Information on EC 1.14.14.1 - unspecific monooxygenase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.14.14.1
-
RECOMMENDED NAME
GeneOntology No.
unspecific monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
show the reaction diagram
a group of heme-thiolate proteins (P-450), acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; formerly EC 1.14.1.1, EC 1.14.99.8 and EC 1.99.1.1; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups; some of the reactions attributed to EC 1.14.15.3 alkane 1-monooxygenase belong here; together with EC 1.6.2.4 NADPH-ferrihemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH2
-
-
-
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
show the reaction diagram
tetracycline substrates, initial monohydroxylation at position 11a followed by intramolecular cyclization and non-enzymatic breakdown to undefined products
-
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
show the reaction diagram
formation of a resonant network stabilizing the P450s catalytic site and allowing for interaction with substrates
-
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
show the reaction diagram
active site structures and function-structure relationships of CYPS
-
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
show the reaction diagram
catalytic reaction mechanism, structure-function relationship, CYP can oxidize non-nucleophilic substrates, CYP possesses genetic variability that may contribute to inter-individual variability observed for drug metabolism, the first step of CYP is the addition of substrate to the enzyme followed by electron transfer from the flavoprotein NADPH-CYP reductase to the substrate-bound CYP, then electrons flow to the FMN prosthetic group and then sequentially to the CYP to ultimately afford a reactive iron-oxo species, although other peroxy forms of the hemoprotein are proposed also to be oxidants involved in CYP-dependent metabolism
-
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O
show the reaction diagram
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Deamination
-
-
-
-
desulfation
-
-
-
-
epoxidation
-
-
-
-
epoxidation
P14779
-
epoxidation
Gordonia rubripertincta B 276, Gordonia rubripertincta B-276
-
-
-
hydroxylation
-
-
-
-
hydroxylation
P14779
-
N-dealkylation
-
-
-
-
N-oxidation
-
-
-
-
O-dealkylation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction of azo, nitro, N-oxide groups
-
-
-
-
S-dealkylation
-
-
-
-
sulfoxidation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
1,5-anhydrofructose degradation
-
acetone degradation I (to methylglyoxal)
-
Aminobenzoate degradation
-
Arachidonic acid metabolism
-
bupropion degradation
-
Caffeine metabolism
-
Drug metabolism - cytochrome P450
-
Fatty acid degradation
-
Linoleic acid metabolism
-
melatonin degradation I
-
Metabolic pathways
-
Metabolism of xenobiotics by cytochrome P450
-
Microbial metabolism in diverse environments
-
nicotine degradation III
-
nicotine degradation IV
-
Retinol metabolism
-
Steroid hormone biosynthesis
-
Tryptophan metabolism
-
vanillin biosynthesis I
-
SYSTEMATIC NAME
IUBMB Comments
substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
A group of heme-thiolate proteins (P-450), 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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3AH15
-
-
-
-
6 beta-hydroxylase
-
-
-
-
6-beta-testosterone hydroxylase
-
-
-
-
7-alkoxycoumarin O-dealkylase
-
-
Aldehyde oxygenase
-
-
-
-
Arachidonic acid epoxygenase
-
-
-
-
aromatase
-
-
-
-
aromatase
-
-
aryl hydrocarbon hydroxylase
-
-
-
-
aryl-4-monooxygenase
-
-
-
-
Brain aromatase
-
-
-
-
class IV cytochrome P450 monooxygenase
Q52TE7
-
clavine oxidase
-
-
clavine oxidase
Claviceps purpurea P1
-
-
-
CLOA
Claviceps purpurea P1
-
-
-
Clone PF26
-
-
-
-
Clone PF3/46
-
-
-
-
Coumarin 7-hydroxylase
-
-
-
-
Cyp
Aspergillus terreus MTCC 6324
-
-
-
CYP monooxygenase
-
-
CYP102
Q735B3
-
CYP102 monooxygenase
-
-
CYP102A1
Bacillus licheniformis DSM13
-
-
-
CYP102A1
P14779
-
CYP102A1
-
isoform, binds arachidonate more tightly than isoform CYP102B1
CYP102A2
Bacillus licheniformis DSM13
-
-
-
CYP102A3
Bacillus licheniformis DSM13
-
-
-
CYP102A3
-
-
CYP102A7
Bacillus licheniformis DSM13
-
-
-
CYP102B1
-
isoform
CYP106
Q737I9
-
CYP107
Q737F3, Q737J4
-
CYP109
Q735A2
-
CYP116B3
-
-
CYP134
-
-
CYP152
-
-
CYP19
-
-
CYP197
-
-
CYP1A1
-
-
-
-
CYP1A1
A7UDB5
-
CYP1A2
-
-
-
-
CYP1A2
A7UDB6
-
CYP1A2
P04799
-
CYP1A3
-
-
-
-
CYP1B1
-
-
CYP24A1
-
-
CYP27A1
-
-
CYP2A3
-
-
-
-
CYP2A6
-
-
CYP2A6
P11509
-
CYP2B6
-
-
CYP2B6
P20813
-
CYP2C11
P08683
-
CYP2C8
-
-
CYP2C8
P10632
-
CYP2D6
P10635
-
CYP2E1
P05182
-
CYP3A1
P04800
-
CYP3A5
P20815
-
CYP3A7
P24462
-
CYP4502F4
-
-
-
-
CYP4F2
-
-
CYP4F3A
-
-
CYP4F3B
-
-
CYP5035A5
Phanerochaete chrysosporium BKM-F-1767
-
-
-
CYP512H1
Phanerochaete chrysosporium BKM-F-1767
-
-
-
CYP5141D1
Phanerochaete chrysosporium BKM-F-1767
-
-
-
CYP5A1
-
-
CYP63A2
Phanerochaete chrysosporium BKM-F-1767
-
-
-
CYP6B1v1
-
-
CYP6B1V1/CYP6B1V2/ CYP6B1V3
-
-
-
-
CYP6B3V1/CYP6B3V2
-
-
-
-
CYP6B4V1/CYP6B4V2
-
-
-
-
CYP6B5V1
-
-
-
-
CYP714D1
Q5KQH7
-
CYP82E2
Q38Q85
-
CYP82E3
Q38Q84
-
CYP82E4v1
Q38Q86
-
CYP82E4v2
Q38Q87
-
CYP8A1
-
-
CYPIA1
-
-
-
-
CYPIA2
-
-
-
-
CYPIA4
-
-
-
-
CYPIA5
-
-
-
-
CYPIB1
-
-
-
-
CYPIIA1
-
-
-
-
CYPIIA10
-
-
-
-
CYPIIA11
-
-
-
-
CYPIIA12
-
-
-
-
CYPIIA13
-
-
-
-
CYPIIA2
-
-
-
-
CYPIIA3
-
-
-
-
CYPIIA4
-
-
-
-
CYPIIA5
-
-
-
-
CYPIIA6
-
-
-
-
CYPIIA7
-
-
-
-
CYPIIA8
-
-
-
-
CYPIIA9
-
-
-
-
CYPIIB1
-
-
-
-
CYPIIB10
-
-
-
-
CYPIIB11
-
-
-
-
CYPIIB12
-
-
-
-
CYPIIB19
-
-
-
-
CYPIIB2
-
-
-
-
CYPIIB20
-
-
-
-
CYPIIB3
-
-
-
-
CYPIIB4
-
-
-
-
CYPIIB5
-
-
-
-
CYPIIB6
-
-
-
-
CYPIIB9
-
-
-
-
CYPIIC1
-
-
-
-
CYPIIC10
-
-
-
-
CYPIIC11
-
-
-
-
CYPIIC12
-
-
-
-
CYPIIC13
-
-
-
-
CYPIIC14
-
-
-
-
CYPIIC15
-
-
-
-
CYPIIC16
-
-
-
-
CYPIIC17
-
-
-
-
CYPIIC18
-
-
-
-
CYPIIC19
-
-
-
-
CYPIIC2
-
-
-
-
CYPIIC20
-
-
-
-
CYPIIC21
-
-
-
-
CYPIIC22
-
-
-
-
CYPIIC23
-
-
-
-
CYPIIC24
-
-
-
-
CYPIIC25
-
-
-
-
CYPIIC26
-
-
-
-
CYPIIC27
-
-
-
-
CYPIIC28
-
-
-
-
CYPIIC29
-
-
-
-
CYPIIC3
-
-
-
-
CYPIIC30
-
-
-
-
CYPIIC31
-
-
-
-
CYPIIC37
-
-
-
-
CYPIIC38
-
-
-
-
CYPIIC39
-
-
-
-
CYPIIC4
-
-
-
-
CYPIIC40
-
-
-
-
CYPIIC41
-
-
-
-
CYPIIC42
-
-
-
-
CYPIIC5
-
-
-
-
CYPIIC6
-
-
-
-
CYPIIC7
-
-
-
-
CYPIIC8
-
-
-
-
CYPIIC9
-
-
-
-
CYPIID1
-
-
-
-
CYPIID10
-
-
-
-
CYPIID11
-
-
-
-
CYPIID14
-
-
-
-
CYPIID15
-
-
-
-
CYPIID16
-
-
-
-
CYPIID17
-
-
-
-
CYPIID18
-
-
-
-
CYPIID19
-
-
-
-
CYPIID2
-
-
-
-
CYPIID3
-
-
-
-
CYPIID4
-
-
-
-
CYPIID5
-
-
-
-
CYPIID6
-
-
-
-
CYPIID9
-
-
-
-
CYPIIE1
-
-
-
-
CYPIIF1
-
-
-
-
CYPIIF3
-
-
-
-
CYPIIF4
-
-
-
-
CYPIIG1
-
-
-
-
CYPIIH1
-
-
-
-
CYPIIH2
-
-
-
-
CYPIIIA1
-
-
-
-
CYPIIIA10
-
-
-
-
CYPIIIA11
-
-
-
-
CYPIIIA12
-
-
-
-
CYPIIIA13
-
-
-
-
CYPIIIA14
-
-
-
-
CYPIIIA15
-
-
-
-
CYPIIIA16
-
-
-
-
CYPIIIA17
-
-
-
-
CYPIIIA18
-
-
-
-
CYPIIIA19
-
-
-
-
CYPIIIA2
-
-
-
-
CYPIIIA21
-
-
-
-
CYPIIIA24
-
-
-
-
CYPIIIA25
-
-
-
-
CYPIIIA27
-
-
-
-
CYPIIIA28
-
-
-
-
CYPIIIA29
-
-
-
-
CYPIIIA3
-
-
-
-
CYPIIIA30
-
-
-
-
CYPIIIA31
-
-
-
-
CYPIIIA5
-
-
-
-
CYPIIIA6
-
-
-
-
CYPIIIA7
-
-
-
-
CYPIIIA8
-
-
-
-
CYPIIIA9
-
-
-
-
CYPIIJ1
-
-
-
-
CYPIIJ2
-
-
-
-
CYPIIJ3
-
-
-
-
CYPIIJ5
-
-
-
-
CYPIIJ6
-
-
-
-
CYPIIK1
-
-
-
-
CYPIIK3
-
-
-
-
CYPIIK4
-
-
-
-
CYPIIL1
-
-
-
-
CYPIIM1
-
-
-
-
CYPIVA4
-
-
-
-
CYPIVA8
-
-
-
-
CYPIVB1
-
-
-
-
CYPIVC1
-
-
-
-
CYPIVF1
-
-
-
-
CYPIVF11
-
-
-
-
CYPIVF12
-
-
-
-
CYPIVF4
-
-
-
-
CYPIVF5
-
-
-
-
CYPIVF6
-
-
-
-
CYPIVF8
-
-
-
-
CYPVIA1
-
-
-
-
CYPVIB1
-
-
-
-
CYPVIB2
-
-
-
-
CYPVIB4
-
-
-
-
CYPVIB5
-
-
-
-
CYPVIB6
-
-
-
-
CYPVIB7
-
-
-
-
CYPXIX
-
-
-
-
CYPXIXA1
-
-
-
-
CYPXIXA2
-
-
-
-
CYPXIXA3
-
-
-
-
cytochrome P-450 4 enzyme
-
-
cytochrome P-450 BM3
-
-
cytochrome P-450 BM3
-
enzyme contains a P-450 heme domain and an NADPH-cytochrome P-450 reductase flavoprotein domain in a single polypeptide chain
cytochrome P-450 BM3
P14779
-
cytochrome P-450 monooxygenase
-
-
cytochrome P450 2B4
-
-
cytochrome P450 3A
-
-
cytochrome P450 3A4
-
-
cytochrome P450 aromatase
Q2I129
-
cytochrome P450 BM3
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
Aspergillus terreus MTCC 6324
-
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
Claviceps purpurea P1
-
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
P05177, P10632, P10635, P11509, P20813
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
Q38Q84, Q38Q85, Q38Q86, Q38Q87
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
Q5KQH7
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
Phanerochaete chrysosporium BKM-F-1767
-
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
;
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
Solanum tuberosum, Sorghum sp.
