Application | Comment | Organism |
---|---|---|
synthesis | useful for acrylamide production | Rhodococcus sp. |
synthesis | industrial production of nicotinamide | Rhodococcus sp. |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Rhodococcus sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | non-heme ferric iron in the catalytic center | Rhodococcus sp. | |
Fe2+ | 0.01 mM ferric citrate increases the enzyme activity | Rhodococcus sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
23000 | - |
x * 23000, alpha + x * 23000, beta | Rhodococcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | two cysteine ligands, alphaCys112 and alphaCys114, are oxidized to a cysteine sulfinic acid and a cysteine sulfenic acid, respectively. Cysteine sulfinic acid in 112 is responsible for the catalytic activity. First metalloprotein having posttranslationally modified cysteine ligands | Rhodococcus sp. |
Purification (Comment) | Organism |
---|---|
anion exchange chromatography and gel filtration, recombinant enzyme | Rhodococcus sp. |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an aliphatic amide = a nitrile + H2O | the iron-type enzyme is photoreactive, it loses the catalytic activity through aerobic incubation in the dark and recovers it by light irradiation | Rhodococcus sp. |
Subunits | Comment | Organism |
---|---|---|
? | x * 23000, alpha + x * 23000, beta | Rhodococcus sp. |