KEGG   ORTHOLOGY: K07409
Entry
K07409                      KO                                     

Name
CYP1A2
Definition
cytochrome P450 family 1 subfamily A polypeptide 2 [EC:1.14.14.1]
Pathway
ko00140  Steroid hormone biosynthesis
ko00232  Caffeine metabolism
ko00380  Tryptophan metabolism
ko00591  Linoleic acid metabolism
ko00830  Retinol metabolism
ko00980  Metabolism of xenobiotics by cytochrome P450
ko00982  Drug metabolism - cytochrome P450
ko01100  Metabolic pathways
ko01110  Biosynthesis of secondary metabolites
ko05204  Chemical carcinogenesis
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09103 Lipid metabolism
   00140 Steroid hormone biosynthesis
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
   00591 Linoleic acid metabolism
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
  09105 Amino acid metabolism
   00380 Tryptophan metabolism
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
  09108 Metabolism of cofactors and vitamins
   00830 Retinol metabolism
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
  09110 Biosynthesis of other secondary metabolites
   00232 Caffeine metabolism
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
  09111 Xenobiotics biodegradation and metabolism
   00980 Metabolism of xenobiotics by cytochrome P450
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
   00982 Drug metabolism - cytochrome P450
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
 09160 Human Diseases
  09161 Cancer: overview
   05204 Chemical carcinogenesis
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   00199 Cytochrome P450
    K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.14  With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.14.1  unspecific monooxygenase
     K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
Cytochrome P450 [BR:ko00199]
 Cytochrome P450, animal type
  CYP1 family
   K07409  CYP1A2; cytochrome P450 family 1 subfamily A polypeptide 2
Other DBs
RN: R03408 R03629 R07000 R07001 R07021 R07022 R07055 R07056 R07098 R07099 R07939 R07943 R07945 R08293 R08294 R08392 R09405 R09407 R09408
Genes
HSA: 1544(CYP1A2)
PTR: 735881(CYP1A2)
PPS: 100975837
GGO: 101130358
PON: 100172368(CYP1A2)
NLE: 100586622
MCF: 102130662(CYP1A2)
CSAB: 103245329(CYP1A2)
RRO: 104672152
RBB: 108531494
CJC: 100392712(CYP1A2)
SBQ: 101037899
MMU: 13077(Cyp1a2)
MCAL: 110301271
MPAH: 110328034
RNO: 24297(Cyp1a2)
MUN: 110558530
CGE: 100755851
NGI: 103736875
CCAN: 109695949
OCU: 100328937(CYP1A2)
TUP: 102484432
CFA: 494010(CYP1A2)
VVP: 112917417
AML: 100472774
UMR: 103678991
UAH: 113240971
ORO: 101381962
ELK: 111153221
FCA: 554345(CYP1A2)
PTG: 102966939
PPAD: 109262688
AJU: 106979449
BTA: 503552(CYP1A2)
BOM: 102280158
BIU: 109575670
BBUB: 102399561
CHX: 102170554
OAS: 101109214
SSC: 100152910(CYP1A2)
CFR: 102518362
CDK: 105087261
BACU: 103007560
LVE: 103071784
OOR: 101287407
DLE: 111177607
PCAD: 102984795
ECB: 100062244(CYP1A2)
EPZ: 103552315
EAI: 106831265
MYB: 102262040
MYD: 102761918
MNA: 107535217
HAI: 109396253
DRO: 112301801
MJV: 108388607
LAV: 100666189
TMU: 101359541
MDO: 100029908
SHR: 116421952
PCW: 110213926
SPIS: 111333828
 » show all
Reference
PMID:3755823
  Authors
Jaiswal AK, Nebert DW, Gonzalez FJ
  Title
Human P3(450): cDNA and complete amino acid sequence.
  Journal
Nucleic Acids Res 14:6773-4 (1986)
DOI:10.1093/nar/14.16.6773
  Sequence
[hsa:1544]

KEGG   ORTHOLOGY: K17683
Entry
K17683            Tight     KO                                     

Name
CYP2A6
Definition
cytochrome P450 family 2 subfamily A polypeptide 6 [EC:1.14.13.-]
Pathway
ko00232  Caffeine metabolism
ko00830  Retinol metabolism
ko00980  Metabolism of xenobiotics by cytochrome P450
ko00982  Drug metabolism - cytochrome P450
ko00983  Drug metabolism - other enzymes
ko01100  Metabolic pathways
ko05204  Chemical carcinogenesis
Disease
H01205  Coumarin resistance
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09108 Metabolism of cofactors and vitamins
   00830 Retinol metabolism
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
  09110 Biosynthesis of other secondary metabolites
   00232 Caffeine metabolism
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
  09111 Xenobiotics biodegradation and metabolism
   00980 Metabolism of xenobiotics by cytochrome P450
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
   00982 Drug metabolism - cytochrome P450
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
   00983 Drug metabolism - other enzymes
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
 09160 Human Diseases
  09161 Cancer: overview
   05204 Chemical carcinogenesis
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   00199 Cytochrome P450
    K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.13  With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.13.-  
     K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
Cytochrome P450 [BR:ko00199]
 Cytochrome P450, animal type
  CYP2 family
   K17683  CYP2A6; cytochrome P450 family 2 subfamily A polypeptide 6
Other DBs
RN: R07000 R07001 R07945 R08225 R08324 R08325 R08326 R08327 R08390 R08391 R08392 R09408 R09421 R09423 R09424 R09425
Genes
HSA: 1548(CYP2A6)
GGO: 101146638
PON: 100457048
MCC: 678689(CYP2A24)
MCF: 102122745(CYP2A24)
Reference
PMID:2726448
  Authors
Miles JS, Bickmore W, Brook JD, McLaren AW, Meehan R, Wolf CR
  Title
Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity.