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase
-
-
cytochrome P450 monooxygenase 116B3
-
-
cytochrome P450 monooxygenase 2A6
-
-
cytochrome P450 monooxygenase 2C8
-
-
cytochrome P450 monooxygenase 2C9
-
-
cytochrome P450 monooxygenase 3A4
-
-
cytochrome P450 monooxygenase pc-2
Q4G2S2
-
cytochrome P450 monooxygenase pc-2
Phanerochaete chrysosporium BKM-F-1767
Q4G2S2
-
-
cytochrome P450 monooxygenase pc-4
Q4L231
-
cytochrome P450 monooxygenase pc-4
Phanerochaete chrysosporium BKM-F-1767
Q4L231
-
-
cytochrome P450 monooxygenase pc-5
Q4L230
-
cytochrome P450 monooxygenase pc-5
Phanerochaete chrysosporium BKM-F-1767
Q4L230
-
-
cytochrome P450 monooxygenase pc-6
Q4G2S3
-
cytochrome P450 monooxygenase pc-6
Phanerochaete chrysosporium BKM-F-1767
Q4G2S3
-
-
cytochrome P450 monooxygenase PC-foxy1
Q4G2S1
-
cytochrome P450 monooxygenase PC-foxy1
Phanerochaete chrysosporium BKM-F-1767
Q4G2S1
-
-
cytochrome P450 oxidoreductase
-
-
Cytochrome P450-D2
-
-
-
-
cytochrome P450-dependent monooxygenase
-
-
cytochrome P450-dependent monooxygenase
-
-
cytochrome P450-dependent monooxygenase 1A2
-
-
cytochrome P450-monooxygenase
-
-
cytochrome-P450 hydroxylase
-
-
cytochrome-P450 hydroxylase
Xanthophyllomyces dendrorhous VKPM Y2410
-
-
-
DAH1
-
-
-
-
DAH2
-
-
-
-
Debrisoquine 4-hydroxylase
-
-
-
-
DMA N-oxidase
-
-
EC 1.14.1.1
-
-
formerly
-
EC 1.14.14.2
-
-
-
-
EC 1.14.99.8
-
-
formerly
-
EC 1.99.1.1
-
-
formerly
-
Estrogen synthetase
-
-
-
-
EUI
Q5KQH7
-
fatty acid hydroxylase
-
-
flavocytochrome P450BM-3
-
-
flavoprotein monooxygenase
-
-
-
-
flavoprotein-linked monooxygenase
-
-
-
-
FMO3
-, P05177, P10632, P10635, P20813, P20815, P24462
-
GA 16a,17-epoxidase
Q5KQH7
-
GA-deactivating enzyme
Q5KQH7
-
Hepatic cytochrome P-450MC1
-
-
-
-
hepatic mixed-function oxidase
-
-
HLp
-
-
-
-
IIA3
-
-
-
-
Isozyme 3A
-
-
-
-
Laurate omega-1 hydroxylase
-
-
-
-
Lauric acid omega-6-hydroxylase
-
-
-
-
liver cytochrome P450-dependent monooxygenase
-
-
LMC1
-
-
-
-
Mephenytoin 4-hydroxylase
-
-
-
-
microsomal monooxygenase
-
-
-
-
microsomal P-450
-
-
-
-
monooxygenase 3
-, P05177, P10632, P10635, P20813, P20815, P24462
-
multifunctional cytochrome P450 monooxygenase
Q70KH6
-
nicotine oxidase
-
CYP2A6
OLF2
-
-
-
-
Olfactive
-
-
-
-
Os05g0482400 protein
Q5KQH7
-
Ovarian aromatase
-
-
-
-
oxidase IV
-
-
oxygenase, flavoprotein-linked mono-
-
-
-
-
P(3)450
-
-
-
-
P-448
-
-
-
-
P-450 PHPAH1
-
-
-
-
P-450(M-1)
-
-
-
-
P-450-MK2
-
-
-
-
P-450AROM
-
-
-
-
P-450IB
-
-
-
-
P-450IIIAM1
-
-
-
-
P-450MC
-
-
-
-
P-450MP
-
-
-
-
P-450UT
-
-
-
-
P1-88
-
-
-
-
P24
-
-
-
-
P450
-
-
P450 17-alpha
-
-
-
-
P450 19A1
-
-
P450 1A1
-
-
P450 1A2
-
-
P450 1B1
-
-
P450 2A6
-
-
P450 2B6
-
-
P450 2C19
-
-
P450 2C9
-
-
P450 2D-29/2D-35
-
-
-
-
P450 2D6
-
-
P450 2E1
-
-
P450 2J2
-
-
P450 3A4
-
-
P450 4A11
-
-
P450 4F2
-
-
P450 BM3
P14779
-
P450 CM3A-10
-
-
-
-
P450 DUT2
-
-
-
-
P450 FA
-
-
-
-
P450 FI
-
-
-
-
P450 form 3B
-
-
-
-
P450 form HP1
-
-
-
-
P450 HSM1
-
-
-
-
P450 HSM2
-
-
-
-
P450 HSM3
-
-
-
-
P450 HSM4
-
-
-
-
P450 IIB1
-
-
-
-
P450 IIC2
-
-
-
-
P450 LM4
-
-
-
-
P450 LM6
-
-
-
-
P450 LMC2
-
-
-
-
P450 MD
-
-
-
-
P450 monooxygenase
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
P450 monooxygenase
-
-
P450 monooxygenase
Bacillus licheniformis DSM13
-
-
-
P450 monooxygenase
-
-
P450 monooxygenase
Phanerochaete chrysosporium BKM-F-1767
-
-
-
P450 monooxygenase
-
-
P450 MP-12/MP-20
-
-
-
-
P450 P49
-
-
-
-
P450 PB1
-
-
-
-
P450 PB4
-
-
-
-
P450 PBC1
-
-
-
-
P450 PBC2
-
-
-
-
P450 PBC3
-
-
-
-
P450 PBC4
-
-
-
-
P450 PCHP3
-
-
-
-
P450 PCHP7
-
-
-
-
P450 TCDDAA
-
-
-
-
P450 TCDDAHH
-
-
-
-
P450 type B2
-
-
-
-
P450 types B0 and B1
-
-
-
-
P450(I)
-
-
-
-
P450-11A
-
-
-
-
P450-15-alpha
-
-
-
-
P450-15-COH
-
-
-
-
P450-16-alpha
-
-
-
-
P450-254C
-
-
-
-
P450-3C
-
-
-
-
P450-6B/29C
-
-
-
-
P450-A3
-
-
-
-
P450-AFB
-
-
-
-
P450-ALC
-
-
-
-
P450-CMF1A
-
-
-
-
P450-CMF1B
-
-
-
-
P450-CMF2
-
-
-
-
P450-CMF3
-
-
-
-
P450-DB1
-
-
-
-
P450-DB2
-
-
-
-
P450-DB3
-
-
-
-
P450-DB4
-
-
-
-
P450-DB5
-
-
-
-
P450-HFLA
-
-
-
-
P450-HP
-
-
-
-
P450-IIA10
-
-
-
-
P450-IIA11
-
-
-
-
P450-IIA3.1
-
-
-
-
P450-IIA3.2
-
-
-
-
P450-IIA4
-
-
-
-
P450-KP1
-
-
-
-
P450-LM2
-
-
-
-
P450-MC1
-
-
-
-
P450-MC4
-
-
-
-
P450-MK1
-
-
-
-
P450-MKJ1
-
-
-
-
P450-MKMP13
-
-
-
-
P450-MKNF2
-
-
-
-
P450-NMB
-
-
-
-
P450-OLF1
-
-
-
-
P450-OLF3
-
-
-
-
P450-P1
-
-
-
-
P450-P2/P450-P3
-
-
-
-
P450-P3
-
-
-
-
P450-PB1 and P450-PB2
-
-
-
-
P450-PCN1
-
-
-
-
P450-PCN2
-
-
-
-
P450-PCN3
-
-
-
-
P450-PM4
-
-
-
-
P450-PP1
-
-
-
-
P450-PROS2
-
-
-
-
P4501A1
-
-
-
-
P450arom
Q2I129
-
P450CB
-
-
-
-
P450CMEF
-
-
-
-
P450E
-
-
-
-
P450EF
-
-
-
-
P450F
-
-
-
-
P450H
-
-
-
-
P450I
-
-
-
-
P450IIC5
-
-
-
-
P450MT2
-
-
-
-
P450RAP
-
-
-
-
P450RLM6
-
-
-
-
P450s 3A
-
-
P450SMO
-
;
-
P52
-
-
-
-
PB15
-
-
-
-
PHP2
-
-
-
-
PHP3
-
-
-
-
PikC hydroxylase
-
-
Progesterone 21-hydroxylase
-
-
-
-
Prostaglandin omega-hydroxylase
-
-
-
-
PTF1
-
-
-
-
PTF2
-
-
-
-
S-mephenytoin 4-hydroxylase
-
-
-
-
sertraline N-demethylase
-
-
Steroid hormones 7-alpha-hydroxylase
-
-
-
-
StyA/StyB
-
-
StyA/StyB
-
-
-
styrene monooxygenase
-
-
styrene monooxygenase
-
-
-
Testosterone 15-alpha-hydroxylase
-
-
-
-
Testosterone 16-alpha hydroxylase
-
-
-
-
Testosterone 6-beta-hydroxylase
-
-
-
-
Testosterone 7-alpha-hydroxylase
-
-
-
-
xenobiotic monooxygenase
-
-
-
-
monooxygenase P450 BM-3
-
-
additional information
Q38Q84, Q38Q85, Q38Q86, Q38Q87
the enzyme belongs to the CYP82E2 family
additional information
Q5KQH7
EUI Is a member of the CYP714 family
additional information
-
P450SMO belongs to class IV of P450 monooxygenase
additional information
-
P450SMO belongs to class IV of P450 monooxygenase
-
additional information
Q70KH6
the enzyme belongs to the CYP151A group
CAS REGISTRY NUMBER
COMMENTARY
62213-32-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain MTCC 6324
-
-
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324
strain MTCC 6324
-
-
Manually annotated by BRENDA team
strain ATCC 10987
-
-
Manually annotated by BRENDA team
strain ATCC 10987
UniProt
Manually annotated by BRENDA team
strain DSM13
-
-
Manually annotated by BRENDA team
Bacillus licheniformis DSM13
strain DSM13
-
-
Manually annotated by BRENDA team
expression in Escherichia coli BL21 (DE3) using the pET281 expression system
SwissProt
Manually annotated by BRENDA team
isozyme CYP102A3, natural fusion protein consisting of a heme domain and a reductase domain
-
-
Manually annotated by BRENDA team
ATCC 20336, isozymes CYP52A13, CYP52A17
-
-
Manually annotated by BRENDA team
strain P1, gene cloA
-
-
Manually annotated by BRENDA team
Claviceps purpurea P1
strain P1, gene cloA
-
-
Manually annotated by BRENDA team
herbicide-resistant and herbicide-susceptible late watergrass populations
-
-
Manually annotated by BRENDA team
Gordonia rubripertincta B 276
B 276
-
-
Manually annotated by BRENDA team
corn earworm
-
-
Manually annotated by BRENDA team
CYP4A11
-
-
Manually annotated by BRENDA team
expression in Oryza sativa
-
-
Manually annotated by BRENDA team
several isozymes, e.g. CYP4F and CYP4A
-
-
Manually annotated by BRENDA team
sole protogynous freshwater fish found that exhibits an adult sex change from functional females to males
UniProt
Manually annotated by BRENDA team
isozyme Cyp4a12
-
-
Manually annotated by BRENDA team
CYP82E2
SwissProt
Manually annotated by BRENDA team
CYP82E3
SwissProt
Manually annotated by BRENDA team
CYP82E4v1
SwissProt
Manually annotated by BRENDA team
CYP82E4v2; three CYP82E isozymes
SwissProt
Manually annotated by BRENDA team
broomrape, a root parasitic weed often in tobacco plants
-
-
Manually annotated by BRENDA team
ssp. japonica, wild-type strain ZS97, gene eui or OSJNBa0095J22.13
SwissProt
Manually annotated by BRENDA team
black swallowtail caterpillar
-
-
Manually annotated by BRENDA team
cytochrome P450 monooxygenase pc-2; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
cytochrome P450 monooxygenase pc-6; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
fragment of cytochrome P450 monooxygenase pc-4; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
fragment of cytochrome P450 monooxygenase pc-5; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
fragment of cytochrome P450 monooxygenase PC-foxy1; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
strain BKM-F-1767 (ATCC 24725)
-
-
Manually annotated by BRENDA team
strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
cytochrome P450 monooxygenase pc-2; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
cytochrome P450 monooxygenase pc-6; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
fragment of cytochrome P450 monooxygenase pc-4; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
fragment of cytochrome P450 monooxygenase pc-5; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
fragment of cytochrome P450 monooxygenase PC-foxy1; strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
SwissProt
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
strain BKM-F-1767 (ATCC 24725)
-
-
Manually annotated by BRENDA team
Phanerochaete chrysosporium BKM-F-1767
strain BKM-F-1767, ATCC 24725, i.e. Sporotrichum pruinosum
-
-
Manually annotated by BRENDA team
2fold increase in enzyme activity on diet of total parenteral nutrition plus choline
-
-
Manually annotated by BRENDA team
isozyme CYP4A1
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
several isozymes, e.g. CYP4F and CYP4A, 9-week-old, male Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
strain DSM 44319
SwissProt
Manually annotated by BRENDA team
strain ECU0066
-
-
Manually annotated by BRENDA team
