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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1f8r

E.C. nameL-amino-acid oxidase
SpeciesCalloselasma rhodostoma ()
E.C. Number (IntEnz) 1.4.3.2
CSA Homologues of 1f8rThere are 34 Homologs
CSA Entries With UniProtID P81382
CSA Entries With EC Number 1.4.3.2
PDBe Entry 1f8r
PDBSum Entry 1f8r
MACiE Entry 1f8r

Literature Report

IntroductionL-aminoacid oxidase is a dimeric flavoprotein. it uses a non-covalently bound FAD cofactor in catalysing the stereospecific oxidative deamination of an L-amino acid substrate to an alpha ketoacid, forming ammonia and hydrogen peroxide. The enzyme shows a marked preference for hydrophobic amino acids including phenylalanine, tryptophan, tyrosine and leucine.
MechansimThe non-covalently bound FAD is first reduced to FADH2 with oxidation of the amino acid to an imino acid. Non-enzymatic hydrolysis at the imine centre leads to the elimination of ammonia and formation of an alpha-ketoacid.
The mechanism is thought to involve a base for the abstraction of a proton from the amino group of the substrate and subsequent transfer of a hydride from the alpha carbon to the N5 of the isoalloxazine ring of FAD to form the imino intermediate.
Reaction

Catalytic Sites for 1f8r

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA223241macie:sideChainThe residue is thought to act as a general base towards the zwitter-ionic form of the substrate, abstracting a proton from the amino group and so activating the substrate to transfer a hydride to the FAD cofactor.
LysA326344macie:sideChainThe residue acts to relay a proton to a structurally conserved water molecule, which is thought to assist peroxide formation from the flavin-hydroperoxy intermediate.

Literature References

Notes:
Pawelek PD
The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
EMBO J 2000 19 4204-4215
PubMed: 10944103
Moustafa IM
Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism.
J Mol Biol 2006 364 991-1002
PubMed: 17046020
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