  Journal
Nucleic Acids Res 17:2907-17 (1989)
DOI:10.1093/nar/17.8.2907
  Sequence
[hsa:1548]
Reference
  Authors
Xu C, Goodz S, Sellers EM, Tyndale RF
  Title
CYP2A6 genetic variation and potential consequences.
  Journal
Adv Drug Deliv Rev 54:1245-56 (2002)
DOI:10.1016/S0169-409X(02)00065-0

KEGG   ORTHOLOGY: K00106
Entry
K00106                      KO                                     

Name
XDH
Definition
xanthine dehydrogenase/oxidase [EC:1.17.1.4 1.17.3.2]
Pathway
ko00230  Purine metabolism
ko00232  Caffeine metabolism
ko00983  Drug metabolism - other enzymes
ko01100  Metabolic pathways
ko01110  Biosynthesis of secondary metabolites
ko01120  Microbial metabolism in diverse environments
ko04146  Peroxisome
Module
M00546  Purine degradation, xanthine => urea
Disease
H00192  Xanthinuria
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09104 Nucleotide metabolism
   00230 Purine metabolism
    K00106  XDH; xanthine dehydrogenase/oxidase
  09110 Biosynthesis of other secondary metabolites
   00232 Caffeine metabolism
    K00106  XDH; xanthine dehydrogenase/oxidase
  09111 Xenobiotics biodegradation and metabolism
   00983 Drug metabolism - other enzymes
    K00106  XDH; xanthine dehydrogenase/oxidase
 09140 Cellular Processes
  09141 Transport and catabolism
   04146 Peroxisome
    K00106  XDH; xanthine dehydrogenase/oxidase
 09180 Brite Hierarchies
  09183 Protein families: signaling and cellular processes
   04147 Exosome
    K00106  XDH; xanthine dehydrogenase/oxidase
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.17  Acting on CH or CH2 groups
   1.17.1  With NAD+ or NADP+ as acceptor
    1.17.1.4  xanthine dehydrogenase
     K00106  XDH; xanthine dehydrogenase/oxidase
   1.17.3  With oxygen as acceptor
    1.17.3.2  xanthine oxidase
     K00106  XDH; xanthine dehydrogenase/oxidase
Exosome [BR:ko04147]
 Exosomal proteins
  Exosomal proteins of breast milk
   K00106  XDH; xanthine dehydrogenase/oxidase
Other DBs
RN: R01768 R01769 R02103 R02107 R07942 R07977 R07978 R07979 R08235
GO: 0004854 0004855
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)
MCAL: 110312137(Xdh)
MPAH: 110335495(Xdh)
RNO: 497811(Xdh)
MUN: 110557067(Xdh)
CGE: 100766626(Xdh)
NGI: 103748365(Xdh)
HGL: 101708017(Xdh)
CCAN: 109701710(Xdh)
OCU: 100144327(XDH)
TUP: 102477455(XDH)
CFA: 483028(XDH)
VVP: 112933009(XDH)
AML: 100465942(XDH)
UMR: 103671606(XDH)
UAH: 113240940(XDH)
ORO: 101376175(XDH)
ELK: 111154104
FCA: 105259797 493692(XDH)
PTG: 102969928
PPAD: 109261405 109262396(XDH)
AJU: 106967886(XDH)
BTA: 280960(XDH)
BOM: 102264420(XDH)
BIU: 109565958(XDH)
BBUB: 102406968(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)
DLE: 111174909(XDH)
PCAD: 102980160(XDH)
MYB: 102262378(XDH)
MYD: 102773370(XDH)
MNA: 107541765(XDH)
HAI: 109395899
DRO: 112297809(XDH)
PALE: 102884734(XDH)
RAY: 107505738(XDH)
MJV: 108404078(XDH)
LAV: 100672640(XDH)
TMU: 101349074
MDO: 100031481(XDH)
SHR: 100933358(XDH)
PCW: 110198166(XDH)
GGA: 396025(XDH)
MGP: 100544067(XDH)
CJO: 107310773(XDH)
NMEL: 110395607(XDH)
APLA: 101799192(XDH)
ACYG: 106031596(XDH)
TGU: 100222890(XDH)
LSR: 110473976(XDH)
SCAN: 103821303(XDH)
GFR: 102040336(XDH)
FAB: 101819038(XDH)
PHI: 102106931(XDH)
PMAJ: 107201507(XDH)
CCAE: 111926289(XDH)
CCW: 104685575(XDH)
ETL: 114073409(XDH)
FPG: 101918653(XDH)
FCH: 102052812(XDH)
CLV: 102092037(XDH)
EGZ: 104134615(XDH)
NNI: 104019267(XDH)
ACUN: 113478412(XDH)
PADL: 103925004(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)
PMUR: 107297206(XDH)
TSR: 106538731(XDH)
PMUA: 114594599(XDH)
GJA: 107112582(XDH)
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)
PHYP: 113533982(xdh)
AMEX: 103031284(xdh)
EEE: 113583665(xdh)
TRU: 101073141(xdh)
LCO: 104938633
MZE: 101478907(xdh)
ONL: 100706331(xdh)
OLA: 101162508(xdh)
XMA: 102231285(xdh)
XCO: 114140507(xdh)
PRET: 103481416(xdh)
CVG: 107104320(xdh)
NFU: 107384577(xdh)
KMR: 108251278(xdh)
ALIM: 106531265(xdh)