strain ECU0066
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
several strains, Ema genes
-
-
Manually annotated by BRENDA team
strains R-922 and I-1529, ema genes, and genes cyp229 and cyp230
-
-
Manually annotated by BRENDA team
strain ATCC 15439
-
-
Manually annotated by BRENDA team
wild-type strains ATCC 24203, ATCC 96594, and ATCC 96815, and astaxanthin-overproducing recombinant strains VKPM and Y2410, gene crtS
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
Y459H and V492E mutant POR alleles severely hinder the CYP1A2-mediated bioactivation of the three pro-carcinogens 2-aminoanthracene, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone and 2-amino-3-methylimidazo(4,5-f)quinoline
physiological function
-
essential role of P450 monooxygenase(s) in nonylphenol degradation under nutrient-rich conditions
physiological function
-
chimeric P450cam-RhFRed reductase domain enzyme shows improved biotransformation of 80% conversion at 30 mM substrate concentration
physiological function
-
CYP2E1 and sulfotransferase SULT1A1 activate an endogenous cellular molecule or a medium component to become mutagenic
physiological function
-
P450 1B1 is able to activate a broad spectrum of chemical carcinogens, including polycyclic hydrocarbons and heterocyclic and aromatic amines
physiological function
-
for all genotype combinations tested, the mosquitoe exhibits multiplicative interactions between kdr and P450 detoxification, whether the resistance alleles are homozygous or heterozygous
physiological function
-
differences in the activity of both CYP3A4 and CYP3A5 in Koreans, Swedes and Tanzanians. Both 4beta-hydroxycholesterol and quinine/3-hydroxyquinine metabolic ratio show a higher CYP3A activity in women than in men
physiological function
-
circadian regulation of cytochrome P450 monooxygenases in phenylpropanoid, carotenoid, oxylipin, glucosinolate, and brassinosteroid biosyntheses, both P450 and non-P450 genes in the many branches of the phenylpropanoid pathway have similar circadian patterns of expression
physiological function
-
isoform CYP102B1 is not required for normal cell growth and secondary metabolite productio
physiological function
Q70KH6
AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin
physiological function
Phanerochaete chrysosporium BKM-F-1767
-
essential role of P450 monooxygenase(s) in nonylphenol degradation under nutrient-rich conditions
-
metabolism
-
cytochrome P450-dependent metabolism of omega-6 polyunsaturated fatty acids, overview
additional information
-
loss of CYP3A4 activity may result in increased risk of drug toxicities and adverse drug reactions in patients with NADPH-P450 reductase mutations
additional information
-
multifunctional properties of versatile P450s from the basidiomycete
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-camphor + O2 + H+ + NADPH
(+)-exo-5-hydroxycamphor + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
(-)-alpha-pinene + NADPH + O2
myrtenol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + NADPH + O2
myrtenol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + NADPH + O2
pinene oxide + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87G/L188Q
mutant A74G/F87V/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + NADPH + O2
pinene oxide + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + NADPH + O2
pinene oxide + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/L188Q
mutant A74G/L188Q, 85% pinene oxide, 15% verbenol
-
?
(-)-alpha-pinene + NADPH + O2
verbenol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 13% pinene oxide, 77% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + NADPH + O2
verbenol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 70% pinene oxide, 20% verbenol, 10% myrtenol
-
?
(-)-alpha-pinene + NADPH + O2
verbenol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/L188Q
mutant A74G/L188Q, 85% pinene oxide, 15% verbenol
-
?
(-)-beta-pinene + NADPH + O2
myrtanal + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 40% pino-carveol, 60% myrtanal
-
?
(-)-beta-pinene + NADPH + O2
myrtanal + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 68% pino-carveol, 32% myrtanal
-
?
(-)-beta-pinene + NADPH + O2
pino-carveol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87G/L188Q
mutant A74G/F87G/L188Q, 40% pino-carveol, 60% myrtanal
-
?
(-)-beta-pinene + NADPH + O2
pino-carveol + NADP+ + H2O
show the reaction diagram
P14779
mutant A74G/F87V/L188Q
mutant A74G/F87V/L188Q, 68% pino-carveol, 32% myrtanal
-
?
(R)-(+)-limonene + O2 + NADPH
(R)-cis-1,2-limonene epoxide + cis-carveol
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis DSM13
-
CYP102A7, high activity
-
-
?
(S)-(-)-limonene + O2 + NADPH
(S)-trans-1,2 limonene epoxide
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis DSM13
-
CYP102A7, high activity
-
-
?
(S)-nicotine + O2 + NADPH
?
show the reaction diagram
-
substrate of CYP3A4, the reaction involves electron transfer via FMN
-
-
?
10,11-epoxymethylfarnesoate + O2 + NADPH
?
show the reaction diagram
-
the major product of C(78-82,F87L,328-330) during 10,11-epoxymethylfarnesoate oxidation is determined to be the 12-hydroxy isomer
-
-
?
10-p-nitrophenoxydecanoic acid + NADPH
?
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis DSM13
-
CYP102A7
-
-
?
11-ketoprogesterone + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
12-methyl-myristic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
12-methyl-tetradecanoic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
13-methyl-myristic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
13-methyl-tetradecanoic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine + NADH + H+ + O2
?
show the reaction diagram
-
CYP1A2 catalyzes the first step of activation of the xenobiotic compound and its genotoxic effect, the second step is catalyzed by the sulfotransferase 1A1-1
-
-
?
2-amino-3-methylimidazo[4,5-f]quinoline + NADH + H+ + O2
?
show the reaction diagram
-
CYP1A2 catalyzes the first step of activation of the xenobiotic compound and its genotoxic effect, the second step is catalyzed by the N(O)-acetyltransferase.
-
-
?
2-hydroxy-1-(4-hydroxyphenyl)guanidine + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
3,7-dimethyl-1-octanol + O2 + NADPH
6-hydroxy-3,7-dimethyl-1-octanol + H2O
show the reaction diagram
-
-
-
-
?
3-cyano-7-ethoxycoumarin + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
-
-
-
?
3-cyano-7-ethoxycoumarin + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
CYP2C19
-
-
?
3-[2-(N,N-diethyl-N-methylammonium)ethyl]-7-methoxy-4-methylcoumarin + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
-
-
-
?
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + O2 + reduced flavoprotein
?
show the reaction diagram
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products, nicotine oxidase activity of CYP2A6
-
-
?
4-chlorostyrene + NADH + H+ + O2
4-chlorostyrene oxide + NAD+ + H2O
show the reaction diagram
-
catalyzed by StyA of Pseudomonas sp. VLB120 and electrochemical FAD reduction
-
-
?
4-chlorothioanisole + NADPH + H+ + O2
4-chlorothioanisole sulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
4-fluorothioanisole + NADPH + H+ + O2
4-fluorothioanisole sulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
4-methoxythioanisole + NADPH + H+ + O2
4-methoxythioanisole sulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
4-methylstyrene + NADH + H+ + O2
4-methylstyrene oxide + NAD+ + H2O
show the reaction diagram
-
catalyzed by StyA of Pseudomonas sp. VLB120 and electrochemical FAD reduction
-
-
?
4-tolylmethylsulfide + NADPH + H+ + O2
4-tolylmethylsulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
6beta-hydroxytestosterone + O2 + NADPH
?
show the reaction diagram
P04799, P04800, P05182, P08683
-
-
-
?
7-ethoxy-4-trifluoromethylcoumarin + NADPH + H+ + O2
ethane + 7-hydroxy-4-trifluoromethylcoumarin + NADP+ + H2O
show the reaction diagram
-
CYP1A2 cooperates with NADPH-cytochrome P450 reductase, which provides NADPH for the reaction. Interaction with their redox partner, NADPH-cytochrome P450 reductase, i.e. CPR, in a 1:1 molar ratio
-
-
?
7-ethoxy-trifluoromethylcoumarin + O2 + NADPH
?
show the reaction diagram
-
O-deethylation
-
-
?
7-ethoxycoumarin + 3 NADH + 3 H+ + O2
ethane + 7-hydroxycoumarin + 3 NAD+ + 2 H2O
show the reaction diagram
-
-
-
-
?
7-ethoxycoumarin + NADPH + O2 + FAD
7-hydroxycoumarin + NADP+ + FADH2 + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + NADPH + O2 + FAD
7-hydroxycoumarin + NADP+ + FADH2 + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + NADPH + O2 + reduced flavin
?
show the reaction diagram
-
-
-
-
?
7-ethoxycoumarin + O2 + NAD(P)H + cytochrome c
7-hydroxycoumarin + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
O-dealkylation
-
-
?
7-ethoxycoumarin + O2 + NADPH
?
show the reaction diagram
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxycoumarin + O2 + NADPH
7-hydroxycoumarin + NADP+ + H2O
show the reaction diagram
-
CYP102A7 catalyses dealkylation, although with activity much lower than towards fatty acids
-
-
?
7-ethoxycoumarin + O2 + NADPH
7-hydroxycoumarin + NADP+ + H2O
show the reaction diagram
-
mediates the O-dealkylation
-
-
?
7-ethoxyresorufin + NADPH + H+ + O2
ethane + 7-hydroxyresofurin + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
7-ethoxyresorufin + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
7-ethoxyresorufin + O2 + NADPH
?
show the reaction diagram
P05177
-
-
-
?
7-ethoxyresorufin + O2 + NADPH
?
show the reaction diagram
P04799, P04800, P05182, P08683
-
-
-
?
