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Literature summary extracted from

  • Faust, A.; Niefind, K.; Hummel, W.; Schomburg, D.
    The structure of a bacterial l-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation (2006), J. Mol. Biol., 367, 234-248.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.4.3.2 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(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.2
-
 Rhodococcus opacus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.3.2
-
 Rhodococcus opacus
1.4.3.2 as HgCl2-derivative, native protein and in complex with L-alanine, L-phenylalanine or o-aminobenzoate Rhodococcus opacus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.2 anthranilate
-
 Rhodococcus opacus

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.2 Rhodococcus opacus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.2
-
 Rhodococcus opacus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.4.3.2 an L-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2 hydride transfer mechanism Rhodococcus opacus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.2 L-alanine + H2O + O2
-
 Rhodococcus opacus 2-oxopropanoic acid + NH3 + H2O2
-
 ?
1.4.3.2 L-phenylalanine + H2O + O2
-
 Rhodococcus opacus phenylpyruvate + NH3 + H2O2
-
 ?
1.4.3.2 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

EC Number Subunits Comment Organism
1.4.3.2 homodimer high-resolution Rhodococcus opacus

Synonyms

EC Number Synonyms Comment Organism
1.4.3.2 LAAO
-
 Rhodococcus opacus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.2 FAD
-
 Rhodococcus opacus
1.4.3.2 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