AOCE: 111587270(xdh)
CSEM: 103389795(xdh)
LCF: 108877173(xdh)
SDU: 111235538(xdh)
SLAL: 111646897(xdh)
HCQ: 109510392(xdh)
BPEC: 110166494(xdh)
SASA: 100380763(xdh)
OTW: 112262239
SALP: 112071841
ELS: 105031569(xdh)
SFM: 108923027(xdh)
PKI: 111834729(xdh)
CMK: 103182679 103187630(xdh)
RTP: 109913754(xdh) 109930681
DSI: Dsimw501_GD18875(Dsim_ry) Dsimw501_GD20335(Dsim_GD20335) Dsimw501_GD20336(Dsim_GD20336) Dsimw501_GD20337(Dsim_GD20337) Dsimw501_GD20338(Dsim_GD20338)
DPA: 109536954
API: 100169249
DNX: 107172284
AGS: 114119532
RMD: 113550991
CEL: CELE_F55B11.1(xdh-1)
ATH: AT4G34890(XDH1) AT4G34900(XDH2)
CRB: 17877660
THJ: 104817905
CPAP: 110811823
CIT: 102622737
TCC: 18589817
GRA: 105799411
GAB: 108456712
DZI: 111301841
VRA: 106759191
VAR: 108333356
VUN: 114185523
CAM: 101495267
LJA: Lj3g3v1694660.1(Lj3g3v1694660.1)
ADU: 107461425
LANG: 109351322
FVE: 101298861
RCN: 112202499
PPER: 18780893
PMUM: 103326686
PAVI: 110760280
PXB: 103965536
ZJU: 107412613
CSV: 101211977
CMO: 103492036
MCHA: 111021441
CMAX: 111485375
CMOS: 111461442
CPEP: 111779652
RCU: 8274436
JCU: 105648267
MESC: 110617223
POP: 7467360
PEU: 105126367
JRE: 109003655
VVI: 100248547
SOT: 102596284
CANN: 107853580
NSY: 104224061
NTO: 104111014
NAU: 109241093
INI: 109160132
SIND: 105163571
OEU: 111404472
HAN: 110866903
CCAV: 112511831
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
PDA: 103715913
EGU: 105056188
MUS: 103989027
DCT: 110115026
PEQ: 110018507
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)
ARA: Arad_9877
SACI: Sinac_0251
FJG: BB050_03475(xdhA_2)
 » show all
Reference
PMID:8224915
  Authors
Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T
  Title
Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene.
  Journal
Gene 133:279-84 (1993)
DOI:10.1016/0378-1119(93)90652-J
  Sequence
[hsa:7498]
Reference
  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

KEGG   ENZYME: 1.14.14.1
Entry
EC 1.14.14.1                Enzyme                                 

Name
unspecific monooxygenase;
microsomal monooxygenase;
xenobiotic monooxygenase;
aryl-4-monooxygenase;
aryl hydrocarbon hydroxylase;
microsomal P-450;
flavoprotein-linked monooxygenase;
flavoprotein monooxygenase;
substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
substrate,NADPH---hemoprotein reductase:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
Reaction(IUBMB)
RH + [reduced NADPH---hemoprotein reductase] + O2 = ROH + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R04122]
Reaction(KEGG)
Substrate
RH [CPD:C01371];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
ROH [CPD:C01335];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
A group of P-450 heme-thiolate proteins, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4, NADPH---hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.
History
EC 1.14.14.1 created 1961 as EC 1.99.1.1, transferred 1965 to EC 1.14.1.1, transferred 1972 to EC 1.14.14.1 (EC 1.14.14.2 created 1972, incorporated 1976, EC 1.14.99.8 created 1972, incorporated 1984), modified 2015
Pathway
ec00071  Fatty acid degradation
ec00140  Steroid hormone biosynthesis
ec00232  Caffeine metabolism
ec00380  Tryptophan metabolism
ec00590  Arachidonic acid metabolism
ec00591  Linoleic acid metabolism
ec00627  Aminobenzoate degradation
ec00830  Retinol metabolism
ec00980  Metabolism of xenobiotics by cytochrome P450
ec00982  Drug metabolism - cytochrome P450
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K00490  cytochrome P450 family 4 subfamily F
K07408  cytochrome P450 family 1 subfamily A polypeptide 1
K07409  cytochrome P450 family 1 subfamily A polypeptide 2
K07410  cytochrome P450 family 1 subfamily B polypeptide 1
K07411  cytochrome P450 family 2 subfamily A
K07412  cytochrome P450 family 2 subfamily B
K07413  cytochrome P450 family 2 subfamily C
K07414  cytochrome P450 family 2 subfamily D
K07416  cytochrome P450 family 2 subfamily F