7-ethoxyresorufin + O2 + NADPH
?
show the reaction diagram
-
7-ethoxyresorufin O-deethylation
-
-
?
7-ethoxyresorufin + O2 + reduced donor
?
show the reaction diagram
-
7-ethoxyresorufin O-deethylation
-
-
?
7-hydroxycoumarin + NADPH + O2 + reduced flavin
?
show the reaction diagram
-
-
-
-
?
7-methoxy-4-(trifluoromethyl)-coumarin + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
-
-
-
?
7-methoxy-4-(trifluoromethyl)-coumarin + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
CYP2C9, CYP2E1
-
-
?
7-methoxycoumarin + 3 NADH + 3 H+ + O2
methane + 7-hydroxycoumarin + 3 NAD+ + 2 H2O
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin + NADPH + O2 + reduced flavin
?
show the reaction diagram
-
-
-
-
?
7-methoxyresorufin + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
7-propoxycoumarin + NADPH + O2 + reduced flavin
?
show the reaction diagram
-
-
-
-
?
acenaphthene + O2 + NAD(P)H + cytochrome c
1-acenaphthenol + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
-
-
-
?
adrenic acid + NADPH + H+ + O2
?
show the reaction diagram
-
i.e. all-cis-7,10,13,16-docosatetraenoic acid
-
-
?
aflatoxin B1 + O2 + NADPH
?
show the reaction diagram
-
-, i.e. AFB1, bioactivation of the carcinogenic mycotoxin to a toxic compound, although not acutely toxic at low concentrations, AFB1 had significant chronic effects, including protracted development, increased mortality, decreased pupation rate, and reduced pupal weight, sensitivity varies with developmental stage, whereas intermediate concentrations causes complete mortality in first instars, this same concentration has no detectable adverse effects on larvae encountering AFB1 in fifth instar. These compounds owe their toxicity to their ability to form irreversible adducts to nucleic acids with the concomitant inhibition of DNA replication and DNA-dependent transcription, mortality, overview
-
-
?
alkene + O2 + reduced flavoprotein
epoxide + H2O + oxidized flavoprotein
show the reaction diagram
Gordonia rubripertincta, Gordonia rubripertincta B-276, Gordonia rubripertincta B 276
-
-
-
-
-
alpha-ionone + O2 + NADPH
?
show the reaction diagram
-
CYP102A7, high activity
-
-
?
aminopyrene + O2 + NADPH
? + formaldehyde + NADP+ + H2O
show the reaction diagram
-
aminopyrene-N-demethylation
-
-
?
aminopyrine + O2 + 2 H+
? + formaldehyde + H2O
show the reaction diagram
-
-
-
-
?
amiprofos-methyl + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
anthraquinone-1,5-disulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity only in roots
-
-
?
anthraquinone-1,5-disulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity only in shoots
-
-
?
anthraquinone-1,8-disulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity only in roots
-
-
?
anthraquinone-1,8-disulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity only in shoots
-
-
?
anthraquinone-1-sulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity in shoots and roots
-
-
?
anthraquinone-1-sulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity only in shoots
-
-
?
anthraquinone-2,6-disulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity in shoots and roots
-
-
?
anthraquinone-2-sulfonic acid + O2 + NADPH
?
show the reaction diagram
-
activity in shoots and roots
-
-
?
arachidonic acid + NADPH + H+ + O2
?
show the reaction diagram
-
-
-
-
?
arachidonic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + 19-hydroxyeicosatetraenoic acid + NADP+ + H2O
show the reaction diagram
-
-
ratio 12:1
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
show the reaction diagram
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
show the reaction diagram
-
-
i.e.20-HETE
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis DSM13
-
CYP102A7
-
-
?
arachidonic acid + O2 + NADPH + H+
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + 11,12-epoxyeicosa-5,8,14-trienoic acid + H2O + NADP+
show the reaction diagram
-
-
reaction products generated by isoform CYP102B1
-
?
arachidonic acid + O2 + NADPH + H+
18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + H2O + NADP+
show the reaction diagram
-
-
reaction products generated by isoform CYP102A1
-
?
aryl hydrocarbons + reduced flavoprotein + O2
?
show the reaction diagram
-
prostaglandins
-
-
-
aryl hydrocarbons + reduced flavoprotein + O2
?
show the reaction diagram
-
e.g. benzo[a]pyrene, ethoxyresuforin, biphenyl, p-nitroanisole, acetanilide, 2-acetylaminofluorene, 2-ethoxycoumarin, estradiol-17beta, testosterone
-
-
-
avermectin + O2 + reduced ferredoxin
4''-oxo-avermectin + H2O + ferredoxin
show the reaction diagram
-
4''-oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin, overview
-
-
?
avermectin + O2 + reduced ferredoxin
4''-oxo-avermectin + H2O + ferredoxin
show the reaction diagram
-
avermectin oxidation activity
-
-
?
bentazon + NADPH + O2 + FAD
?
show the reaction diagram
-
ring-hydroxylation
-
-
?
benzo-pyrene + NADPH + O2 + FAD
?
show the reaction diagram
-
recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
bergapten + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
beta-ionone + O2 + NAD(P)H
4-hydroxy-beta-ionone + H2O + NAD(P)+
show the reaction diagram
-
-
-
-
?
beta-ionone + O2 + NADPH
4-hydroxy-beta-ionone + H2O + NADP+
show the reaction diagram
-
CYP102A7, high activity
-
-
?
beta-ionone + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
substrate only for mutant A74G/F88V/S189Q
-
-
?
bispyribac-sodium + O2 + reduced flavoprotein
?
show the reaction diagram
-
-
-
-
?
capric acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
about 10% of the activity with palmitic acid, wild-type
-
-
?
caprylic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
substrate only for mutant A74G/F88V/S189Q
-
-
?
chlormadinone acetate + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group, recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
ring methyl-hydroxylation
-
-
?
chlorotoluron + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
chlortetracycline + reduced flavoprotein + O2
11a-hydroxy-chlortetracycline + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
chlorzoxazone + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
compactin + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
coumarin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
cytochrome c + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
cytochrome c + O2 + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
decanoic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
demeclocycline + reduced flavoprotein + O2
11a-hydroxy-demeclocycline + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
dibenzylfluorescein + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
-
-
-
?
dibenzylfluorescein + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
CYP3A4, CYP19
-
-
?
diclofop + NADPH + O2 + FAD
?
show the reaction diagram
-
ring-hydroxylation
-
-
?
dihydronaphthalene + NADH + H+ + O2
dihydronaphthalene oxide + NAD+ + H2O
show the reaction diagram
-
catalyzed by StyA of Pseudomonas sp. VLB120 and electrochemical FAD reduction
-
-
?
dimethylaniline + O2 + NADPH
?
show the reaction diagram
-
substrate of CYP3A4
-
-
?
docosahexaenoic acid + NADPH + H+ + O2
22-hydroxydocosahexaenoic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
dodecanoic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
dodecanoic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
isozyme CYP52A17, good substrate
-
-
?
doxycycline + reduced flavoprotein + O2
11a-hydroxy-doxycycline + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
eicosapentaenoic acid + NADPH + H+ + O2
20-hydroxyeicosapentaenoic acid + 19-hydroxyeicosapentaenoic acid + NADP+ + H2O
show the reaction diagram
-
-
ratio 4:3
-
?
eicosapentaenoic acid + NADPH + H+ + O2
20-hydroxyeicosapentaenoic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
eicosapentaenoic acid + NADPH + H+ + O2
20-hydroxyeicosatetraenoic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
eicosenoic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
elymoclavine + O2 + NADPH
paspalic acid + H2O + NADP+
show the reaction diagram
-
-
-, the product is the precursor for D-lysergic acid
-
?
elymoclavine + O2 + NADPH
paspalic acid + H2O + NADP+
show the reaction diagram
Claviceps purpurea P1
-
-
-, the product is the precursor for D-lysergic acid
-
?
erythromycin + O2 + 2 H+
? + formaldehyde + H2O
show the reaction diagram
-
-
-
-
?
ethyl benzene + O2 + NAD(P)H + cytochrome c
1-phenylethyl alcohol + 2-phenylethyl alcohol + + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
recombinant enzyme
-
-
?
ethylmethylsulfide + NADPH + H+ + O2
ethylmethylsulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
farnesol + O2 + NADPH
?
show the reaction diagram
-
CYP102A1 oxidizes farnesol to three products (2,3-epoxyfarnesol, 10,11-epoxyfarnesol, and 9-hydroxyfarnesol), whereas CYP4C7 produces 12-hydroxyfarnesol as the major product. Chimeric proteins C(78-82,F87L) and C(78-82,F87L,328-330) show the most complete change in substrate selectivity from fatty acids to farnesol, and both retain superior enzyme activity with respect to CYP102A1 approximately 5times and approximately 2times greater, respectively. C(78-82,F87L,328-330) produces 12-hydroxyfarnesol as the major metabolite, as does CYP4C7
-
-
?
fenoxaprop-ethyl + O2 + reduced flavoprotein
?
show the reaction diagram
-
-
-
-
?
fenthion + O2 + NADPH
?
show the reaction diagram
P11509
fenthion-sulfoxide and fenthion-oxon, are formed by some CYPs although at very different levels, depending on the relative CYP hepatic content. Fenthion-oxon formation is favored and at low fenthion concentrations CYP2B6 and CYP1A2 are mainly involved in its formation. At higher levels, a more widespread CYP involvement is evident, as in the case of fenthion-sulfoxide
-
-
?
fenthion-sulfoxide + O2 + NADPH
fenthion-sulfone
show the reaction diagram
P11509
CYP1A1, CYP2C9 and CYP3A4 form only traces or negligible levels of fenthion-sulfone, CYP1A2 forms only traces or negligible levels of fenthion-sulfone, CYP2B6 forms only traces or negligible levels of fenthion-sulfone
-
-
?
fluorene + O2 + NAD(P)H + cytochrome c
9-fluorenol + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
-
-
-
?
fluoxetine + O2 + 2 H+
? + formaldehyde + H2O
show the reaction diagram
-
-
-
-
?
geraniol + O2 + NADPH
8-hydroxygeraniol + 10-hydroxygeraniol + H2O
show the reaction diagram
-
-
-
-
?
geranylacetone + O2 + NADPH
9,10-epoxygeranylacetone + 11-hydroxygeranylacetone + 5,6-epoxygeranylacetone
show the reaction diagram
-
CYP102A7, high activity
-
-
?
giberellic acid GA12 + NADPH + O2
16alpha,17-epoxy GA12 + NADP+ + H2O
show the reaction diagram
-, Q5KQH7
-
product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
giberellic acid GA4 + NADPH + H+ + O2
16alpha,17-epoxy GA4 + NADP+ + H2O
show the reaction diagram
-, Q5KQH7
-
the product is transformed further to 16,17-dihydro-16alpha,17-dihydroxy-GA4 in the plant
-
?
giberellic acid GA4 + NADPH + H+ + O2
16alpha,17-epoxy GA4 + NADP+ + H2O
show the reaction diagram
-, Q5KQH7
-
product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
giberellic acid GA9 + NADPH + O2
16alpha,17-epoxy GA9 + NADP+ + H2O
show the reaction diagram
-, Q5KQH7
-
product identification by GC-MS, the epoxid is transformed into 16,17-dihydro-16alpha,17-dihydroxy-GA4 under acidic conditions with acidic acid
-
?
hexadecanoic acid + NADPH
?
show the reaction diagram
-
CYP102A7, highest binding affinity
-
-
?
indene + O2 + NAD(P)H + cytochrome c
indenol + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
-
-
-
?
isopimpinellin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
lauric acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
lauric acid + O2 + NADPH
?
show the reaction diagram
-
products of hydroxylation by wild-type CYP102A1 are 11-OH, 10-OH, 9-OH, 8-OH, 7-OH, and 6-OH, corresponding to omega-1 to omega-6 hydroxylation
-
-
?
lauric acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
linoleic acid + NADPH
?
show the reaction diagram
-
CYP102A1, CYP102A2, CYP102A3 and CYP102A7. CYP102A7 with high binding affinity
-
-
?
linoleic acid + NADPH + H+ + O2
(9Z,12Z)-18-hydroxyoctadeca-9,12-dienoic acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
linoleic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
isozyme CYP52A17, good substrate, isozyme CYP52A13, good substrate
-
-
?
m-xylene + O2 + NAD(P)H + cytochrome c
3-methylbenzyl alcohol + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
recombinant enzyme
-
-
?
macrolide YC-17 + reduced ferredoxin + O2
methymycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
macrolide YC-17 + reduced ferredoxin + O2
neomethymycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
macrolide YC-17 + reduced ferredoxin + O2
novamethymycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
medroxyprogesterone acetate + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
mefenacet + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
methanol + NADPH + O2 + FAD
formaldehyde + NADP+ + H2O + FADH2
show the reaction diagram
-
the oxidation by oxygen molar ratio of NADPH oxidized/Oz consumed, measured polarographically, is 2.0, H2O2 is produced during reoxidation of the flavoprotein by oxygen
-
-
?
methylfarnesoate + O2 + NADPH
?
show the reaction diagram
-
the major product of C(78-82,F87L,328-330) during methylfarnesoate oxidation is determined to be the 12-hydroxy isomer
-
-
?
methylphenylsulfide + NADH + H+ + O2
methylphenylsulfoxide + NAD+ + H2O
show the reaction diagram
-
catalyzed by StyA of Pseudomonas sp. VLB120 and electrochemical FAD reduction
-
-
?
methyltestosterone + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
metolachlor + NADPH + O2 + FAD
?
show the reaction diagram
Sorghum sp.
