KEGG   ENZYME: 1.17.3.2Help
Entry
EC 1.17.3.2                 Enzyme                                 

Name
xanthine oxidase;
hypoxanthine oxidase;
hypoxanthine:oxygen oxidoreductase;
Schardinger enzyme;
xanthine oxidoreductase;
hypoxanthine-xanthine oxidase;
xanthine:O2 oxidoreductase;
xanthine:xanthine oxidase
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With oxygen as acceptor
BRITE hierarchy
Sysname
xanthine:oxygen oxidoreductase
Reaction(IUBMB)
xanthine + H2O + O2 = urate + H2O2 [RN:R02107]
Reaction(KEGG)
Substrate
xanthine [CPD:C00385];
H2O [CPD:C00001];
O2 [CPD:C00007]
Product
urate [CPD:C00366];
H2O2 [CPD:C00027]
Comment
An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [4,5,7,10] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [4,6,10].
History
EC 1.17.3.2 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, transferred 2004 to EC 1.17.3.2, modified 2011
Pathway
ec00230  Purine metabolism
ec00232  Caffeine metabolism
ec00983  Drug metabolism - other enzymes
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00106  xanthine dehydrogenase/oxidase
Genes
HSA: 7498(XDH)
PTR: 470347(XDH)
PPS: 100986628(XDH)
GGO: 101138402(XDH)
PON: 100454383(XDH)
NLE: 100594931(XDH)
MCC: 708046(XDH)
MCF: 102116275(XDH)
CSAB: 103220539(XDH)
RRO: 104659929(XDH)
RBB: 108516631(XDH)
CJC: 100414932(XDH)
SBQ: 101044169(XDH)
MMU: 22436(Xdh)
RNO: 497811(Xdh)
CGE: 100766626(Xdh)
NGI: 103748365(Xdh)
HGL: 101708017(Xdh)
CCAN: 109701710(Xdh)
OCU: 100144327(XDH)
TUP: 102477455(XDH)
CFA: 483028(XDH)
AML: 100465942(XDH)
UMR: 103671606(XDH)
ORO: 101376175(XDH)
AJU: 106967886(XDH)
BTA: 280960(XDH)
BOM: 102264420(XDH)
BIU: 109565958(XDH)
PHD: 102326880(XDH)
CHX: 100861280(XDH)
OAS: 780499(XDH)
SSC: 100515259(XDH)
CFR: 102523581(XDH)
CDK: 105095605(XDH)
BACU: 103004564(XDH)
LVE: 103084498(XDH)
OOR: 101284574(XDH)
MYB: 102262378(XDH)
MYD: 102773370(XDH)
PALE: 102884734(XDH)
LAV: 100672640(XDH)
TMU: 101349074
MDO: 100031481(XDH)
SHR: 100933358(XDH)
OAA: 100078272(XDH) 100078370
GGA: 396025(XDH)
MGP: 100544067(XDH)
CJO: 107310773(XDH)
APLA: 101799192(XDH)
ACYG: 106031596(XDH)
TGU: 100222890(XDH)
GFR: 102040336(XDH)
FAB: 101819038(XDH)
PHI: 102106931(XDH)
PMAJ: 107201507(XDH)
CCW: 104685575(XDH)
FPG: 101918653(XDH)
FCH: 102052812(XDH)
CLV: 102092037(XDH)
EGZ: 104134615(XDH)
AAM: 106482734(XDH)
ASN: 102374197(XDH)
AMJ: 102564016(XDH)
PSS: 102461631(XDH)
CMY: 102945230(XDH)
CPIC: 101953114(XDH)
ACS: 100566790(xdh)
PVT: 110087557(XDH)
PBI: 103056546(XDH)
GJA: 107112582(XDH) 107125178
XLA: 108716095(xdh.L) 108717383
XTR: 100497499(xdh)
NPR: 108796807(XDH)
DRE: 560486(xdh)
SANH: 107674096 107697780(xdh)
CCAR: 109084316 109107555(xdh)
IPU: 108269840(xdh)
AMEX: 103031284(xdh)
TRU: 101073141(xdh)
LCO: 104938633(xdh)
MZE: 101478907(xdh)
OLA: 101162508(xdh)
XMA: 102231285(xdh)
PRET: 103481416(xdh)
NFU: 107384577(xdh)
CSEM: 103389795(xdh)
LCF: 108877173(xdh)
HCQ: 109510392(xdh)
BPEC: 110166494(xdh)
SASA: 100380763(xdh)
ELS: 105031569(xdh)
SFM: 108923027(xdh)
LCM: 106702173
CMK: 103182679 103187630(xdh)
SPU: 576712(XDH)
DSI: Dsimw501_GD18875(Dsim_ry) Dsimw501_GD20335(Dsim_GD20335) Dsimw501_GD20336(Dsim_GD20336) Dsimw501_GD20337(Dsim_GD20337) Dsimw501_GD20338(Dsim_GD20338)
AME: 724718
TCA: 655982 656059 656456(GLEAN_12132) 656621 656938 658680(GLEAN_09714) 658886
DPA: 109536954
API: 100169249
CEL: CELE_F55B11.1(xdh-1)
CBR: CBG21624
ATH: AT4G34890(XDH1) AT4G34900(XDH2)
CRB: 17877660
THJ: 104817905
CIT: 102622737
TCC: 18589817
GRA: 105799411
DZI: 111301841
VRA: 106759191
VAR: 108333356
