spacer
View the latest EBI news stories and important announcements...
more

spacer
Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1c0k

E.C. nameD-amino-acid oxidase
SpeciesRhodosporidium toruloides (Rhodotorula gracilis)
E.C. Number (IntEnz) 1.4.3.3
CSA Homologues of 1c0kThere are 56 Homologs
CSA Entries With UniProtID P80324
CSA Entries With EC Number 1.4.3.3
PDBe Entry 1c0k
PDBSum Entry 1c0k
MACiE Entry M0110

Literature Report

IntroductionD amino acid oxidase acts to oxidise D amino acids to their imino counterparts, using FAD as a cofactor. This has been found to play an important role in the degradation of certain neurotransmitters such as D serine in mammals, but the enzyme is also found in other eukaryotes and its function has not been fully characterised. It shows mechanistic correlation with other enzymes able to oxidise amino groups.
MechansimThe mechanism of the reaction is through direct hydride transfer from the alpha carbon of the amino acid to the N5 of the FAD, with concomitant deprotonation of the alpha amino group by Ser 335's side chain allowing orbital overlap between the nitrogen lone pair and the carbon's sigma* orbital to occur, resulting in the imine product. The transition state for this process is planar and stabilised by hydrogen bonding between the carbonyl of Ser 335 and the amino group.
Reaction

Catalytic Sites for 1c0k

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
SerA1335335macie:sideChainThe side chain acts as an acid base to mediate transfer of the proton from the alpha amino group to bulk water, whilst the carbonyl group stabilises the transition state.
SerA1335335macie:mainChainCarbonylThe side chain acts as an acid base to mediate transfer of the proton from the alpha amino group to bulk water, whilst the carbonyl group stabilises the transition state.

Literature References

Notes:
Umhau S
The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
Proc Natl Acad Sci U S A 2000 97 12463-12468
PubMed: 11070076
spacer
spacer