-
de-ethylation
-
-
?
myristic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
myristic acid + reduced flavoprotein + O2
omega-hydroxy-myristic acid + oxidized flavoprotein + H2O
show the reaction diagram
-
isozyme CYP52A17, best substrate
isoform CYP52A17, additional fornmation of about 15% dicarbonic acid
-
?
N'-nitrosonornicotine + O2 + reduced flavoprotein
?
show the reaction diagram
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products, nicotine oxidase activity of CYP2A6
-
-
?
naphthalene + O2 + NAD(P)H + cytochrome c
1-naphthol + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
regioselective oxidation
-
-
?
naphthalene + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
substrate only for mutant A74G/F88V/S189Q
-
-
?
narbomycin + reduced ferredoxin + O2
pikromycin + ferredoxin + H2O
show the reaction diagram
-
-, the organism is a pikromycin producer
-
-
?
nerylacetone + O2 + NADPH
9,10-epoxynerylacetone + 5,6-epoxynerylacetone
show the reaction diagram
-
CYP102A7, high activity
-
-
?
nonylphenol + O2 + NADPH
?
show the reaction diagram
Phanerochaete chrysosporium, Phanerochaete chrysosporium BKM-F-1767
-
-
-
-
?
norflurazon + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
octane + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
substrate only for mutant A74G/F88V/S189Q and for mutant A74G/S189Q
-
-
?
oleandomycin + reduced ferredoxin + O2
4-hydroxy-oleandomycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
oleic acid + NADPH
?
show the reaction diagram
-
CYP102A1, CYP102A2, CYP102A3 and CYP102A7
-
-
?
oleic acid + O2 + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
oleic acid + reduced flavoprotein + O2
omega-hydroxy oleic acid + n-decan-dicarboxylic acid + oxidized flavoprotein + H2O
show the reaction diagram
-
isozyme CYP52A13, best substrate,isozyme CYP52A17, good substrate
isozyme CYP52A13, products in ratio 1:1, CYP52A17, ratio 3:7 of hydroxy- and dicarboxy-product
-
?
omega-(p-nitrophenyl)decanoic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
omega-(p-nitrophenyl)dodecanoic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
omega-(p-nitrophenyl)octanoic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
oxytetracycline + reduced flavoprotein + NADPH + O2
11a-hydroxy-oxytetracycline + oxidized flavoprotein + H2O + NADP+
show the reaction diagram
-
-
-
-
?
p-chlorothioanisole + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
p-fluorothioanisole + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
p-methoxythioanisole + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
p-nitrophenol + O2 + NADPH
?
show the reaction diagram
P04799, P04800, P05182, P08683
-
-
-
?
p-nitrophenol + O2 + NADPH
?
show the reaction diagram
P05177
CYP2E1
-
-
?
p-tolyl methyl sulfide + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
palmitic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
palmitic acid + O2 + NADPH
?
show the reaction diagram
-
products of hydroxylation by wild-type CYP102A1 are 15-OH, 14-OH, 13-OH, 12-OH, 11-OH, and 10-OH, corresponding to omega-1 to omega-6 hydroxylation, with omega-1 to omega-3 being the major products in both cases
-
-
?
palmitic acid + O2 + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
palmitic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
palmitic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
isozyme CYP52A17, good substrate
-
-
?
palmitoleic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
pendimethalin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
phenyl ethyl sulfide + O2 + NADPH
?
show the reaction diagram
-
-
-
-
?
phenylmethylsulfide + NADPH + H+ + O2
phenylmethylsulfoxide + NADP+ + H2O
show the reaction diagram
-
enantioselectivity for the biosulfoxidation catalyzed by the recombinant enzyme expressed from an improved engineered Escherichia coli strain
-
-
?
pilocarpine + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
progesterone + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
prostaglandin + NADPH + O2
20-hydroxy-prostaglandin + NADP+ + H2O
show the reaction diagram
-
physiological functions are the metabolic inactivation of prostaglandins and the production of 20-hydroxyeicosatetraenoic acid, CYP4A4
-
-
?
prostaglandin A1 + NADPH + O2
20-hydroxy-prostaglandin A1 + NADP+ + H2O
show the reaction diagram
-
CYP4A4, CYP4A6, CYP4A7
-
-
?
prostaglandin A2 + NADPH + O2
20-hydroxy-prostaglandin A2 + NADP+ + H2O
show the reaction diagram
-
CYP4A4, CYP4A6, CYP4A7
-
-
?
prostaglandin D2 + NADPH + O2
20-hydroxy-prostaglandin D2 + NADP+ + H2O
show the reaction diagram
-
CYP4A4
-
-
?
prostaglandin E1 + NADPH + O2
20-hydroxy-prostaglandin E1 + NADP+ + H2O
show the reaction diagram
-
CYP4A4
-
-
?
prostaglandin E2 + NADPH + O2
20-hydroxy-prostaglandin E2 + NADP+ + H2O
show the reaction diagram
-
CYP4A4
-
-
?
prostaglandin F2alpha + NADPH + O2
20-hydroxy-prostaglandin F2alpha + NADP+ + H2O
show the reaction diagram
-
CYP4A4
-
-
?
psoralen + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
pyributicarb + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
quinine + NADPH + H+ + O2
3-hydroxyquinine + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
quinine + NADPH + H+ + O2
3-hydroxyquinine + NADP+ + H2O
show the reaction diagram
-
in the microsomal membranes, CYP3A4 interacts with the NADPH-P450 reductase to receive electrons used in metabolism of drugs and xenobiotics. The heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
-
-
?
S-mephenytoin + O2 + 2 H+
?
show the reaction diagram
-
-
-
-
?
sertraline + O2 + 2 H+
demethylsertraline + formaldehyde + H2O
show the reaction diagram
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
sertraline + O2 + 2 H+
desmethylsertraline + formaldehyde + H2O
show the reaction diagram
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
simvastatin + O2 + reduced flavoprotein
6-beta-hydroxy-methyl-simvastatin + oxidzed flavoprotein + H2O
show the reaction diagram
-
-
-
-
-
stearic acid + NADPH
?
show the reaction diagram
-
CYP102A7
-
-
?
stearic acid + O2 + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
stearic acid + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
styrene + NADH + H+ + O2
styrene oxide + NAD+ + H2O
show the reaction diagram
-
enantioselective oxygenations catalyzed by StyA1 and StyA2B, proposed mechanism of StyA/StyB from Pseudomonas sp. VLB120, overview, enantioselective oxygenations catalyzed by StyA and StyB, proposed mechanism of StyA/StyB from Pseudomonas sp. VLB120, overview
-
-
?
styrene + NADH + H+ + O2
styrene oxide + NAD+ + H2O
show the reaction diagram
-
enantioselective oxygenations catalyzed by StyA1 and StyA2B, proposed mechanism of StyA/StyB from Pseudomonas sp. VLB120, overview, enantioselective oxygenations catalyzed by StyA and StyB, proposed mechanism of StyA/StyB from Pseudomonas sp. VLB120, overview
-
-
?
styrene + O2 + H2O2
(R)-styrene oxide + (S)-styrene oxide + H2O
show the reaction diagram
-
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
-
-
?
styrene + O2 + NAD(P)H
(R)-styrene oxide + (S)-styrene oxide + H2O + NAD(P)+
show the reaction diagram
-
-
enantioselective styrene oxidation with different CYP102A1 mutants, 25% S-isomer for the wild-type enzyme, 58% S-isomer for mutant A74E/F87V/P386S, 49% R-isomer for mutant F87A, 65% R-isomer for mutant A74G/F87V/L188Q, and 92% R-isomer for mutant F87G
-
?
testosterone + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
-
-
?
testosterone + O2 + NADPH
?
show the reaction diagram
P10632, P10635, P20813, P20815, P24462
CYP3A4
-
-
?
testosterone + O2 + NADPH + H+
6beta-hydroxytestosterone + NADP+ + H2O
show the reaction diagram
P05177
CYP3A4
-
-
?
testosterone enanthate + O2 + NADPH
?
show the reaction diagram
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
CYP107
-
-
?
tetracycline + reduced flavoprotein + O2
11a-hydroxy-tetracycline + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
tetradecanoic acid + NADPH
?
show the reaction diagram
-
CYP102A7, highest activity
-
-
?
thiobencarb + O2 + reduced flavoprotein
?
show the reaction diagram
-
-
-
-
?
tolbutamide + O2 + NADPH
?
show the reaction diagram
P04799, P04800, P05182, P08683
-
-
-
?
tolbutamide + O2 + NADPH
?
show the reaction diagram
P05177
CYP2C9
-
-
?
toluene + O2 + NAD(P)H + cytochrome c
benzyl alcohol + H2O + NAD(P)+ + reduced cytochrome c
show the reaction diagram
Q52TE7, -
-
-
-
?
trifluralin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
xanthotoxin + reduced flavoprotein + O2
? + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
minocycline + reduced flavoprotein + O2
11a-hydroxy-minocycline + oxidized flavoprotein + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
self-sufficient fatty acid monooxygenase
-
-
-
additional information
?
-
-
enzyme catalyses hydroxylation in the omega-1, omega-2 and omega-3 positions and/or epoxidation of medium- and long-chain fatty acids
-
-
-
additional information
?
-
-
no activity with prostaglandins of E type, CYP4A6, no activity with prostaglandins of E type, CYP4A7
-
-
-
additional information
?
-
-
no substrate: chloropropham, quizalofopethyl, isoxaben
-
-
-
additional information
?
-
-
tetracycline substrates, initial monohydroxylation at position 11a followed by intramolecular cyclization and non-enzymatic breakdown to undefined products
-
-
-
additional information
?
-
-
a xenobiotic-metabolizing cytochrome P450 monooxygenase that contributes extensively to drug and toxin metabolism, CYP3A4 is the predominant enzyme in the clearance of about 50% of therapeutic drugs
-
-
-
additional information
?
-
-
effect of toxification on hepaic metabolism and biotransformation enzyme levels, overview
-
-
-
additional information
?
-
-
effect of toxification on hepatic metabolism and biotransformation enzyme levels, overview
-
-
-
additional information
?
-
-, Q5KQH7
EUI acts as a gibberellic acid inactivating enzyme, in eui mutant plans, the biological activity of GA4 is reduced, expression of Eui is tightly regulated during plant development with the stage-specific eui phenotypes, GA biosynthesis and catabolism pathways, overview, the enzyme negatively regulates gibberellic acid metabolism, mechanism, overview
-
-
-
additional information
?
