Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co3+ | a Co-type NHase, Co3+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113 | Pseudonocardia thermophila |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudonocardia thermophila | Q7SID2 | - |
- |
Pseudonocardia thermophila JCM 3095 | Q7SID2 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an aliphatic amide = a nitrile + H2O | modeling of the catalytic mechanism of nitrile hydratase by semi-empirical quantum mechanical calculation using the enzyme crystal structure, PDB code 1IRE, overview. Active site activation is the first step of NHase catalysis, in which the Co2+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113. Then the oxygen atom in the Co-OH attacks the C atom in the -CN triple bond of acrylonitrile, forming a precursor of acrylamide, proton rearrangement happens transforming the precursor into the final product of acrylamide, under the assistance of the hydrogen atom in the -OH group of alpha-Ser112 | Pseudonocardia thermophila |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acrylonitrile + H2O | analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview | Pseudonocardia thermophila | acrylamide | - |
? | |
acrylonitrile + H2O | analysis of the structure model of the enzyme-substrate complex and catalytic mechanism, overview | Pseudonocardia thermophila JCM 3095 | acrylamide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Co-type NHase | - |
Pseudonocardia thermophila |
NHase | - |
Pseudonocardia thermophila |