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Literature summary for 1.17.98.4 extracted from

  • Axley, M.J.; Böck, A.; Stadtman, T.C.
    Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium (1991), Proc. Natl. Acad. Sci. USA, 88, 8450-8454.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.98.4

Protein Variants

Protein Variants Comment Organism
additional information mutant form of the enzyme in which cysteine replaces selenocysteine. The mutant and wild-type enzymes display similar pH dependencies with respect to activity and stability, although the mutant enzyme profiles are slightly shifted to more alkaline pH. The mutant enzyme binds formate with greater affinity than does the wild-type enzyme, as shown by reduced values of Km and Kd. The mutant enzyme has a turnover number which is more than two orders of magnitude lower than that of the native selenium-containing enzyme. The lower turnover number results from a diminished reaction rate for the initial step of the overall reaction Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide iodoacetamide-dependent loss of activity occurrs only when formate is present Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
9
-
 formate pH 7.5, 24°C, mutant form of the enzyme in which cysteine replaces selenocysteine Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Se formate dehydrogenase H contains selenocysteine as an integral amino acid. Selenium of formate dehydrogenase H is directly involved in formate oxidation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formate + benzyl viologen ping-pong bi-bi kinetic mechanism Escherichia coli CO2 + reduced benzyl viologen
-
 ?

Synonyms

Synonyms Comment Organism
formate dehydrogenase H
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9
-
 formate pH 7.5, 24°C, mutant form of the enzyme in which cysteine replaces selenocysteine Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.7 pH 6.5: about 40% of maximal activity, pH 9.7: about 40% of maximal activity Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.8
-
 room temperature, 20 h, about 45% loss of activity Escherichia coli
5.3 6.4 room temperature, 20 h, stable Escherichia coli
7
-
 room temperature, 20 h, about 60% loss of activity Escherichia coli