-
-
in humans, CYP3A4 appears to be the dominant CYP and contributes to over 60% of the metabolism of drugs, the Ah receptor is important in CYP1A1 regulation, a number of mechanisms occur to regulate CYP including enhancement of mRNA stability, modulation of heme degradation, enzyme phosphorylation, and protein-protein interactions
-
-
-
additional information
?
-
-, Q4G2S1, Q4G2S2, Q4G2S3, Q4L230, Q4L231
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
-
additional information
?
-
-
no fluctuations between the light and dark periods under ad libitum and restricted feeding conditions, effects on P450 monooxygenase activities in male rats, overview
-
-
-
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview
-
-
-
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview, PPARalpha agonist increased the transcription activity of rat CYP4A1
-
-
-
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
-
additional information
?
-
-, Q38Q84, Q38Q85, Q38Q86, Q38Q87
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
-
additional information
?
-
-
the enzyme is involved in macrolide biosynthesis and performs unusual C4-hydroxylation
-
-
-
additional information
?
-
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
-
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
-
additional information
?
-
-
activity involves cytochrome c reduction, CYP102A1 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions, an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
-
-
-
additional information
?
-
-
activity involves cytochrome c reduction, CYP102A3 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions
-
-
-
additional information
?
-
-
CYP mainly catalyzes C-H abstraction but also oxidizes nitrogen- and sulfur-containing compounds and generally converts lipophilic compounds into more hydrophilic metabolites
-
-
-
additional information
?
-
-, Q5KQH7
EUI catalyzes the 16alpha,17-epoxidation of non-13-hydroxylated gibberellic acids with very high activity on giberellic acid GA4, substrate specificity, overview, no activity with the 13-hydroxylated GA1, GA20, and GA53
-
-
-
additional information
?
-
Q52TE7, -
product identifications, no activity with alpha-pinene, terpeneol, ethoxyresorufin, and cyclohexane, a natural self-sufficient fusion protein consisting of ferredoxin, flavin-containing reductase, and P450 monooxygenase, substrate specificity: in the presence of NADPH, the enzyme shows hydroxylation activity towards polycyclic aromatic hydrocarbons naphthalene, indene, acenaphthene, toluene, fluorene, m-xylene, and ethyl benzene, the conversion of naphthalene, acenaphthene, and fluorene results in respective ring monohydroxylated metabolites, alkyl aromatics like toluene, m-xylene, and ethyl benzene are hydroxylated exclusively at the side chains
-
-
-
additional information
?
-
-
regiospecific and stereo-specific activity, overview
-
-
-
additional information
?
-
-
structural diversification of macrolactones by the substrate-flexible enzyme, substrate specificity, degree of plasticity towards alternative substrates, overview, modeling of macrolide conformations and enzyme-substrate complex
-
-
-
additional information
?
-
-
substrate specificity: the enzyme catalyzes the NADPH- and oxygen-dependent N-oxidation of a variety of lipid-soluble set- and tert-amines, the sec-amines are oxidized to the hydroxylamines, and the tert-amines to the amine oxides, no oxidation of primary amines, overview
-
-
-
additional information
?
-
-
substrates bind in a cavity above the heme surface, function-structure relationship, the outer surfaces of the active site cavity are formed by portions of beta-sheets 1 and 4, helices FG, and the loop between helices B and C, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes oxidation of methanol, acetone, dimethylsulfoxide, n-hexadecane, n-octadecane, and naphthalene
-
-
-
additional information
?
-
-, Q38Q84, Q38Q85, Q38Q86, Q38Q87
the enzyme demethylates nicotine to nornicotine
-
-
-
additional information
?
-
-
the enzyme performs dealkylation of 7-alkoxycoumarin
-
-
-
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview
-
-
-
additional information
?
-
P14779
wild type CYP102A1 has no oxidizing activity toward ()-alpha- and ()-beta-pinene
-
-
-
additional information
?
-
-, Q2I129
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
-
additional information
?
-
-
CYP102A7 is active towards medium-chain fatty acids but shows a strong preference for saturated over unsaturated fatty acids. Besides fatty acids, CYP102A7 is able to catalyse the oxidation of cyclic and acyclic terpenes with high activity and coupling efficiency. 7-methoxycoumarin is not converted by CYP102A7. No NADPH consumption with 11-deoxycortisol, dextromethorphane, testosterone and cyclic and acyclic alkanes as substrates
-
-
-
additional information
?
-
P11509
CYP2C19 can not form fenthion-oxon-sulfoxide from fenthion-oxon
-
-
-
additional information
?
-
-
no activity with anthraquinone-1,8-disulfonic acid
-
-
-
additional information
?
-
-
no hydroxylation activity towards naphthalene, indene, ethyl benzene, and m-xylene
-
-
-
additional information
?
-
-
reacts with activity-based proteins of varying chemical composition, quite distinct from their natural substrates
-
-
-
additional information
?
-
Q70KH6
AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin. The enzymatic reaction involves a tandem oxygenation process including a regio- and stereospecific hydroxylation, followed by heterocyclization, overview
-
-
-
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
-
additional information
?
-
-
the multifunctional enantioselective flavoprotein monooxygenase system composed of a single styrene monooxygenase, SMO, StyA1 and another styrene monooxygenase fused to an NADH-flavin oxidoreductase, StyA2B. StyA1 and StyA2B convert styrene and chemical analogues to the corresponding epoxides at the expense of FADH2, provided from StyA2B. The StyA1/StyA2B system presents the highest monooxygenase activity in an equimolar ratio of StyA1 and StyA2B, indicating transient protein complex formation
-
-
-
additional information
?
-
-
YP116B3 catalyzes the dealkylation of 7-ethoxycoumarin and the hydroxylation of substituted and unsubstituted aromatics, overview
-
-
-
additional information
?
-
Q70KH6
AurH catalyzes an unprecedented tandem oxygenation process. First, AurH catalyzes an asymmetric hydroxylation of deoxyaureothin, yielding (7R)-7-hydroxydeoxyaureothin as an intermediate, thus setting the absolute configuration of the final product. Second, AurH mediates another C-O bond formation that leads to O-heterocyclization. Structure-function relationship analysis by computational docking, site-directed mutagenesis, and chemical analyses, overview
-
-
-
additional information
?
-
-
CYP1A2 catalyzes the O-demethylation of 7-methoxyresorufin
-
-
-
additional information
?
-
-
CYP1A2 cooperates with NADPH-cytochrome P450 reductase, CPR. Differential sensitivity of CPR binding to CYP1A2 depending on the substrate present, overview
-
-
-
additional information
?
-
-
palmitate, stearate, and oleate show negligible binding to isoform CYP102B1, in contrast to CYP102A1
-
-
-
additional information
?
-
-
StyA1 is also active when FADH2 is supplied by StyB from Pseudomonas sp. VLB120 or PheA2, a small component of a flavin-dependent two-component phenol monooxygenase, from Rhodococcus opacus 1CP, but in both cases the reductase produces an excess of FADH2, resulting in a high waste of NADH. The epoxidation rate of StyA1 heavily depends on the type of reductase
-
-
-
additional information
?
-
-
the enzyme shows (omega-1)-hydroxylase activity against arachidonic acid, linoleic acid, and especially against eicosapentaenoic acid and docosahexaenoic acid, substrate specificities of isozymes, overview
-
-
-
additional information
?
-
-
the multifunctional enantioselective flavoprotein monooxygenase system composed of a single styrene monooxygenase, SMO, StyA1 and another styrene monooxygenase fused to an NADH-flavin oxidoreductase, StyA2B. StyA1 and StyA2B convert styrene and chemical analogues to the corresponding epoxides at the expense of FADH2, provided from StyA2B. The StyA1/StyA2B system presents the highest monooxygenase activity in an equimolar ratio of StyA1 and StyA2B, indicating transient protein complex formation, StyA1 is also active when FADH2 is supplied by StyB from Pseudomonas sp. VLB120 or PheA2, a small component of a flavin-dependent two-component phenol monooxygenase, from Rhodococcus opacus 1CP, but in both cases the reductase produces an excess of FADH2, resulting in a high waste of NADH. The epoxidation rate of StyA1 heavily depends on the type of reductase
-
-
-
additional information
?
-
-
no hydroxylation activity towards naphthalene, indene, ethyl benzene, and m-xylene
-
-
-
additional information
?
-
Aspergillus terreus MTCC 6324
-
the enzyme catalyzes oxidation of methanol, acetone, dimethylsulfoxide, n-hexadecane, n-octadecane, and naphthalene
-
-
-
additional information
?
-
Xanthophyllomyces dendrorhous VKPM Y2410
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
-
additional information
?
-
Claviceps purpurea P1
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster, the enzyme possibly also catalyzes the oxidation of agroclavine, overview
-
-
-
additional information
?
-
Phanerochaete chrysosporium BKM-F-1767
-, Q4G2S1, Q4G2S2, Q4G2S3, Q4L230, Q4L231
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
-
additional information
?
-
Bacillus licheniformis DSM13
-
CYP102A7 is active towards medium-chain fatty acids but shows a strong preference for saturated over unsaturated fatty acids. Besides fatty acids, CYP102A7 is able to catalyse the oxidation of cyclic and acyclic terpenes with high activity and coupling efficiency. 7-methoxycoumarin is not converted by CYP102A7. No NADPH consumption with 11-deoxycortisol, dextromethorphane, testosterone and cyclic and acyclic alkanes as substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-(methylnitrosamino)-1-(3pyridyl)-1-butanone + O2 + reduced flavoprotein
?
show the reaction diagram
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
7-ethoxycoumarin + 3 NADH + 3 H+ + O2
ethane + 7-hydroxycoumarin + 3 NAD+ + 2 H2O
show the reaction diagram
-
-
-
-
?
7-ethoxycoumarin + NADPH + O2 + FAD
7-hydroxycoumarin + NADP+ + FADH2 + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + NADPH + O2 + FAD
7-hydroxycoumarin + NADP+ + FADH2 + ?
show the reaction diagram
-
wild-type enzyme and recombinant enzyme P4502B6 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
7-ethoxycoumarin + O2 + NADPH
?
show the reaction diagram
-
7-ethoxycoumarin O-deethylation
-
-
?
7-ethoxyresorufin + O2 + NADPH
?
show the reaction diagram
-
7-ethoxyresorufin O-deethylation
-
-
?
