D00037
type: Enzyme
cath: Rossmann fold
cath: D-Amino Acid Oxidase; Chain A, domain 2
ec: https://purl.uniprot.org/enzyme/1.4.3.3
uniprot: P00371
kegg enzyme: D-amino-acid oxidase
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Penicillin and cephalosporin biosynthesis
kegg pathway: Arginine and proline metabolism
kegg pathway: D-Arginine and D-ornithine metabolism
kegg cofactor: FAD
kegg substrate: D-Amino acid
kegg substrate: H2O
kegg substrate: O2
kegg product: 2-Oxo acid
kegg product: NH3
kegg product: H2O2
pdb: 1aa8A01
pdb: 1aa8B01
pdb: 1an9A01
pdb: 1an9B01
pdb: 1daoA01
pdb: 1daoB01
pdb: 1daoC01
pdb: 1daoD01
pdb: 1daoE01
pdb: 1daoF01
pdb: 1daoG01
pdb: 1daoH01
pdb: 1ddoA01
pdb: 1ddoB01
pdb: 1ddoC01
pdb: 1ddoD01
pdb: 1ddoE01
pdb: 1ddoF01
pdb: 1ddoG01
pdb: 1ddoH01
pdb: 1eviA01
pdb: 1eviB01
pdb: 1kifA01
pdb: 1kifB01
pdb: 1kifC01
pdb: 1kifD01
pdb: 1kifE01
pdb: 1kifF01
pdb: 1kifG01
pdb: 1kifH01
pdb: 1ve9A01
pdb: 1ve9B01
pdb: 1aa8A02
pdb: 1aa8B02
pdb: 1an9A02
pdb: 1an9B02
pdb: 1daoA02
pdb: 1daoB02
pdb: 1daoC02
pdb: 1daoD02
pdb: 1daoE02
pdb: 1daoF02
pdb: 1daoG02
pdb: 1daoH02
pdb: 1ddoA02
pdb: 1ddoB02
pdb: 1ddoC02
pdb: 1ddoD02
pdb: 1ddoE02
pdb: 1ddoF02
pdb: 1ddoG02
pdb: 1ddoH02
pdb: 1eviA02
pdb: 1eviB02
pdb: 1kifA02
pdb: 1kifB02
pdb: 1kifC02
pdb: 1kifD02
pdb: 1kifE02
pdb: 1kifF02
pdb: 1kifG02
pdb: 1kifH02
pdb: 1ve9A02

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

D-Amino Acid Oxidase; Chain A, domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.9.10
catalytic domain: index.html

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260

Penicillin and cephalosporin biosynthesis
type: KeggPathway
references: KEGG:MAP00311

Arginine and proline metabolism
type: KeggPathway
references: KEGG:MAP00330

D-Arginine and D-ornithine metabolism
type: KeggPathway
references: KEGG:MAP00472

FAD
type: KeggCofactor
references: KEGG:C00016
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide

D-Amino acid
type: KeggSubstrate
references: KEGG:C00405
compound type: amino acids

H2O
type: KeggSubstrate
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: H2O

O2
type: KeggSubstrate
references: KEGG:C00007
references: CHEBI:15379
references: CHEBI:26689
references: CHEBI:27140
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: others

2-Oxo acid
type: KeggProduct
references: KEGG:C00161
compound type: carbohydrate
compound type: carboxyl group

NH3
type: KeggProduct
references: KEGG:C00014
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: amine group
compound type: organic ion

H2O2
type: KeggProduct
references: KEGG:C00027
references: CHEBI:16240
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: others

1aa8A01
type: Pdb
references: 1aa8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aa8
main chain in catalysis: GLN 53;GLY 313

1aa8B01
type: Pdb
references: 1aa8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aa8
main chain in catalysis: GLN 53;GLY 313

1an9A01
type: Pdb
references: 1an9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1an9
main chain in catalysis: GLN 53;GLY 313

1an9B01
type: Pdb
references: 1an9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1an9
main chain in catalysis: GLN 53;GLY 313

1daoA01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoB01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoC01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoD01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoE01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoF01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoG01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1daoH01
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
main chain in catalysis: GLN 53;GLY 313

1ddoA01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoB01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoC01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoD01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoE01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoF01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoG01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1ddoH01
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
main chain in catalysis: GLN 53;GLY 313

1eviA01
type: Pdb
references: 1evi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evi
main chain in catalysis: GLN 53;GLY 313

1eviB01
type: Pdb
references: 1evi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evi
main chain in catalysis: GLN 53;GLY 313

1kifA01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifB01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifC01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifD01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifE01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifF01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifG01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1kifH01
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
main chain in catalysis: GLN 53;GLY 313

