Literature summary 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.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.17.98.4 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.17.98.4 |
iodoacetamide |
iodoacetamide-dependent loss of activity occurrs only when formate is present |
Escherichia coli |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.17.98.4 |
9 |
- |
formate |
pH 7.5, 24°C, mutant form of the enzyme in which cysteine replaces selenocysteine |
Escherichia coli |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.17.98.4 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
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 |
ping-pong bi-bi kinetic mechanism |
Escherichia coli |
CO2 + reduced benzyl viologen |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.17.98.4 |
formate dehydrogenase H |
- |
Escherichia coli |
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
1.17.98.4 |
9 |
- |
formate |
pH 7.5, 24°C, mutant form of the enzyme in which cysteine replaces selenocysteine |
Escherichia coli |
|
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.17.98.4 |
7.5 |
8.5 |
- |
Escherichia coli |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
1.17.98.4 |
6.5 |
9.7 |
pH 6.5: about 40% of maximal activity, pH 9.7: about 40% of maximal activity |
Escherichia coli |
pH Stability
EC Number |
pH Stability |
pH Stability Maximum |
Comment |
Organism |
---|
1.17.98.4 |
4.8 |
- |
room temperature, 20 h, about 45% loss of activity |
Escherichia coli |
1.17.98.4 |
5.3 |
6.4 |
room temperature, 20 h, stable |
Escherichia coli |
1.17.98.4 |
7 |
- |
room temperature, 20 h, about 60% loss of activity |
Escherichia coli |