7-methoxycoumarin + 3 NADH + 3 H+ + O2
methane + 7-hydroxycoumarin + 3 NAD+ + 2 H2O
show the reaction diagram
-
-
-
-
?
aflatoxin B1 + O2 + NADPH
?
show the reaction diagram
-
i.e. AFB1, bioactivation of the carcinogenic mycotoxin to a toxic compound, although not acutely toxic at low concentrations, AFB1 had significant chronic effects, including protracted development, increased mortality, decreased pupation rate, and reduced pupal weight, sensitivity varies with developmental stage, whereas intermediate concentrations causes complete mortality in first instars, this same concentration has no detectable adverse effects on larvae encountering AFB1 in fifth instar. These compounds owe their toxicity to their ability to form irreversible adducts to nucleic acids with the concomitant inhibition of DNA replication and DNA-dependent transcription, mortality, overview
-
-
?
aminopyrene + O2 + NADPH
? + formaldehyde + NADP+ + H2O
show the reaction diagram
-
aminopyrene-N-demethylation
-
-
?
arachidonic acid + O2 + NADPH
20-hydroxyeicosatetraenoic acid + H2O + NADP+
show the reaction diagram
-
-
i.e. 20-HETE, a potent constrictor of renal microvessels and inhibits Na+ reabsorption in the proximal tubule and thick ascending limb
-
?
avermectin + O2 + reduced ferredoxin
4''-oxo-avermectin + H2O + ferredoxin
show the reaction diagram
-
4''-oxo-avermectin is a key intermediate in the manufacture of the agriculturally important insecticide emamectin benzoate from the natural product avermectin, overview
-
-
?
bentazon + NADPH + O2 + FAD
?
show the reaction diagram
-
ring-hydroxylation
-
-
?
benzo-pyrene + NADPH + O2 + FAD
?
show the reaction diagram
-
recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
a combination of oxidative N-demethylation and hydroxylation of the ring-methyl group, recombinant enzyme CYP1A1 fused to yeast reductase and expressed in transgenic tobacco plants
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
recombinant wild-type enzyme and enzyme mutant fused to yeast reductase expressed in transgenic potato plants
-
-
?
chlorotoluron + NADPH + O2 + FAD
?
show the reaction diagram
-
ring methyl-hydroxylation
-
-
?
diclofop + NADPH + O2 + FAD
?
show the reaction diagram
-
ring-hydroxylation
-
-
?
elymoclavine + O2 + NADPH
paspalic acid + H2O + NADP+
show the reaction diagram
Claviceps purpurea, Claviceps purpurea P1
-
-
the product is the precursor for D-lysergic acid
-
?
giberellic acid GA4 + NADPH + H+ + O2
16alpha,17-epoxy GA4 + NADP+ + H2O
show the reaction diagram
-, Q5KQH7
-
the product is transformed further to 16,17-dihydro-16alpha,17-dihydroxy-GA4 in the plant
-
?
macrolide YC-17 + reduced ferredoxin + O2
methymycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
macrolide YC-17 + reduced ferredoxin + O2
neomethymycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
macrolide YC-17 + reduced ferredoxin + O2
novamethymycin + ferredoxin + H2O
show the reaction diagram
-
-
-
-
?
N'-nitrosonornicotine + O2 + reduced flavoprotein
?
show the reaction diagram
-
nicotine oxidase activity of CYP2A6, activates the tobacco-derived carcinogens to mutagenic products
-
-
?
narbomycin + reduced ferredoxin + O2
pikromycin + ferredoxin + H2O
show the reaction diagram
-
the organism is a pikromycin producer
-
-
?
prostaglandin + NADPH + O2
20-hydroxy-prostaglandin + NADP+ + H2O
show the reaction diagram
-
physiological functions are the metabolic inactivation of prostaglandins and the production of 20-hydroxyeicosatetraenoic acid, CYP4A4
-
-
?
quinine + NADPH + H+ + O2
3-hydroxyquinine + NADP+ + H2O
show the reaction diagram
-
in the microsomal membranes, CYP3A4 interacts with the NADPH-P450 reductase to receive electrons used in metabolism of drugs and xenobiotics. The heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
-
-
?
sertraline + O2 + 2 H+
demethylsertraline + formaldehyde + H2O
show the reaction diagram
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
sertraline + O2 + 2 H+
desmethylsertraline + formaldehyde + H2O
show the reaction diagram
-
i.e. (1S,4S)-N-methyl-4-(3,4-dichlorophenyl)-1,2,3,4-tetrahydro-1-naphthylamine, a one-step oxidative N-demethylation
-
-
?
styrene + NADH + H+ + O2
styrene oxide + NAD+ + H2O
show the reaction diagram
-
enantioselective oxygenations catalyzed by StyA1 and StyA2B, proposed mechanism of StyA/StyB from Pseudomonas sp. VLB120, overview
-
-
?
metolachlor + NADPH + O2 + FAD
?
show the reaction diagram
Sorghum sp.
-
de-ethylation
-
-
?
additional information
?
-
-
a xenobiotic-metabolizing cytochrome P450 monooxygenase that contributes extensively to drug and toxin metabolism, CYP3A4 is the predominant enzyme in the clearance of about 50% of therapeutic drugs
-
-
-
additional information
?
-
-
effect of toxification on hepaic metabolism and biotransformation enzyme levels, overview
-
-
-
additional information
?
-
-
effect of toxification on hepatic metabolism and biotransformation enzyme levels, overview
-
-
-
additional information
?
-
-, Q5KQH7
EUI acts as a gibberellic acid inactivating enzyme, in eui mutant plans, the biological activity of GA4 is reduced, expression of Eui is tightly regulated during plant development with the stage-specific eui phenotypes, GA biosynthesis and catabolism pathways, overview, the enzyme negatively regulates gibberellic acid metabolism, mechanism, overview
-
-
-
additional information
?
-
-
in humans, CYP3A4 appears to be the dominant CYP and contributes to over 60% of the metabolism of drugs, the Ah receptor is important in CYP1A1 regulation, a number of mechanisms occur to regulate CYP including enhancement of mRNA stability, modulation of heme degradation, enzyme phosphorylation, and protein-protein interactions
-
-
-
additional information
?
-
-, Q4G2S1, Q4G2S2, Q4G2S3, Q4L230, Q4L231
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
-
additional information
?
-
-
no fluctuations between the light and dark periods under ad libitum and restricted feeding conditions, effects on P450 monooxygenase activities in male rats, overview
-
-
-
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview
-
-
-
additional information
?
-
-
the cytochrome P-450 4, CYP4, family catalyze the omega-hydroxylation of fatty acids, metabolic regulation, overview, PPARalpha agonist increased the transcription activity of rat CYP4A1
-
-
-
additional information
?
-
-
the enzyme catalyzes a wide range of reactions in secondary metabolism, overview, the enzyme is important in metabolism of herbicides, overview
-
-
-
additional information
?
-
-, Q38Q84, Q38Q85, Q38Q86, Q38Q87
the enzyme demethylates nicotine to nornicotine, nornicotine serves as the precursor in the synthesis of the well characterized carcinogen N'-nitrosonornicotine during the curing and processing of tobacco
-
-
-
additional information
?
-
-
the enzyme is involved in macrolide biosynthesis and performs unusual C4-hydroxylation
-
-
-
additional information
?
-
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
-
additional information
?
-
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
-
additional information
?
-
-, Q2I129
the concomitant down-regulation of P450arom and up-regulation of P45011beta are of pivotal importance to the sex change
-
-
-
additional information
?
-
Q70KH6
AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin. The enzymatic reaction involves a tandem oxygenation process including a regio- and stereospecific hydroxylation, followed by heterocyclization, overview
-
-
-
additional information
?
-
-
CYP4A enzymes predominantly function as AA omega-hydroxylases, hydroxy metabolites are roduced by the individual CYP isoforms in a regio- and stereoselective manner. CYP isoforms that do not produce 20-hydroxyeicosatetraenoic acid but function predominantly as AA (omega-1)-hydroxylases include CYP1A1, but also act regioselective
-
-
-
additional information
?
-
-
the multifunctional enantioselective flavoprotein monooxygenase system composed of a single styrene monooxygenase, SMO, StyA1 and another styrene monooxygenase fused to an NADH-flavin oxidoreductase, StyA2B. StyA1 and StyA2B convert styrene and chemical analogues to the corresponding epoxides at the expense of FADH2, provided from StyA2B. The StyA1/StyA2B system presents the highest monooxygenase activity in an equimolar ratio of StyA1 and StyA2B, indicating transient protein complex formation
-
-
-
additional information
?
-
-
YP116B3 catalyzes the dealkylation of 7-ethoxycoumarin and the hydroxylation of substituted and unsubstituted aromatics, overview
-
-
-
additional information
?
-
-
the multifunctional enantioselective flavoprotein monooxygenase system composed of a single styrene monooxygenase, SMO, StyA1 and another styrene monooxygenase fused to an NADH-flavin oxidoreductase, StyA2B. StyA1 and StyA2B convert styrene and chemical analogues to the corresponding epoxides at the expense of FADH2, provided from StyA2B. The StyA1/StyA2B system presents the highest monooxygenase activity in an equimolar ratio of StyA1 and StyA2B, indicating transient protein complex formation
-
-
-
additional information
?
-
Xanthophyllomyces dendrorhous VKPM Y2410
-
the enzyme is involved in the biosynthesis of astaxanthin, overview
-
-
-
additional information
?
-
Claviceps purpurea P1
-
the enzyme possibly also catalyzes the oxidation of agroclavine, overview, the enzyme bridges the clavine and ergoline alkaloid pathways, it is critical in the ergot alkaloid gene cluster
-
-
-
additional information
?
-
Phanerochaete chrysosporium BKM-F-1767
-, Q4G2S1, Q4G2S2, Q4G2S3, Q4L230, Q4L231
mechanisms of secondary metabolism and oxidative biotransformation pathways in this model white rot fungus, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cytochrome c
Q52TE7, -
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
cytochrome P450
-
-
-
FAD
-
14 nmol FAD per enzyme
FAD
-
bound, binding structure, overview
FAD
-
FAD totally recovers activities in the BTC1A2_PORV492E membranes, for both 7-ethoxyresorufin and 7-methoxyresorufin, but only partially recovers these activities in the BTC1A2_PORY459H membranes
Ferredoxin
-
-
-
Ferredoxin
Q52TE7, -
bound
-
flavoprotein
-
-
-
FMN
Q52TE7, -
bound, quantification of the molar ratio of FMN to protein of 1.1:1
FMN
-
bound, binding structure, overview
FMN
-
the C-terminal reductase portion of P450SMO comprises an FMN-binding
FMN
-
the heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
heme
-
the heme unit in CYP3A4 is the catalytic center and electrons are transferred through reduced FMN to heme through electrostatic interactions
heme
-
structure modeling of the heme domain of CYP116B3
NAD(P)H
Q52TE7, -
NADPH is preferred to NADH giving twofold higher activity
NADH
-
the C-terminal reductase portion of P450SMO comprises an NADH-binding
NADPH
-
dependent on
NADPH
Q5KQH7
-
NADPH
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
-
NADPH
-
required, supplied by the NADPH-P450 reductase
additional information
-
the enzyme appears to be free from cytochromes
-
additional information
-
engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH; residues S965, R966 and Y974 are important in the Rossman fold-like binding motif for the cofactor binding and discrimination, overview
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
Q52TE7, -
heme iron, a cytochrome P450 enzyme
Fe2+
-
the enzyme contains small amounts of a hemoprotein
Fe2+
-
in a catalytic cytochrome P450 ferric heme center
Fe2+
-
heme iron
Fe2+
-
heme iron
Fe2+
-
a heme iron, the enzyme is a cytochrome P450 monooxygenase
Fe2+
-
heme iron, His226 is involved in metal ion coordination
Fe2+
-
a heme-containing P450 monooxygenase
Fe2+
Q5KQH7
heme iron
Fe2+
-
an electron transferred to CYP(Fe3+), interacting with the proper substrate, reduces Fe3+ in the heme system to Fe2+, allowing a consequent interaction of the CYP(Fe2+)-substrate complex with O2. The second transferred electron allows for transformation of the O2-CYP(Fe2+)-substrate complex into a form with an anion potentialized reactive oxygen species -O2-CYP(Fe2+)-substrate, permitting destabilization of the bond between the atoms of the oxygen molecule to form a bond of one of the oxygen atoms with the substrate. The second oxygen atom is reduced to H2O by reductive equivalent transport systems (cytochrome P450 reductase, cytochrome b5 reductase/cytochrome b5, adrenodoxin reductase/adrenodoxin)