CAM: 101495267
LJA: Lj3g3v1694660.1(Lj3g3v1694660.1)
ADU: 107461425
LANG: 109351322
FVE: 101298861
PPER: 18780893
PMUM: 103326686
PAVI: 110760280
PXB: 103965536
ZJU: 107412613
CSV: 101211977
MCHA: 111021441
CMAX: 111485375
CMOS: 111461442
CPEP: 111779652
RCU: 8274436
JCU: 105648267
POP: 7467360
JRE: 109003655
VVI: 100248547
SOT: 102596284
NSY: 104224061
NTO: 104111014
INI: 109160132
SIND: 105163571
OEU: 111404472
HAN: 110866903
DCR: 108226793
BVG: 104889971
SOE: 110801608
NNU: 104603426
OSA: 4333171
DOSA: Os03t0429800-01(Os03g0429800)
OBR: 102707013
BDI: 100827961
ATS: 109737702(LOC109737702) 109742032(LOC109742032)
SBI: 110434890
ZMA: 100384368
SITA: 101785503
EGU: 105056188
MUS: 103989027
CRE: CHLREDRAFT_117669(XDH1)
APRO: F751_6411
SLB: AWJ20_3928(AOH2)
NCR: NCU03350(xdh-1)
NTE: NEUTE1DRAFT130703(NEUTE1DRAFT_130703)
MGR: MGG_12738
SSCK: SPSK_00201
MAW: MAC_05768
MAJ: MAA_01730
CMT: CCM_08980
MBE: MBM_00517
ANG: ANI_1_1056034(An03g01530) ANI_1_902184(An04g05440)
ABE: ARB_02280
TVE: TRV_04973
DDI: DDB_G0291047(xdh)
DFA: DFA_00340(xdh)
SMIN: v1.2.005299.t1(symbB.v1.2.005299.t1) v1.2.012038.t1(symbB.v1.2.012038.t1) v1.2.019051.t1(symbB.v1.2.019051.t1)
ARA: Arad_9877
SACI: Sinac_0251
FJG: BB050_03475(xdhA_2)
 » show all
Taxonomy
Reference
1
  Authors
Avis, P.G., Bergel, F. and Bray, R.C.
  Title
Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cow's milk.
  Journal
J Chem Soc (Lond):1100-1105 (1955)
Reference
2  [PMID:6960894]
  Authors
Battelli MG, Lorenzoni E.
  Title
Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.
  Journal
Biochem J 207:133-8 (1982)
Reference
3
  Authors
Bray, R.C.
  Title
Xanthine oxidase.
  Journal
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 533-556.
Reference
4  [PMID:4342395]
  Authors
Corte ED, Stirpe F.
  Title
The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme.
  Journal
Biochem J 126:739-45 (1972)
Reference
5  [PMID:3459393]
  Authors
Ikegami T, Nishino T
  Title
The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver.
  Journal
Arch Biochem Biophys 247:254-60 (1986)
DOI:10.1016/0003-9861(86)90582-5
Reference
6  [PMID:3294898]
  Authors
Engerson TD, McKelvey TG, Rhyne DB, Boggio EB, Snyder SJ, Jones HP
  Title
Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues.
  Journal
J Clin Invest 79:1564-70 (1987)
DOI:10.1172/JCI112990
Reference
7  [PMID:2610112]
  Authors
Saito T, Nishino T, Tsushima K
  Title
Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them.
  Journal
Adv Exp Med Biol 253B:179-83 (1989)
Reference
8  [PMID:2350174]
  Authors
Carpani G, Racchi M, Ghezzi P, Terao M, Garattini E.
  Title
Purification and characterization of mouse liver xanthine oxidase.
  Journal
Arch Biochem Biophys 279:237-41 (1990)
DOI:10.1016/0003-9861(90)90487-J
Reference
9  [PMID:11092937]
  Authors
Eger BT, Okamoto K, Enroth C, Sato M, Nishino T, Pai EF, Nishino T.
  Title
Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk.
  Journal
Acta Crystallogr D Biol Crystallogr 56 Pt 12:1656-8 (2000)
Reference
10 [PMID:18513323]
  Authors
Nishino T, Okamoto K, Eger BT, Pai EF, Nishino T
  Title
Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase.
  Journal
FEBS J 275:3278-89 (2008)
DOI:10.1111/j.1742-4658.2008.06489.x
Other DBs
ExplorEnz - The Enzyme Database: 1.17.3.2
IUBMB Enzyme Nomenclature: 1.17.3.2
ExPASy - ENZYME nomenclature database: 1.17.3.2
UM-BBD (Biocatalysis/Biodegradation Database): 1.17.3.2
BRENDA, the Enzyme Database: 1.17.3.2
CAS: 9002-17-9

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