Inhibitors | Comment | Organism | Structure |
---|---|---|---|
iodoacetamide | inhibition is enhanced in the presence of formate | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | the enzyme may contain one 4Fe-4S cluster | Escherichia coli | |
Mo | contains bis-molybdopterin guanine dinucleotide | Escherichia coli | |
Se | selenocysteine is located at amino acid position 140 | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
formate + HycB | Escherichia coli | the hydrogenase 3 Fe-S subunit HycB may represent the electron transfer partner of FDH-H | CO2 + reduced HycB | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | FDH-H synthesis is optimal when Escherichia coli grows fermentatively | Escherichia coli | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
formate + benzyl viologen | FDH-H remains essentially unchanged when deuteroformate is used as a substrate | Escherichia coli | CO2 + reduced benzyl viologen | - |
? | |
formate + HycB | the hydrogenase 3 Fe-S subunit HycB may represent the electron transfer partner of FDH-H | Escherichia coli | CO2 + reduced HycB | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | hydrogenase 3 (Hyd-3) together with formate dehydrogenase H (FDH-H) forms part of the formate hydrogenlyase (FHL) complex | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
Fdh-H | hydrogenase 3 (Hyd-3) together with formate dehydrogenase H (FDH-H) forms part of the formate hydrogenlyase (FHL) complex | Escherichia coli |
formate hydrogenlyase | hydrogenase 3 (Hyd-3) together with formate dehydrogenase H (FDH-H) forms part of the formate hydrogenlyase (FHL) complex | Escherichia coli |