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: K21723
Entry
K21723                      KO                                     

Name
ndmB
Definition
methylxanthine N3-demethylase [EC:1.14.13.179]
Pathway
ko00232  Caffeine metabolism
ko01100  Metabolic pathways
ko01110  Biosynthesis of secondary metabolites
ko01120  Microbial metabolism in diverse environments
Module
M00915  Caffeine degradation, caffeine => xanthine
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09110 Biosynthesis of other secondary metabolites
   00232 Caffeine metabolism
    K21723  ndmB; methylxanthine N3-demethylase
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
    1.14.13.179  methylxanthine N3-demethylase
     K21723  ndmB; methylxanthine N3-demethylase
Other DBs
RN: R07939 R07954 R07961 R07962 R07967 R07968 R07975 R07976
COG: COG4638
Genes
PCAF: DSC91_007650
MMS: mma_0224
AG: AFD03117(ndmB)
Reference
  Authors
Summers RM, Louie TM, Yu CL, Gakhar L, Louie KC, Subramanian M
  Title
Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids.
  Journal
J Bacteriol 194:2041-9 (2012)
DOI:10.1128/JB.06637-11
  Sequence

KEGG   ENZYME: 1.14.13.179
Entry
EC 1.14.13.179              Enzyme                                 

Name
methylxanthine N3-demethylase;
ndmB (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
theobromine:oxygen oxidoreductase (N3-demethylating)
Reaction(IUBMB)
(1) theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde [RN:R07961 R07962];
(2) 3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde [RN:R07967 R07968]
Reaction(KEGG)
Substrate
theobromine [CPD:C07480];
O2 [CPD:C00007];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
3-methylxanthine [CPD:C16357]
Product
7-methylxanthine [CPD:C16353];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
formaldehyde [CPD:C00067];
xanthine [CPD:C00385]
Comment
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, methylxanthine N1-demethylase, and has higher activity with NADH than with NADPH [1]. Also demethylates caffeine and theophylline with lower efficiency. Forms part of the degradation pathway of methylxanthines.
History
EC 1.14.13.179 created 2013
Pathway
ec00232  Caffeine metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K21723  methylxanthine N3-demethylase
Genes
PCAF: DSC91_007650
MMS: mma_0224
Reference
1  [PMID:20966097]
  Authors
Summers RM, Louie TM, Yu CL, Subramanian M
  Title
Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source.
  Journal
Microbiology 157:583-92 (2011)
DOI:10.1099/mic.0.043612-0
  Sequence
Reference
2  [PMID:22328667]
  Authors
Summers RM, Louie TM, Yu CL, Gakhar L, Louie KC, Subramanian M
  Title
Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids.
  Journal
J Bacteriol 194:2041-9 (2012)
DOI:10.1128/JB.06637-11
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.179
IUBMB Enzyme Nomenclature: 1.14.13.179
ExPASy - ENZYME nomenclature database: 1.14.13.179
BRENDA, the Enzyme Database: 1.14.13.179

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
17 [PMID:825720]
  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   REACTION: R07939
Entry
R07939                      Reaction                               

Name
caffeine:oxygen oxidoreductase (N3-demethylating)
Definition
Caffeine + NADPH + Oxygen + H+ <=> 1,7-Dimethylxanthine + NADP+ + Formaldehyde + H2O
Equation
Comment
CYP1A2
Reaction class
RC00001  C00005_C00006
RC00334  C07481_C13747
RC01797  C00067_C07481
Enzyme
Pathway
rn00232  Caffeine metabolism
rn01100  Metabolic pathways
rn01110  Biosynthesis of secondary metabolites
rn01120  Microbial metabolism in diverse environments
Module
M00915  Caffeine degradation, caffeine => xanthine
Orthology
K07409  cytochrome P450 family 1 subfamily A polypeptide 2 [EC:1.14.14.1]
K21723  methylxanthine N3-demethylase [EC:1.14.13.179]

KEGG   REACTION: R07954
Entry
R07954                      Reaction                               

Name
caffeine:oxygen oxidoreductase (N3-demethylating)
Definition
Caffeine + NADH + H+ + Oxygen <=> 1,7-Dimethylxanthine + NAD+ + Formaldehyde + H2O
Equation
Reaction class
RC00001  C00003_C00004
RC00334  C07481_C13747
RC01797  C00067_C07481
Enzyme
Pathway
rn00232  Caffeine metabolism
rn01100  Metabolic pathways
rn01110  Biosynthesis of secondary metabolites
rn01120  Microbial metabolism in diverse environments
Module
M00915  Caffeine degradation, caffeine => xanthine
Orthology
K21723  methylxanthine N3-demethylase [EC:1.14.13.179]

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