Literature summary for 1.17.98.4 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

General Stability	Organism
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

Metals/Ions	Comment	Organism
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
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
Se	selenocysteine-containing enzyme. The molybdenum-coordinated selenocysteine is essential for catalytic activity of the native enzyme	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
80000	-	gel filtration	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Oxidation Stability

Oxidation Stability	Organism
the formate-reduced enzyme is extremely sensitive to air inactivation	Escherichia coli

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
formate + benzyl viologen	-	Escherichia coli	CO2 + reduced benzyl viologen	-	?

Subunits

Subunits	Comment	Organism
?	x * 80000, SDS-PAGE	Escherichia coli

Synonyms

Synonyms	Comment	Organism
formate dehydrogenase H	-	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	-	Escherichia coli

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
6	-	maximum stability	Escherichia coli