EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.5.1.77 | DL-5-(p-Hydroxyphenyl)hydantoin + H2O |
- |
Blastobacter sp. |
? |
- |
? |
| 3.5.1.77 | more |
strictly D-specific |
Agrobacterium sp. |
? |
- |
? |
| 3.5.1.77 | more |
no activity with N-acetyl-D-amino acids or N-carbamoyl-L-amino acids as substrate |
Agrobacterium tumefaciens |
? |
- |
? |
| 3.5.1.77 | more |
the enzyme does not hydrolyze beta-ureidopropionate |
Blastobacter sp. |
? |
- |
? |
| 3.5.1.77 | more |
D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer |
Agrobacterium sp. |
? |
- |
? |
| 3.5.1.77 | more |
strict specificity towards N-carbamoyl-D-amino acids, no activity with N-carbamoyl-L-amino acids |
Ensifer adhaerens |
? |
- |
? |
| 3.5.1.77 | more |
modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview |
Bradyrhizobium japonicum |
? |
- |
- |
| 3.5.1.77 | more |
the enantioselective D-carbamoylase (AcHyuC) from Arthrobacter crystallopoietes is much more compatible with hydantoinase process than other reported D-N-carbamoylases. AcHyuC has a substrate preference for aromatic carbamoyl-compounds. No activity with N-carbamoyl-DL-2-chlorophenylglycine, N-carbamoyl-DL-methionine, N-carbamoyl-DL-leucine, and N-carbamoyl-DL-isoleucine |
Arthrobacter crystallopoietes |
? |
- |
- |
| 3.5.1.77 | more |
modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview |
Bradyrhizobium japonicum CPAC 15 |
? |
- |
- |
| 3.5.1.77 | more |
the enantioselective D-carbamoylase (AcHyuC) from Arthrobacter crystallopoietes is much more compatible with hydantoinase process than other reported D-N-carbamoylases. AcHyuC has a substrate preference for aromatic carbamoyl-compounds. No activity with N-carbamoyl-DL-2-chlorophenylglycine, N-carbamoyl-DL-methionine, N-carbamoyl-DL-leucine, and N-carbamoyl-DL-isoleucine |
Arthrobacter crystallopoietes CGMCC1.1926 |
? |
- |
- |
