensitive to air inactivation |
Escherichia coli |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.17.98.4 |
- |
Escherichia coli |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.17.98.4 |
formate + benzyl viologen |
- |
Escherichia coli |
CO2 + reduced benzyl viologen |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.17.98.4 |
? |
x * 80000, SDS-PAGE |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.17.98.4 |
formate dehydrogenase H |
- |
Escherichia coli |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.17.98.4 |
8 |
- |
- |
Escherichia coli |
pH Stability
EC Number |
pH Stability |
pH Stability Maximum |
Comment |
Organism |
---|
1.17.98.4 |
6 |
- |
maximum stability |
Escherichia coli |