Application | Comment | Organism |
---|---|---|
additional information | a helical domain is exclusively responsible for the unusual dimerisation mode of the enzyme and is not found in other members of the family so far. Most groups present at the active site are involved in substrate recognition, binding and fixation, i.e. they direct the trajectory of the interacting orbitals. In this mode of catalysis orbital steering/interactions are the predominant factors for the chemical step(s). A mirrorsymmetrical relationship between the two substrate-binding sites of D and L-amino acid oxidases is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the residues in the active site | Rhodococcus opacus |
Cloned (Comment) | Organism |
---|---|
- |
Rhodococcus opacus |
Crystallization (Comment) | Organism |
---|---|
- |
Rhodococcus opacus |
as HgCl2-derivative, native protein and in complex with L-alanine, L-phenylalanine or o-aminobenzoate | Rhodococcus opacus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
anthranilate | - |
Rhodococcus opacus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus opacus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Rhodococcus opacus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an L-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2 | hydride transfer mechanism | Rhodococcus opacus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-alanine + H2O + O2 | - |
Rhodococcus opacus | 2-oxopropanoic acid + NH3 + H2O2 | - |
? | |
L-phenylalanine + H2O + O2 | - |
Rhodococcus opacus | phenylpyruvate + NH3 + H2O2 | - |
? | |
L-phenylalanine + H2O + O2 | hydride transfer as the mechanism of dehydrogenation. The substrate-binding domain of LAAO is made up of residues 52-128, 230-238 and 315-422. The substrate-binding domain has almost the same topology as the snake venom LAAO | Rhodococcus opacus | phenylpyruvate + NH3 + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | high-resolution | Rhodococcus opacus |
Synonyms | Comment | Organism |
---|---|---|
LAAO | - |
Rhodococcus opacus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Rhodococcus opacus | |
FAD | the whole cofactor is buried inside the protein and is not solvent accessible. The FAD-binding domain consists of three discontinuous regions of the structure: residues 4-51, 239-314 and 423-488. The main structural feature of this domain is a fivestranded beta-pleated sheet sandwiched between three alpha-helices and a four-stranded beta-pleated sheet. The FAD-binding domain corresponds to a general topology throughout the whole GR2-famil | Rhodococcus opacus |