K07418  cytochrome P450 family 2 subfamily J
K07420  cytochrome P450 family 2 subfamily S polypeptide 1
K07424  cytochrome P450 family 3 subfamily A
K07426  cytochrome P450 family 4 subfamily B polypeptide 1
K07428  cytochrome P450 family 4 subfamily X
K07429  cytochrome P450 family 4 subfamily Z
K14338  cytochrome P450 / NADPH-cytochrome P450 reductase
K17684  cytochrome P450 family 2 subfamily A polypeptide 7
K17685  cytochrome P450 family 2 subfamily A polypeptide 13
K17690  cytochrome P450 family 3 subfamily A polypeptide 5
K17691  cytochrome P450 family 3 subfamily A polypeptide 7
K17692  cytochrome P450 family 3 subfamily A polypeptide 43
K17712  cytochrome P450 family 2 subfamily D polypeptide 6
K17718  cytochrome P450 family 2 subfamily C polypeptide 8
K17720  cytochrome P450 family 2 subfamily C polypeptide 18
K17728  cytochrome P450 family 4 subfamily F polypeptide 8
K17729  cytochrome P450 family 4 subfamily F polypeptide 11
K17730  cytochrome P450 family 4 subfamily F polypeptide 12
Genes
HSA: 100861540(CYP3A7-CYP3A51P) 107987478 107987479(CYP2D6) 11283(CYP4F8) 1543(CYP1A1) 1544(CYP1A2) 1545(CYP1B1) 1549(CYP2A7) 1551(CYP3A7) 1553(CYP2A13) 1558(CYP2C8) 1562(CYP2C18) 1564(CYP2D7) 1565(CYP2D6) 1572(CYP2F1) 1573(CYP2J2) 1577(CYP3A5) 1580(CYP4B1) 199974(CYP4Z1) 260293(CYP4X1) 29785(CYP2S1) 57834(CYP4F11) 64816(CYP3A43) 66002(CYP4F12)
PTR: 100614519 100616514(CYP4F11) 101058187 107966456 112206755 450909(CYP2C8) 453744(CYP1A1) 456557(CYP4B1) 456833(CYP4X1) 456834 456896(CYP2J2) 459163(CYP1B1) 468754(CYP4F12) 470228(CYP2D6) 472456(CYP3A43) 735881(CYP1A2) 737263(CYP3A7) 737374(CYP3A5) 738883 739649(CYP2S1) 748442(CYP4F8)
PPS: 100967379 100967578 100969491 100970184 100972566 100974522 100975837 100975985 100976184 100976333 100978561 100979109 100979695 100982833 100983164 100984148 100988273(CYP2D6) 100989599 100994607 100995728 103785103 103785155
GGO: 101126416 101127173 101127384 101127998 101129522 101130358 101134278 101139245 101141065 101142890 101147001 101147010 101147362 101148349 101151604 101152395 101152766 101153230 109025371 115931944 115936030
PON: 100172192(CYP1B1) 100172368(CYP1A2) 100173089(CYP4F12) 100174280(CYP4F11) 100434899 100435763 100436403 100437391 100441499 100442601 100444727 100446370 100447634 100447840 100449185 100452833 100453198 100455064 100456680 100457153 100458527 100458875 100459240
NLE: 100579248 100580051 100580500 100580825 100582281 100583040 100585507 100586622 100589053 100591599 100592711 100593273 100593769 100602226 100606221 100606376 105737754 115830387 115830830
MCC: 100144394(CYP3A7) 100424240(CYP2C76) 100424795 100424965 114674219 678683(CYP2C8) 678686(CYP2C75) 678690(CYP2A23) 678691(CYP2D6) 678692(CYP3A5) 678694(CYP1A1) 678696(CYP2F1) 693631 701855(CYP2C18) 702239 702954(CYP2A26) 705884 709290 709535 709770(CYP3A43) 710385(CYP1B1) 718335(CYP4F8) 718379(CYP4F12) 719353 722086
MCF: 102114994(CYP2C76) 102117212(CYP2C20) 102119662(CYP2J2) 102121341(CYP2A26) 102123758(CYP2A23) 102123985 102125382 102125467 102125667 102129994(CYP1A1) 102130053 102130662(CYP1A2) 102131739(CYP4F12) 102135027(CYP4F11) 102140079(CYP2D44) 102143092(CYP2D17) 102143277 102143360(CYP3A43) 102145015(CYP) 102145601(CYP2C18) 102146134(CYP3A5) 102146810 107126471
CSAB: 103216300(CYP2C18) 103216303(CYP2C8) 103220462(CYP1B1) 103223410 103223412 103224719(CYP2J2) 103224873(CYP4X1) 103224875(CYP4Z1) 103224876(CYP4B1) 103234078 103234083 103234090 103234718 103234724 103235509 103235510 103235511 103245329(CYP1A2) 103245331(CYP1A1) 103246765(CYP3A43) 103246770(CYP3A5) 103246772(CYP3A7)
RRO: 104661011 104661013 104662102 104662104 104664669 104664684 104665592 104668045 104670080 104670158 104672095 104672151 104672152 104673586 104676091 104676095 104676097 104676180 104676181 104680972
