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Enzymes

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Name ^help_outline H₂O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline L-serine Identifier CHEBI:33384 Charge 0 Formula C3H7NO3 InChIKey^help_outline MTCFGRXMJLQNBG-REOHCLBHSA-N SMILES^help_outline [NH3+][C@@H](CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 78 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline O₂ Identifier CHEBI:15379 (CAS: 7782-44-7) ^help_outline Charge 0 Formula O2 InChIKey^help_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILES^help_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,709 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline 3-hydroxypyruvate Identifier CHEBI:17180 (Beilstein: 3904014) ^help_outline Charge -1 Formula C3H3O4 InChIKey^help_outline HHDDCCUIIUWNGJ-UHFFFAOYSA-M SMILES^help_outline OCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O₂ Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) ^help_outline Charge 0 Formula H2O2 InChIKey^help_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILES^help_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 449 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline NH₄⁺ Identifier CHEBI:28938 (CAS: 14798-03-9) ^help_outline Charge 1 Formula H4N InChIKey^help_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILES^help_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 528 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:61344	RHEA:61345	RHEA:61346	RHEA:61347
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	1 proteins

Related reactions ^help_outline

More general form(s) of this reaction

RHEA:13781
an L-α-amino acid + H₂O + O₂ = a 2-oxocarboxylate + H₂O₂ + NH₄⁺

Publications

The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation.

Faust A., Niefind K., Hummel W., Schomburg D.

l-Amino acid oxidase from Rhodococcus opacus (roLAAO) is classified as a member of the GR(2)-family of flavin-dependent oxidoreductases according to a highly conserved sequence motif for the cofactor binding. The monomer of the homodimeric enzyme consists of three well-defined domains: the FAD-bin ... >> More

l-Amino acid oxidase from Rhodococcus opacus (roLAAO) is classified as a member of the GR(2)-family of flavin-dependent oxidoreductases according to a highly conserved sequence motif for the cofactor binding. The monomer of the homodimeric enzyme consists of three well-defined domains: the FAD-binding domain corresponding to a general topology throughout the whole GR(2)-family; a substrate-binding domain with almost the same topology as the snake venom LAAO and a helical domain exclusively responsible for the unusual dimerisation mode of the enzyme and not found in other members of the family so far. We describe here high-resolution structures of the binary complex of protein and cofactor as well as the ternary complexes of protein, cofactor and ligands. This structures in addition to the structural knowledge of snake venom LAAO and DAAO from yeast and pig kidney permit more insight into different steps in the reaction mechanism of this class of enzymes. There is strong evidence for hydride transfer as the mechanism of dehydrogenation. This mechanism appears to be uncommon in a sense that the chemical transformation can proceed efficiently without the involvement of amino acid functional groups. 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 mirror-symmetrical 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. These results are of general relevance for the mechanism of flavoproteins and lead to the proposal of a common dehydrogenation step in the mechanism for l and d-amino acid oxidases. << Less

J. Mol. Biol. 367:234-248(2007) [PubMed] [EuropePMC]

Comments

Published in: https://doi.org/10.1016/S0141-0229(02)00072-8 Geueke B., Hummel W. A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization. Enzyme Microb. Technol. 31:77-87 (2002)