Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is activated by absorption of photons of wavelength of about 630 nm | Rhodococcus sp. |
Application | Comment | Organism |
---|---|---|
synthesis | nitrile hydratase is an enzyme used in the industrial biotechnological production of acrylamide | Rhodococcus sp. |
Crystallization (Comment) | Organism |
---|---|
analysis of the crystal structure of inactive NHase, overview | Rhodococcus sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NO | Substantial structural changes upon NO ligand binding to the iron center, indicating that some mechanical signals are sent upon NO photodissociation, determination NO diffusion paths in NHase, overview | Rhodococcus sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co3+ | contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta | Rhodococcus sp. | |
Fe3+ | contains nonheme iron or noncorrin cobalt, the ion is bound buried in the protein core at the interface of two domains alpha and beta, photosensitivity of the Fe-type NHase | Rhodococcus sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acrylonitrile + H2O | Rhodococcus sp. | - |
acrylamide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an aliphatic amide = a nitrile + H2O | water dynamics and catalytic mechanism, a water molecule bound to the metal ion directly attacks the nitrile carbon, overview. Dynamics of the active site channel, NO diffusion paths, and water molecules positions are key components in the functioning of this important industrial enzyme | Rhodococcus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acrylonitrile + H2O | - |
Rhodococcus sp. | acrylamide | - |
? | |
additional information | hydrogen bonds between betaArg56 and alphaCys114 sulfenic acid are important to maintain the enzymatic activity, molecular dynamics simulations determining the differences in the dynamics of lightactive and dark-inactive forms of NHase, overview | Rhodococcus sp. | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NHase | - |
Rhodococcus sp. |