CJC: 100385343(CYP2D19) 100389345(CYP2C18) 100390915(CYP2C8) 100391987(CYP2C76) 100392712(CYP1A2) 100393083(CYP1A1) 100395270(CYP1B1) 100397287(CYP2J2) 100398692 100399054(CYP2A6) 100404344(CYP3A4) 100404952(CYP3A5) 100405792(CYP3A90) 100406326(CYP2S1) 100411508(CYP4F12) 100411868(CYP4F11) 100413208(CYP4B1) 100413928(CYP4X1) 100415600(CYP2D8) 100415609(CYP4Z1)
MMU: 100041375(Cyp3a41b) 100066(Cyp2j11) 106648(Cyp4f15) 107141(Cyp2c50) 13076(Cyp1a1) 13077(Cyp1a2) 13078(Cyp1b1) 13085(Cyp2a12) 13086(Cyp2a4) 13087(Cyp2a5) 13088(Cyp2b10) 13089(Cyp2b13) 13090(Cyp2b19) 13094(Cyp2b9) 13095(Cyp2c29) 13096(Cyp2c37) 13097(Cyp2c38) 13098(Cyp2c39) 13099(Cyp2c40) 13101(Cyp2d10) 13105(Cyp2d9) 13107(Cyp2f2) 13109(Cyp2j5) 13110(Cyp2j6) 13112(Cyp3a11) 13113(Cyp3a13) 13114(Cyp3a16) 13120(Cyp4b1) 208285(Cyp4f17) 223706(Cyp2d34) 226105(Cyp2c70) 226143(Cyp2c23) 230459(Cyp2j13) 242546(Cyp2j12) 243881(Cyp2b23) 320997(Cyp4f39) 337924(Cyp3a44) 380997(Cyp2d12) 404195(Cyp2c54) 433247(Cyp2c68) 53973(Cyp3a41a) 545123(Cyp2d11) 56388(Cyp3a25) 56448(Cyp2d22) 631304(Cyp4f40) 665095(Cyp2j8) 677156(Cyp4f37) 69888(Cyp2c66) 70101(Cyp4f16) 71754(Cyp2d40) 72082(Cyp2c55) 72303(Cyp2c65) 74134(Cyp2s1) 74519(Cyp2j9) 76279(Cyp2d26) 81906(Cyp4x1)
RNO: 100910127 100910877 100912642 103691072(CYP2B15) 103691092 108348266 170509(Cyp3a62) 171352(Cyp3a9) 171518(Cyp2c22) 171521(Cyp2c13) 171522(Cyp2d4) 24296(Cyp1a1) 24297(Cyp1a2) 24299(Cyp2a3) 24300(Cyp2b1) 24303(Cyp2d3) 24307(Cyp4b1) 246767(Cyp4x1) 24894(Cyp2a1) 24895(Cyp2a2) 25011(Cyp2c12) 25053(Cyp2d2) 252931(Cyp3a18) 25426(Cyp1b1) 25642(Cyp3a23/3a1) 266682(Cyp3a2) 266684(Cyp2d1) 286904(Cyp4f4) 286905(Cyp4f5) 286953(Cyp2b3) 286963(Cyp2d5) 292728(Cyp2b21) 29277(Cyp2c11) 29295(Cyp2b12) 29298(Cyp2c7) 293989(Cyp2c6v1) 299566(Cyp4f39) 308445(Cyp2s1) 313373(Cyp2j10) 313375(Cyp2j3) 361523(Cyp2b2) 499353(Cyp2c24) 500801(Cyp4f17) 502969(Cyp2j16) 503122(Cyp4f40) 54246(Cyp2f4) 65210(Cyp2j4) 685222(Cyp2b15) 83790(Cyp2c23)
OCU: 100008805(CYP4B1) 100301544(CYP2J1) 100316858(CYP2D24) 100327257(CYP2B4) 100328549(CYP2C5) 100328596(CYP2A11) 100328598(CYP2A10) 100328613(CYP1A1) 100328924(CYP2C2) 100328933(CYP2C) 100328935(CYP2C30) 100328936(CYP2C14) 100328937(CYP1A2) 100328938(CYP2C16) 100328947(CYP2B5) 100328948 100328954(CYP3A6) 100338914 100345193 100346743(CYP2C1) 100349436(CYP2C4) 100353317 100353460 100353574 100353821 100358590 103351405
CFA: 100686778(CYP1A1) 100688697 415120(CYP2D15) 415122(CYP2C18) 415127(CYP3A26) 415129(CYP3A12) 474177(CYP2B6) 482505(CYP4X1) 483038(CYP1B1) 484491(CYP2S1) 484493(CYP2A7) 484494(CYP2A13) 489851 494010(CYP1A2) 608452(CYP4B1) 610195(CYP2J2) 612477
BTA: 100847677 282211(CYP2D14) 282214(CYP3A5) 282870(CYP1A1) 503552(CYP1A2) 504769(CYP2B6) 507988(CYP3A4) 511470(CYP1B1) 511498 511936 514971(CYP2S1) 517246(CYP3A24) 526682(CYP3A5) 530571 530929 535243(CYP2C18) 540149(CYP4B1) 540707 615697 616593(CYP2C87) 785540 785824(MGC127055)
SSC: 100126281(CYP3A46) 100144468(CYP3A22) 100152910(CYP1A2) 100523190 100523909 100524750(CYP2J34) 100524940 100525112 100621407 100625479 100627093 100739741 102165015 106510546 110261221 397687(CYP2D25) 403103(CYP1A1) 403104(CYP2B22) 403106(CYP2C32) 403107(CYP2C33) 403108(CYP2C34) 403110(CYP2C36) 403111(CYP2C42) 403149(CYP2A19) 403215(CYP2C49) 403324(CYP3A29)
GGA: 100858007(RP11-400G3.5) 100859277(CYP4F22) 101750603(CYP2J21) 396051(CYP1A2) 396052(CYP1A1) 414832(CYP3A5) 414833(CYP2C45) 416477(CYP3A4) 417981(CYP2D6) 421466(CYP1B1) 424618(CYP4B7) 424676(CYP2J23) 424677(CYP2J22) 771974(CYP4A22)
XLA: 100036770(cyp2a6.L) 100036771(cyp4b1.2.L) 100036772(cyp4b1.L) 100036775(cyp1a1.L) 100036876(LOC100488227.L) 100037189(cyp3a4) 100337623(cyp1a1.S) 108698626 108699286 108714294 108714295 108714516 108715021 108715777 108715778 108716653(cyp1b1.L) 108717803(cyp1b1.S) 108718493 373549(LOC100487918.L) 379297(cyp2c8.1.S) 379479(cyp2d6-b) 398964 444392 444542(cyp2c8.2.L) 446878(cyp2d6.S) 495363(cyp3a5.L)