1ve9A01
type: Pdb
references: 1ve9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ve9
main chain in catalysis: GLN 53;GLY 313

1ve9B01
type: Pdb
references: 1ve9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ve9
main chain in catalysis: GLN 53;GLY 313

1aa8A02
type: Pdb
references: 1aa8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aa8
catalytic residue: TYR 224

1aa8B02
type: Pdb
references: 1aa8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aa8
catalytic residue: TYR 224

1an9A02
type: Pdb
references: 1an9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1an9
catalytic residue: TYR 224

1an9B02
type: Pdb
references: 1an9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1an9
catalytic residue: TYR 224

1daoA02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoB02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoC02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoD02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoE02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoF02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoG02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1daoH02
type: Pdb
references: 1dao
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dao
catalytic residue: TYR 224

1ddoA02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoB02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoC02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoD02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoE02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoF02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoG02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1ddoH02
type: Pdb
references: 1ddo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ddo
catalytic residue: TYR 224

1eviA02
type: Pdb
references: 1evi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evi
catalytic residue: TYR 224

1eviB02
type: Pdb
references: 1evi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1evi
catalytic residue: TYR 224

1kifA02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifB02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifC02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifD02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifE02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifF02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifG02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1kifH02
type: Pdb
references: 1kif
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kif
catalytic residue: TYR 224

1ve9A02
type: Pdb
references: 1ve9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ve9
catalytic residue: TYR 224

1ve9B02
type: Pdb
references: 1ve9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ve9
catalytic residue: TYR 224

Analogue
compound: FAD
pdb: 1daoA01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoB01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoC01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoD01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoE01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoF01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoG01
ligand het code: FAB

Analogue
compound: FAD
pdb: 1daoH01
ligand het code: FAB

IntermediateAnalogue
pdb: 1aa8A02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1aa8B02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1an9A02
ligand het code: BE2

IntermediateAnalogue
pdb: 1an9B02
ligand het code: BE2

IntermediateBound
pdb: 1ddoA02
ligand het code: ITR

IntermediateBound
pdb: 1ddoB02
ligand het code: ITR

IntermediateBound
pdb: 1ddoC02
ligand het code: ITR

IntermediateBound
pdb: 1ddoD02
ligand het code: ITR

IntermediateBound
pdb: 1ddoE02
ligand het code: ITR

IntermediateBound
pdb: 1ddoF02
ligand het code: ITR

IntermediateBound
pdb: 1ddoG02
ligand het code: ITR

IntermediateBound
pdb: 1ddoH02
ligand het code: ITR

IntermediateAnalogue
pdb: 1eviA02
ligand het code: 2PC

IntermediateAnalogue
pdb: 1eviB02
ligand het code: 2PC

IntermediateAnalogue
pdb: 1kifA02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifB02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifC02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifD02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifE02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifF02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifG02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1kifH02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1ve9A02
ligand het code: BEZ

IntermediateAnalogue
pdb: 1ve9B02
ligand het code: BEZ

Active site plasticity in D-amino acid oxidase: a crystallographic analysis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY
medline id: 97297794
references: http://www.ncbi.nlm.nih.gov/pubmed/9153426
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00371
journal: Biochemistry
volume: 36
pages: 5853-60
published year: 1997
authors:
  item: Todone F
  item: Vanoni MA
  item: Mozzarelli A
  item: Bolognesi M
  item: Coda A
  item: Curti B
  item: Mattevi A

ReferenceForCatalyticMechanism
reference index: 9
reference section: Scheme 1, Scheme 2, Scheme 3

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.7, p.618-619

ReferenceForCatalyticMechanism
reference index: 13
reference section: p.15

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.5, p.7498-7499

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.5858-5859

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.1, p.804-806

ReferenceForCatalyticMechanism
reference index: 19
reference section: Fig.6, Fig.7, p.829-832

ReferenceForCatalyticMechanism
reference index: 22
reference section: Scheme 2, p.1741-1744

ReferenceForCatalyticMechanism
reference index: 23

ReferenceForCatalyticMechanism
reference index: 24
reference section: Scheme 2

ReferenceForCatalyticMechanism
reference index: 26
reference section: Fig.6, p.12466-12468

ReferenceForCatalyticMechanism
reference index: 28
reference section: Fig.1, p.14120-14121

ReferenceForCatalyticMechanism
reference index: 29
reference section: p.540-541, p.542-544

ReferenceForCatalyticMechanism
reference index: 30
reference section: Scheme 1, Scheme 3, p.29-31

pH dependence of catalysis of the monomer of hog kidney D-amino acid oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/20559
journal: Med J Osaka Univ
volume: 27
pages: 33-46
published year: 1976
authors:
  item: Horiike K
  item: Shiga K
  item: Nishina Y
  item: Yamano T

Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene.
type: BibliographicResource
comment: PRELIMINARY STUDIES ON ACTIVE SITE
medline id: 82120157
references: http://www.ncbi.nlm.nih.gov/pubmed/6120171
references: P00371
journal: J Biol Chem
volume: 257
pages: 1937-44
published year: 1982
authors:
  item: Swenson RP
  item: Williams CH Jr
  item: Massey V

Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride.
type: BibliographicResource
comment: PRELIMINARY STUDIES ON ACTIVE SITE
medline id: 83082913
references: http://www.ncbi.nlm.nih.gov/pubmed/6129252
references: P00371
journal: J Biol Chem
volume: 258
pages: 497-502
published year: 1983
authors:
  item: Swenson RP
  item: Williams CH Jr
  item: Massey V

Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and histidine-217 in porcine kidney D-amino acid oxidase on its catalytic function.
type: BibliographicResource
comment: MUTAGENESIS OF Y-55/M-110/H-217 TO SHOW THEY ARE NOT IN ACTIVE SITE
medline id: 8900569
references: http://www.ncbi.nlm.nih.gov/pubmed/2901989
references: P00371
journal: FEBS Lett
volume: 238
pages: 269-72
published year: 1988
authors:
  item: Watanabe F
  item: Fukui K
  item: Momoi K
  item: Miyake Y

Two spectrophotometric assays for D-amino acid oxidase: for the study of distribution patterns.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2907883
journal: Int J Biochem
volume: 20
pages: 1235-8
published year: 1988
authors:
  item: Nagata Y
  item: Shimojo T
  item: Akino T

Site-specific mutagenesis of lysine-204, tyrosine-224, tyrosine-228, and histidine-307 of porcine kidney D-amino acid oxidase and the implications as to its catalytic function.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2570065
journal: J Biochem (Tokyo)
volume: 105
pages: 1024-9
published year: 1989
authors:
  item: Watanabe F
  item: Fukui K
  item: Momoi K
  item: Miyake Y

Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization.
type: BibliographicResource
comment: ACTIVE SITES TYR-228 AND HIS-307
medline id: 91201275
references: http://www.ncbi.nlm.nih.gov/pubmed/1673125
references: P00371
journal: J Biochem (Tokyo)
volume: 109
pages: 171-7
published year: 1991
authors:
  item: Miyano M
  item: Fukui K
  item: Watanabe F
  item: Takahashi S
  item: Tada M
  item: Kanashiro M
  item: Miyake Y

Regional differences for the D-amino acid oxidase-catalysed oxidation of D-methionine in chicken small intestine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1351830
journal: Comp Biochem Physiol B
volume: 101
pages: 509-11
published year: 1992
authors:
  item: Brachet P
  item: Puigserver A

Intrinsic primary, secondary, and solvent kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase: evidence against a concerted mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7908225
journal: Biochemistry
volume: 33
pages: 4001-7
published year: 1994
authors:
  item: Denu JM
  item: Fitzpatrick PF

Studies on the kinetic mechanism of pig kidney D-amino acid oxidase by site-directed mutagenesis of tyrosine 224 and tyrosine 228.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7989339
journal: J Biol Chem
volume: 269
pages: 31666-73
published year: 1994
authors:
  item: Pollegioni L
  item: Fukui K
  item: Massey V

Structures of charge-transfer complexes of flavoenzyme D-amino acid oxidase: a study by resonance Raman spectroscopy and extended Huckel molecular orbital method.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8690726
journal: J Biochem (Tokyo)
volume: 118
pages: 614-20
published year: 1995
authors:
  item: Nishina Y
  item: Sato K
  item: Miura R
  item: Shiga K

Synthesis, characterization and preliminary crystallographic data of N6-(6-carbamoylhexyl)-FAD-D-amino-acid oxidase from pig kidney, a semi-synthetic oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8681967
journal: Eur J Biochem
volume: 238
pages: 519-28
published year: 1996
authors:
  item: Stocker A
  item: Hecht HJ
  item: Buckmann AF

Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY
medline id: 97018220
references: http://www.ncbi.nlm.nih.gov/pubmed/8864836
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00371
journal: J Biochem (Tokyo)
volume: 120
pages: 14-7
published year: 1996
authors:
  item: Mizutani H
  item: Miyahara I
  item: Hirotsu K
  item: Nishina Y
  item: Shiga K
  item: Setoyama C
  item: Miura R

Crystallization of expressed porcine kidney D-amino acid oxidase and preliminary X-ray crystallographic characterization.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8827446
journal: J Biochem (Tokyo)
volume: 119
pages: 1114-7
published year: 1996
authors:
  item: Setoyama C
  item: Miura R
  item: Nishina Y
  item: Shiga K
  item: Mizutani H
  item: Miyahara I
  item: Hirotsu K

Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
medline id: 96353844
references: http://www.ncbi.nlm.nih.gov/pubmed/8755502
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00371
journal: Proc Natl Acad Sci U S A
volume: 93
pages: 7496-501
published year: 1996
authors:
  item: Mattevi A
  item: Vanoni MA
  item: Todone F
  item: Rizzi M
  item: Teplyakov A
  item: Coda A
  item: Bolognesi M
  item: Curti B

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00037#17
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9153402
journal: Biochemistry
volume: 36
pages: 5624-32
published year: 1997
authors:
  item: Vanoni MA
  item: Cosma A
  item: Mazzeo D
  item: Mattevi A
  item: Todone F
  item: Curti B
title: Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase.

Structure of D-amino acid oxidase: new insights from an old enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9434899
journal: Curr Opin Struct Biol
volume: 7
pages: 804-10
published year: 1997
authors:
  item: Mattevi A
  item: Vanoni MA
  item: Curti B

Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9399588
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biochem (Tokyo)
volume: 122
pages: 825-33
published year: 1997
authors:
  item: Miura R
  item: Setoyama C
  item: Nishina Y
  item: Shiga K
  item: Mizutani H
  item: Miyahara I
  item: Hirotsu K

Glycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9268372
journal: J Biol Chem
volume: 272
pages: 22248-52
published year: 1997
authors:
  item: Raibekas AA
  item: Massey V

The role of a conserved histidine residue, His324, in Trigonopsis variabilis D-amino acid oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10427728
journal: FEMS Microbiol Lett
volume: 176
pages: 443-8
published year: 1999
authors:
  item: Lin LL
  item: Wang WC
  item: Ju SS
  item: Chien HR
  item: Hsu WH

D-Amino acid oxidase: new findings.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11130179
journal: Cell Mol Life Sci
volume: 57
pages: 1732-47
published year: 2000
authors:
  item: Pilone MS

Three-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10876160
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biochem (Tokyo)
volume: 128
pages: 73-81
published year: 2000
authors:
  item: Mizutani H
  item: Miyahara I
  item: Hirotsu K
  item: Nishina Y
  item: Shiga K
  item: Setoyama C
  item: Miura R

Substrate recognition and activation mechanism of D-amino acid oxidase: a study using substrate analogs.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10920257
journal: J Biochem (Tokyo)
volume: 128
pages: 213-23
published year: 2000
authors:
  item: Nishina Y
  item: Sato K
  item: Miura R
  item: Shiga K

Design and properties of human D-amino acid oxidase with covalently attached flavin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10716694
journal: Proc Natl Acad Sci U S A
volume: 97
pages: 3089-93
published year: 2000
authors:
  item: Raibekas AA
  item: Fukui K
  item: Massey V

The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11070076
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Proc Natl Acad Sci U S A
volume: 97
pages: 12463-8
published year: 2000
authors:
  item: Umhau S
  item: Pollegioni L
  item: Molla G
  item: Diederichs K
  item: Welte W
  item: Pilone MS
  item: Ghisla S

On the ligands in charge-transfer complexes of porcine kidney flavoenzyme D-amino acid oxidase in three redox states: a resonance Raman study.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11686926
journal: J Biochem (Tokyo)
volume: 130
pages: 637-47
published year: 2001
authors:
  item: Nishina Y
  item: Sato K
  item: Shi R
  item: Setoyama C
  item: Miura R
  item: Shiga K

First-principles molecular dynamics investigation of the D-amino acid oxidative half-reaction catalyzed by the flavoenzyme D-amino acid oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12450374
journal: Biochemistry
volume: 41
pages: 14111-21
published year: 2002
authors:
  item: Tilocca A
  item: Gamba A
  item: Vanoni MA
  item: Fois E

Yeast D-amino acid oxidase: structural basis of its catalytic properties.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12445787
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 324
pages: 535-46
published year: 2002
authors:
  item: Pollegioni L
  item: Diederichs K
  item: Molla G
  item: Umhau S
  item: Welte W
  item: Ghisla S
  item: Pilone MS

On the mechanism of Rhodotorula gracilis D-amino acid oxidase: role of the active site serine 335.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15450847
journal: Biochim Biophys Acta
volume: 1702
pages: 19-32
published year: 2004
authors:
  item: Boselli A
  item: Piubelli L
  item: Molla G
  item: Sacchi S
  item: Pilone MS
  item: Ghisla S
  item: Pollegioni L

ophio-amino-acid oxidase
type: KeggEnzyme

L-amino acid:O2 oxidoreductase
type: KeggEnzyme

new yellow enzyme
type: KeggEnzyme