| Entry |
|
|---|
| Name |
D-amino-acid oxidase;
ophio-amino-acid oxidase;
L-amino acid:O2 oxidoreductase;
new yellow enzyme |
|---|
| Class |
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
 |
|---|
| Sysname |
D-amino-acid:oxygen oxidoreductase (deaminating) |
|---|
| Reaction(IUBMB) |
a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01340] |
|---|
| Reaction(KEGG) |
R01340 > R02457 R02894 R02923 R05861 R07400;
(other) R00366 R04221 R06124
 |
|---|
| Substrate |
D-amino acid [CPD:C00405];
H2O [CPD:C00001];
O2 [CPD:C00007] |
|---|
| Product |
2-oxo acid [CPD:C00161];
NH3 [CPD:C00014];
H2O2 [CPD:C00027] |
|---|
| Cofactor |
FAD [CPD:C00016] |
|---|
| Comment |
A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts
on glycine. |
|---|
| Pathway |
PATH: ec00260 Glycine, serine and threonine metabolism
PATH: ec00311 Penicillin and cephalosporin biosynthesis
PATH: ec00330 Arginine and proline metabolism
PATH: ec00472 D-Arginine and D-ornithine metabolism
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00273 D-amino-acid oxidase |
|---|
| Genes |
HSA: 1610(DAO)
PTR: 743881(DAO)
MCC: 706373(DAO)
MMU: 13142(Dao)
RNO: 114027(Dao)
CFA: 486317(DAO)
BTA: 615334(DAO)
SSC: 397134(DAO1)
ECB: 100059819
MDO: 100024682
OAA: 100082667
GGA: 416894(DAO)
TGU: 100227661
XLA: 735104
XTR: 100036595(dao)
DRE: 402994(dao.3) 405800(dao.2) 791584
BFO: BRAFLDRAFT_115405
DME: Dmel_CG11236
CEL: C47A10.5
TAD: TRIADDRAFT_60526
KLA: KLLA0A08492g
DHA: DEHA0B06754g
NCR: NCU06558
AFM: AFUA_5G11290 AFUA_5G13940 AFUA_6G10230
ANG: An01g02430
UMA: UM05703.1
MBR: MONBRDRAFT_15811
TET: TTHERM_00633280 TTHERM_00787140
AZO: azo1482(mnmC) azo1919
PUB: SAR11_0547
MTU: Rv1905c(aao)
MTC: MT1956
MRA: MRA_1916(aao)
MBO: Mb1940c(aao)
MBB: BCG_1944c(aao)
MAV: MAV_2796
MUL: MUL_2926(aao)
NCA: Noca_1780
SEN: SACE_0979(aao)
RXY: Rxyl_0526
PMB: A9601_19131
PMC: P9515_18941
PMF: P9303_30031
PMG: P9301_18941
PME: NATL1_21851
 |
|---|
| Structures |
PDB: 1AN9 1C0I 1C0K 1C0P 1DAO 1DDO 1EVI 1KIF 1VE9 2DU8
2E48 2E49 2E4A 2E82 3CUK 3G3E |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:14314378]
DIXON M, KLEPPE K.
D-AMINO ACID OXIDASE. I. DISSOCIATION AND RECOMBINATION OF THE
HOLOENZYME.
Biochim. Biophys. Acta. 96 (1965) 357-67.
Sus scofa [GN:ssc] |
|---|
Reference
Authors
Title
Journal
|
2
Dixon, M. and Kleppe, K.
D-Amino acid oxidase. II. Specificity, competitive inhibition and
reaction sequence.
Biochim. Biophys. Acta 96 (1965) 368-382. |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:14314379]
DIXON M, KLEPPE K.
D-AMINO ACID OXIDASE. 3. EFFECT OF PH.
Biochim. Biophys. Acta. 96 (1965) 383-9.
Sus scofa [GN:ssc] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:13767909]
MASSEY V, PALMER G, BENNETT R.
The purification and some properties of D-amino acid oxidase.
Biochim. Biophys. Acta. 48 (1961) 1-9.
Sus scofa [GN:ssc] |
|---|
Reference
Authors
Title
Journal
|
5
Meister, A. and Wellner, D.
Flavoprotein amino acid oxidase.
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
ed., vol. 7, Academic Press, New York, 1963, p. 609-648. |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.4.3.3
IUBMB Enzyme Nomenclature: 1.4.3.3
ExPASy - ENZYME nomenclature database: 1.4.3.3
BRENDA, the Enzyme Database: 1.4.3.3
CAS: 9000-88-8 |
|---|