XTR: 100037911(cyp1a1) 100145080(cyp4b1) 100145323 100487054 100487846 100487918 100488078 100488227 100488386 100490477(cyp1b1) 100494106 100494419(cyp3a4.2) 100495359 100495518 101731511 116406634 448236(cyp2c8.2) 496407(cyp2a6.9) 496408(cyp2a6.8) 548436(cyp2d6) 548503(cyp3a4.3) 548774(cyp4f2) 550102(cyp4b1.2)
DRE: 100034366(cyp2p8) 100034406(cyp2p7) 100150054(cyp1b1) 140634(cyp1a) 387527(cyp4t8) 553969(cyp3a65) 797309(cyp2j20)
IPU: 100313516(cyp1b) 108258748(CYP3A125) 108258760(cyp3a27) 108258762(CYP3A128) 108258764(CYP3A127) 108264711(cyp1a1) 108269368
OLA: 100125806(cyp1a) 100302452(cyp2p3) 101155406(cyp3a) 101159216 101165838
DMN: 117188691
AME: 727290
HST: 105187605
PGC: 109858307
OBO: 105280474
NVI: 100121599(Cyp303a1)
CSOL: 105360113
MDL: 103580958
TCA: 658783(CYP305A1)
DPA: 109543005
ATD: 109595197
BMOR: 101743283(CYP303A1)
BMAN: 114246377
PMAC: 106717103
PRAP: 111003399
API: 100162206
DNX: 107166593
AGS: 114124824
BTAB: 109029996
OBI: 106870255
EPA: 110232159
CSV: 101207867
CPEP: 111792333
NCR: NCU05185
NTE: NEUTE1DRAFT145879(NEUTE1DRAFT_145879)
MBE: MBM_08168
ANI: AN6835.2
ANG: ANI_1_2654014(An01g06820) ANI_1_396144(An16g02820) ANI_1_622054(An06g02530)
ABE: ARB_05231
TVE: TRV_02270
ZTR: MYCGRDRAFT_100796(CYP-40) MYCGRDRAFT_70343(CYP-50)
ABP: AGABI1DRAFT122003(AGABI1DRAFT_122003) AGABI1DRAFT93343(AGABI1DRAFT_93343)
ABV: AGABI2DRAFT188118(AGABI2DRAFT_188118)
DFA: DFA_07281(CYP513C1) DFA_10184
PCT: PC1_0268
RPI: Rpic_4258
REH: H16_B1009(h16_B1009)
CNC: CNE_2c09660(cypE)
RME: Rmet_3467
BCEO: I35_5939
BCED: DM42_5902
BCON: NL30_31780
BPSL: WS57_03680
BJA: blr2882
BRS: S23_51340
BRAD: BF49_1812
RPB: RPB_3645
RPD: RPD_1820
VGO: GJW-30_1_03917(cypE)
ELI: ELI_00100
BSU: BSU07250(yetO) BSU27160(cypB)
BSH: BSU6051_07250(yetO) BSU6051_27160(cypB)
BSUT: BSUB_00799(yetO) BSUB_02898(cypB)
BSUL: BSUA_00799(yetO) BSUA_02898(cypB)
BSS: BSUW23_03690(cypD) BSUW23_13125(cypB)
BSQ: B657_07250(cypD) B657_27160(cypB)
BSX: C663_0751(cypD) C663_2550(cypE)
BLI: BL02398(cypE)
BLD: BLi02848(yrhJ)
BLH: BaLi_c29470(cypB)
BAQ: BACAU_0708(yetO) BACAU_2438(yrhJ)
BYA: BANAU_0661(yetO) BANAU_2583(yrhJ)
BAML: BAM5036_0659(cypD) BAM5036_2365(cypB)
BAMA: RBAU_0722(cypD) RBAU_2563(cypB)
BAMN: BASU_0699(cypD) BASU_2369(cypB)
BAMB: BAPNAU_0670(YetO) BAPNAU_1137(yrhJ)
BAMY: V529_06850(yetO) V529_27090(yrhJ)
BAO: BAMF_0695(yetO) BAMF_2522(cypB)
BAZ: BAMTA208_03280(yetO) BAMTA208_13325(cypB)
BQL: LL3_00745(yetO) LL3_02800(yrhJ)
BXH: BAXH7_00690(yetO) BAXH7_02724(yrhJ)
BQY: MUS_0726(yetO) MUS_2901(yrhJ)
BAN: BA_3221(cypD)
BAR: GBAA_3221(cypD)
BAT: BAS2993
BAH: BAMEG_1392(cypD)
BAI: BAA_3269(cypD)
BANT: A16_32460
BANR: A16R_32890
BANS: BAPAT_3089
BANV: DJ46_1971(cyp102A1)
BCE: BC3211
BCA: BCE_3239(cypD)
BCR: BCAH187_A3250(cypD)
BCB: BCB4264_A3231(cypD)
BCU: BCAH820_3229(cypD)
BCG: BCG9842_B2016(cypD)
BCQ: BCQ_3034(cypD)
BCX: BCA_3251(cypD)
BNC: BCN_3047
BCF: bcf_15685
BCER: BCK_18985
BTL: BALH_2868
BTB: BMB171_C2898(cypD)
BTT: HD73_2783
BTHI: BTK_13800
BTC: CT43_CH3164(cypD)
BTM: MC28_2359
BTG: BTB_c32980(cypD)
BTI: BTG_03315
BTW: BF38_4372(cyp102A1)
BWW: bwei_1841(cypD)
BMYC: DJ92_5480(cyp102A1)
BTRO: FJR70_03215(cypD)
BPU: BPUM_1680
BPUM: BW16_09260
BPUS: UP12_08650
BMQ: BMQ_3237
BMD: BMD_3248
BMH: BMWSH_1945(cypD)
BMEG: BG04_163(cYP102a1)
BACW: QR42_08590
BACL: BS34A_08250(yetO) BS34A_29630(cypB)
BEO: BEH_16435
BGY: BGLY_3163
PPO: PPM_3514(M1_3883)
PPOL: X809_33460
PPQ: PPSQR21_035110(cysJ)
PPOY: RE92_19680
PMS: KNP414_03453(cypD)
PMW: B2K_06870
PSWU: SY83_13600
ASOC: CB4_02158(cypE)
MCHE: BB28_22565
MSTE: MSTE_04573
MMIN: MMIN_05950
SMA: SAVERM_575(cyp2)
SCB: SCAB_5931
SCT: SCAT_4838(CYP102A)
SHY: SHJG_8055
SDV: BN159_1745(cypD)
SALU: DC74_6871
SALL: SAZ_35695
STRE: GZL_01897
SLD: T261_1104
STRM: M444_30060
SLE: sle_05650(sle_05650)
SALJ: SMD11_0205(cypD_E)
SRO: Sros_6421
SEN: SACE_4205(cypD)
PDX: Psed_5892
PSEE: FRP1_10540
KAL: KALB_657
HAU: Haur_2522
DGO: DGo_PB0521(cypD)
SACI: Sinac_6636
PBOR: BSF38_00176(cypB)
SGN: SGRA_1002
 » show all
Reference
1  [PMID:13426111]
  Authors
BOOTH J, BOYLAND E.
  Title
The biochemistry of aromatic amines.  III.  Enzymic hydroxylation by rat-liver microsomes.
  Journal
Biochem J 66:73-8 (1957)
DOI:10.1042/bj0660073
Reference
2  [PMID:5132997]
  Authors
Fujita T, Mannering GJ.
  Title
Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene.
  Journal
Chem Biol Interact 3:264-5 (1971)
DOI:10.1016/0009-2797(71)90053-6
Reference
3  [PMID:187601]
  Authors
Haugen DA, Coon MJ.
  Title
Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450.
  Journal
J Biol Chem 251:7929-39 (1976)
Reference
4  [PMID:3415241]
  Authors
Imaoka S, Inoue K, Funae Y.
  Title
Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography.
  Journal
Arch Biochem Biophys 265:159-70 (1988)
DOI:10.1016/0003-9861(88)90381-5
Reference
5  [PMID:434823]
  Authors
Johnson EF, Zounes MC, Muller-Eberhard U.
  Title
Characterization of three forms of rabbit microsomal cytochrome P-450 by peptide mapping utilizing limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
  Journal
Arch Biochem Biophys 192:282-9 (1979)
DOI:10.1016/0003-9861(79)90093-6
Reference
6  [PMID:489601]
  Authors
Kupfer D, Miranda GK, Navarro J, Piccolo DE, Theoharides AD.
  Title
Effect of inducers and inhibitors of monooxygenase on the hydroxylation of prostaglandins in the guinea pig. Evidence for several monooxygenases catalyzing omega- and omega-1-hydroxylation.
  Journal
J Biol Chem 254:10405-14 (1979)
Reference
7  [PMID:7298645]
  Authors
Lang MA, Gielen JE, Nebert DW.
  Title
Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice.
  Journal
J Biol Chem 256:12068-75 (1981)
Reference
8  [PMID:7298644]
  Authors
Lang MA, Nebert DW.
  Title
Structural gene products of the Ah locus. Evidence for many unique P-450-mediated monooxygenase activities reconstituted from 3-methylcholanthrene-treated C57BL/6N mouse liver microsomes.
  Journal
J Biol Chem 256:12058-67 (1981)
Reference
9  [PMID:2916844]
  Authors
Leo MA, Lasker JM, Raucy JL, Kim CI, Black M, Lieber CS.
  Title
Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8.
  Journal
Arch Biochem Biophys 269:305-12 (1989)
DOI:10.1016/0003-9861(89)90112-4
Reference
10 [PMID:4401153]
  Authors
Lu AY, Kuntzman R, West S, Jacobson M, Conney AH.
  Title
Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. II. Role of the cytochrome P-450 and P-448 fractions in drug and steroid hydroxylations.
  Journal
J Biol Chem 247:1727-34 (1972)
Reference
11 [PMID:13314626]
  Authors
MITOMA C, POSNER HS, REITZ HC, UDENFRIEND S.
  Title
Enzymatic hydroxylation of aromatic compounds.
  Journal
Arch Biochem Biophys 61:431-41 (1956)
DOI:10.1016/0003-9861(56)90366-6
Reference
12
  Authors
Mitoma, C. and Udenfriend, S.
  Title
Aryl-4-hydroxylase.
  Journal
Methods Enzymol 5:816-819 (1962)
Reference
13 [PMID:7295706]
  Authors
Napoli JL, Okita RT, Masters BS, Horst RL.
  Title
Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite.
  Journal
Biochemistry 20:5865-71 (1981)
DOI:10.1021/bi00523a033
Reference
14 [PMID:4387094]
  Authors
Nebert DW, Gelboin HV.
  Title
Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme.
  Journal
J Biol Chem 243:6242-9 (1968)
Reference
15 [PMID:3264134]
  Authors
Suhara K, Ohashi K, Takahashi K, Katagiri M.
  Title
Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)beta.
  Journal
Arch Biochem Biophys 267:31-7 (1988)
DOI:10.1016/0003-9861(88)90004-5
Reference
16 [PMID:7462235]
  Authors
Theoharides AD, Kupfer D.
  Title
Evidence for different hepatic microsomal monooxygenases catalyzing omega- and (omega-1)-hydroxylations of prostaglandins E1 and E2. Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation.
  Journal
J Biol Chem 256:2168-75 (1981)
Reference
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  Authors
Thomas PE, Lu AY, Ryan D, West SB, Kawalek J, Levin W.
  Title
Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448.
  Journal
Mol Pharmacol 12:746-58 (1976)
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.1
IUBMB Enzyme Nomenclature: 1.14.14.1
ExPASy - ENZYME nomenclature database: 1.14.14.1
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.14.1
BRENDA, the Enzyme Database: 1.14.14.1
CAS: 9038-14-6

KEGG   ENZYME: 1.17.3.2
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
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)
MCAL: 110312137(Xdh)
MPAH: 110335495(Xdh)
RNO: 497811(Xdh)
MUN: 110557067(Xdh)
CGE: 100766626(Xdh)
NGI: 103748365(Xdh)
HGL: 101708017(Xdh)
CCAN: 109701710(Xdh)
OCU: 100144327(XDH)
TUP: 102477455(XDH)
CFA: 483028(XDH)
VVP: 112933009(XDH)
AML: 100465942(XDH)
UMR: 103671606(XDH)
UAH: 113240940(XDH)
ORO: 101376175(XDH)
ELK: 111154104
FCA: 105259797 493692(XDH)
PTG: 102969928
PPAD: 109261405 109262396(XDH)
AJU: 106967886(XDH)
BTA: 280960(XDH)
BOM: 102264420(XDH)
BIU: 109565958(XDH)
BBUB: 102406968(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)
DLE: 111174909(XDH)
PCAD: 102980160(XDH)
MYB: 102262378(XDH)
MYD: 102773370(XDH)
MNA: 107541765(XDH)
HAI: 109395899
DRO: 112297809(XDH)
PALE: 102884734(XDH)
RAY: 107505738(XDH)
MJV: 108404078(XDH)
LAV: 100672640(XDH)
TMU: 101349074
MDO: 100031481(XDH)
SHR: 100933358(XDH)
PCW: 110198166(XDH)
GGA: 396025(XDH)
MGP: 100544067(XDH)
CJO: 107310773(XDH)
NMEL: 110395607(XDH)
APLA: 101799192(XDH)
ACYG: 106031596(XDH)
TGU: 100222890(XDH)
LSR: 110473976(XDH)
SCAN: 103821303(XDH)
GFR: 102040336(XDH)
FAB: 101819038(XDH)
PHI: 102106931(XDH)
PMAJ: 107201507(XDH)
CCAE: 111926289(XDH)
CCW: 104685575(XDH)
ETL: 114073409(XDH)
FPG: 101918653(XDH)
FCH: 102052812(XDH)
CLV: 102092037(XDH)
EGZ: 104134615(XDH)
NNI: 104019267(XDH)
ACUN: 113478412(XDH)
PADL: 103925004(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)
PMUR: 107297206(XDH)
TSR: 106538731(XDH)
PMUA: 114594599(XDH)
GJA: 107112582(XDH)
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)
PHYP: 113533982(xdh)
AMEX: 103031284(xdh)
EEE: 113583665(xdh)
TRU: 101073141(xdh)
LCO: 104938633
MZE: 101478907(xdh)
ONL: 100706331(xdh)
OLA: 101162508(xdh)
XMA: 102231285(xdh)
XCO: 114140507(xdh)
PRET: 103481416(xdh)
CVG: 107104320(xdh)
NFU: 107384577(xdh)
KMR: 108251278(xdh)
ALIM: 106531265(xdh)
AOCE: 111587270(xdh)
CSEM: 103389795(xdh)
LCF: 108877173(xdh)
SDU: 111235538(xdh)
SLAL: 111646897(xdh)
HCQ: 109510392(xdh)
BPEC: 110166494(xdh)
SASA: 100380763(xdh)
OTW: 112262239
SALP: 112071841
ELS: 105031569(xdh)
SFM: 108923027(xdh)
PKI: 111834729(xdh)
CMK: 103182679 103187630(xdh)
RTP: 109913754(xdh) 109930681
DSI: Dsimw501_GD18875(Dsim_ry) Dsimw501_GD20335(Dsim_GD20335) Dsimw501_GD20336(Dsim_GD20336) Dsimw501_GD20337(Dsim_GD20337) Dsimw501_GD20338(Dsim_GD20338)
DPA: 109536954
API: 100169249
DNX: 107172284
AGS: 114119532
RMD: 113550991
CEL: CELE_F55B11.1(xdh-1)
ATH: AT4G34890(XDH1) AT4G34900(XDH2)
CRB: 17877660
THJ: 104817905
CPAP: 110811823
CIT: 102622737
TCC: 18589817
GRA: 105799411
GAB: 108456712
DZI: 111301841
VRA: 106759191
VAR: 108333356
VUN: 114185523
CAM: 101495267
LJA: Lj3g3v1694660.1(Lj3g3v1694660.1)
ADU: 107461425
LANG: 109351322
FVE: 101298861
RCN: 112202499
PPER: 18780893
PMUM: 103326686
PAVI: 110760280
PXB: 103965536
ZJU: 107412613
CSV: 101211977
CMO: 103492036
MCHA: 111021441
CMAX: 111485375
CMOS: 111461442
CPEP: 111779652
RCU: 8274436
JCU: 105648267
MESC: 110617223
POP: 7467360
PEU: 105126367
JRE: 109003655
VVI: 100248547
SOT: 102596284
CANN: 107853580
NSY: 104224061
NTO: 104111014
NAU: 109241093
INI: 109160132
SIND: 105163571
OEU: 111404472
HAN: 110866903
CCAV: 112511831
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
PDA: 103715913
EGU: 105056188
MUS: 103989027
DCT: 110115026
PEQ: 110018507
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)
ARA: Arad_9877
SACI: Sinac_0251
FJG: BB050_03475(xdhA_2)
 » show all
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)
DOI:10.1042/bj2070133
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)
DOI:10.1042/bj1260739
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)
DOI:10.1007/978-1-4684-5676-9_27
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)
DOI:10.1107/S0907444900012890
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

KEGG   REACTION: R07945
Entry
R07945                      Reaction                               

Definition
1,7-Dimethylxanthine <=> 1,7-Dimethyluric acid
Equation
Comment
CYP2A6, CYP1A2
Reaction class
RC02017  C13747_C16356
Enzyme
1.14.13.-       1.14.14.1
Pathway
rn00232  Caffeine metabolism
rn01100  Metabolic pathways
Orthology
K07409  cytochrome P450 family 1 subfamily A polypeptide 2 [EC:1.14.14.1]
K17683  cytochrome P450 family 2 subfamily A polypeptide 6 [EC:1.14.13.-]

KEGG   REACTION: R07977
Entry
R07977                      Reaction                               

Name
1,7-dimethylxanthine:oxygen oxidoreductase
Definition
1,7-Dimethylxanthine + Oxygen + H2O <=> 1,7-Dimethyluric acid + Hydrogen peroxide
Equation
Reaction class
RC02017  C13747_C16356
RC02755  C00007_C00027
Enzyme
Pathway
rn00232  Caffeine metabolism
rn01100  Metabolic pathways
rn01110  Biosynthesis of secondary metabolites
Orthology
K00106  xanthine dehydrogenase/oxidase [EC:1.17.1.4 1.17.3.2]

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