Fe2+
-
the C-terminal reductase portion of P450SMO comprises a [2Fe2S] ferredoxin center
Fe2+
-
heme protein
Fe2+
-
heme protein
Fe2+
-
heme protein
Fe2+
Q70KH6
heme protein
Fe2+
-
heme protein
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-(1-naphthyl)-2-thiourea
-
92% inhibition at 0.5 mM, selective inhibitor
1-aminobenzotriazole
-
moderately prohibits spontaneous mutations of V79-hCYP2E1-hSULT1A1 cells. In combination with SULT1A1 inhibitor pentachlorophenol completely prohibits spontaneous mutations of V79-hCYP2E1-hSULT1A1 cells
17alpha-ethynylestradiol
-
reactive intermediates of 17alpha-ethynylestradiol inactivate P450s in a NADPH-dependent mechanism-based manner by a combination of heme alkylation and apoprotein modification
8-methoxypsoralen
-
-
anastrozole
-
profiling inhibition of probe 1 labeling of P450 19A1, inhibits labeling of P450 2C9 by probe 5
Ancymidol
Q70KH6
a P450 inhibitor, that induces conformational changes at the active site. It is primarily bound through the interaction of the pyrimidine ring system to the heme iron and to the conserved residue T247. Other interactions to the inhibitor are mediated by loose and hydrophobic contacts, mainly to residues F89, A243, L175, L290, T295
bifonazole
-
an anti-fungal drug, complex formation with CYP2B4, inhibits monooxygenase activity and induces a type II binding spectrum in CYP2B4 mutant H226Y, plastic regions efficiently, because conformational changes are clustered, the 2B4-bifonazole dimer is different from the ligand-free 2B4dH dimer, which involves the coordination of His226 to the heme iron of the other monomer
bifonazole
P24462
CYP19
bitertanol
-
7-ethoxyresorufin O-deethylation is inhibited by the fungicide bitertanol, IC50: 800-900 nM
Cd2+
-
strong inhibition of 7-ethoxyresorufin-O-deethylase, EROD, and a lower inhibition of 7-ethoxycoumarin-O-deethylase, ECOD, activity, cadmium causes damage to the protein structure
chlorotoluron
-
metabolism in sensitive plants is induced by blue light
chlorotoluron
-
a herbicide
chlorotoluron
-
chlorotoluron treatment of the transgenic plants could lead to inhibition of the germination of broomrape, overview
chlorotoluron
-
a herbicide
cimetidine
-
specific inhibition
Cu2+
-
inhibits the enzyme in vitro and inactivate it in vivo, but also induce the enzyme in vivo in the first 24 h, overview
diethyldithiocarbamate
P24462
CYP2E1
dimethyl sulfoxide
-
CYP102A7 exhibits 50% of its initial activity in the presence of 26% dimethyl sulfoxide
Emulgen
-
a detergent that inactivates the enzyme at high concentrations
-
formestane
-
profiling inhibition of probe 1 labeling of P450 19A1, decreases probe 5 labeling of P450 2C19 and 1 labeling of P450 3A4
furafylline
P24462
-
furafylline
P11509
CYP1A2, at 0.005 mM fenthion, causes a 30% decrease in fenthion-sulfoxide formation. At 0.1 mM fenthion, CYP1A2 inhibition is not evident. Influences fenthion-oxon formation with a 25% inhibition at 0.005 mM or 0.1 mM fenthion concentrations
H2O2
-
at high concentrations
imidazole
-
at 20 mM, only half of P450SMO activity remains
Ketoconazole
P24462
CYP3A4
N-benzoyloxycarbonyl-Leu-Leu-leucinal
-
MG132, high concentrations are cytotoxic and can suppress CYP3A synthesis. Biphasic concentration effect on CYP3A turnover: stabilization at 0.005 to 0.01 mM with marked suppression at more than 0.1 mM. Marked (approximately 4fold) MG132 concentration-dependent RNA-dependent protein kinase-like ER-bound elF2alpha-kinase autophosphorylation, along with an 8fold increase in elF2alpha-phosphorylation. In parallel, MG132 also activates general control nonderepressible-2 elF2alpha kinase in a concentration-dependent manner, but not the heme-regulated inhibitor elF2alpha kinase. Consequently dramatic translational shutoff of total hepatic protein, including but not limited to CYP3A and tryptophan 2,3-dioxygenase protein syntheses
N2
-
99% inhibition at 100% in gas phase
Pb2+
-
inhibits the enzyme in vitro and inactivate it in vivo, but also induce the enzyme in vivo in the first 24 h, overview
piperonyl butoxide
-
-
piperonyl butoxide
-
significant inhibition by 75% in nutrient-rich malt extract cultures but no inhibition in defined low-nitrogen cultures
Quinidine
P24462
-
sulfaphenazole
P24462
CYP2C9
sulfaphenazole
P11509
CYP2C9, at 0.005 mM fenthion, causes a 30% decrease in fenthion-sulfoxide formation. At 0.01 mM fenthion, causes a 48% decrease of formed sulfoxide. Fenthion-oxon formation is reduced by 30% at 0.1 mM fenthion
ticlopidine
P11509
CYP2B6 and CYP2C19, 40% loss of sulfoxide formation. Decrease in fenthion-oxon formation by 71% and 64% at 0.005 mM or 0.1 mM fenthion concentrations, respectively, which is mainly attributable to CYP2B6
Tranylcypromine
P24462
; CYP2C19
methanol
P11509
partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzyme; partially affects (10-20%) activity of the active recombinant enzymes
additional information
-
no inhibition by erythrocuprein, cyanide, azide, SKF-525A, and catalase
-
additional information
-
CYP1A2, and likely other drug-metabolizing CYPs, are impaired by Antley-Bixler syndrome-related cytochrome P450 reductase mutations as observed in the steroidogenic CYPs
-
additional information
P24462
inhibition by Cree anti-diabetic plant ethanolic extracts; inhibition by Cree anti-diabetic plant ethanolic extracts. Extracts from Rhododendron groenlandicum, Sorbus decora, and Kalmia angustifolia are identified as having strong inhibition towards many CYP isoforms. Most inhibitory extracts towards CYP2B6-mediated metabolism are Juniperus communis followed by Rhododendron groenlandicum and Rhododendron tomentosum; inhibition by Cree anti-diabetic plant ethanolic extracts. Extracts from Rhododendron groenlandicum, Sorbus decora, and Kalmia angustifolia are identified as having strong inhibition towards many CYP isoforms. Most inhibitory extracts towards CYP2C9-mediated metabolism are Lycopodium clavatum followed by Sorbus decora and Juniperus communis. Most inhibitory extracts towards CYP2C19-mediated metabolism are Lycopodium clavatum followed by Juniperus communis and Larix laricina. Most inhibitory extracts towards CYP2E1-mediated metabolism are Kalmia angustifolia followed by Gaultheria hispidula and Rhododendron groenlandicum. Most inhibitory extracts towards CYP19-mediated metabolism ware Sorbus decora followed by Kalmia angustifolia and Abies balsamea. Most inhibitory extracts towards CYP3A4-mediated dibenzylfluorescein metabolism are Pinus banksiana followed by Picea mariana and Salix planifolia. Most inhibitory extracts towards CYP3A4-mediated testosterone metabolism are Larix laricina followed by Juniperus communis and Rhododendron groenlandicum. Gaultheria hispidula, Juniperus communis, Larix laricina, Picea mariana, Rhododendron tomentosum, Salix planifolia and Sarracenia purpurea, have diverging inhibition towards the two substrates dibenzylfluorescein and testosterone; inhibition by Cree anti-diabetic plant ethanolic extracts. Most inhibitory extracts towards CYP1A2-mediated metabolism are Rhododendron groenlandicum followed by Pinus banksiana and Picea mariana; inhibition by Cree anti-diabetic plant ethanolic extracts. Most inhibitory extracts towards CYP2C8-mediated metabolism are Sorbus decora followed by Lycopodium clavatum and Rhododendron tomentosum; inhibition by Cree anti-diabetic plant ethanolic extracts. Most inhibitory extracts towards CYP2D6-mediated metabolism are Rhododendron groenlandicum followed by Sarracenia purpurea and Kalmia angustifolia; inhibition by Cree anti-diabetic plant ethanolic extracts. Most inhibitory extracts towards CYPMost inhibitory extracts towards CYP3A5-mediated metabolism are Sorbus decora followed by Rhododendron groenlandicum and Kalmia angustifolia
-
additional information
P11509
antiCYP2B6 antibodies inhibition at 0.005 mM fenthion is not statistically significant, whereas at 0.1 mM fenthion it significantly inhibits the reaction (1520%). Fenthion-oxon formation is mainly influenced by antiCYP2B6 antibodies, with 59% and 40% inhibition at 0.005 mM and 0.1 mM fenthion, respectively; at 0.005 mM fenthion, antiCYP1A2 antibodies cause the highest inhibition of fenthion-sulfoxide formation (25%); at 0.005 mM fenthion, antiCYP2C9 antibodies cause the highest inhibition of fenthion-sulfoxide formation (20%). At 0.1 mM fenthion, presence of antiCYP2C9 antibodies cause a 28% decrease of formed sulfoxide. Anti2C19 antibodies inhibitions at 0.005 mM fenthion is not statistically significant, whereas at 0.1 mM fenthion it significantly inhibits the reaction (1520%). The presence of troleandomycin and antiCYP3A4 antibodies do not affect fenthion-sulfoxide formation in any of the experimental conditions used
-
additional information
-
only sour cherry, blueberry, and black currant juices suppress the first step of xenobiotic enzymatic activation by CYP1A2, whereas most plant-derived beverages, from diverse plants, inhibit the second step catalyzed by other enzymes, relative inhibition rates, detailed overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
amphetamine
-
activates
anastrozole
-
increases labeling of P450 1A2 by probe 3 up to 175% of control values
Cd2+
-
activation of aminopyrene-N-demethylase activity of CYP2B or CYP3A isoenzymes, which is increased 3- to 4-fold
dimethylsulfoxid
-
up to 25% v/v
FADH2
-
induces activation of StyA1 requiring interprotein communication
FMN
-
the linker region between P450 and FMN domain proves to be important for the effective biotransformation of (+)-camphor
n-octylamine
-
strongly activates
NADPH-P450 reductase
-
supports the CYP3A4 activity through providing NADPH, mutations in NADPH-P450 reductase, identified in patients with disordered steroidogenesis/Antley-Bixler syndrome, reduce CYP3A4 activity. NADPH-P450 reductase mutants Y181D, A457H, Y459H, V492E and R616X loose more than 99% of CYP3A4 activity, while NADPH-P450 reductase mutations A287P, C569Y and V608F loose 60-85% activity
-
phenethylamine
-
activates
Phenobarbital
-
induces the enzyme
primary alkylamines
-
increase the sec- and tert-amine N-oxidase activity of both the isolated enzyme and microsomes
-
mescaline
-
activates
additional information
-
induction of CYP1A by beta-naphthoflavone
-
additional information
-
no induction by cadaverine, aniline, and 4-chloroaniline
-
additional information
-
a drug-induced enzyme
-
additional information
-
chlorotoluron metabolism in sensitive plants is induced by blue light, induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview
-
additional information
-
induction of P450 in wounded tissues, all plant P450s depend on NADPH-cytochrome P450 reductase for providing the reducing equivalents needed to activate molecular oxygen, induction of the enzyme by light due to coupling of P450 monooxygenase to photosynthetic electron transfer systems in chloroplasts, overview
-
additional information
-
the enzyme is induced in cases of toxification by sublethal concentrations of oil effluent
-
additional information
-
the enzyme is induced and inhibited by the fungicide bitertanol, application increases the activiy of several cytochrome P450 monooxygenases in liver, kidney, and lung several fold, overview
-
additional information
-
the enzymes of both herbicide-resiatnt and herbicide-sensitive type are induced by bispyribac-sodium, fenoxaprop-ethyl, and thiobencarb, but to a higher extent the herbicide-resistant enzyme type, enzyme induction is part of the multi-herbicide resistace mechanism, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0129
-
12-methyl-tetradecanoic acid
-
CYP102A7, at pH 7.5
0.0165
-
13-methyl-tetradecanoic acid
-
CYP102A7, at pH 7.5
0.11
-
chlortetracycline
-
pH 8.5
0.0041
-
cytochrome c
-
CYP102A7, at pH 7.5
0.0199
-
demeclocycline
-
pH 8.5
0.102
-
dodecanoic acid
-
CYP102A7, at pH 7.5
0.0837
-
doxycycline
-
pH 8.5
0.0016
-
fenthion
P11509
desulfuration by recombinant human CYPs to fenthion-oxon
0.0022
-
fenthion
P11509
sulfoxidation to fenthion-sulfoxide
0.0024
-
fenthion
P11509
CYP2C19, desulfuration by recombinant human CYPs to fenthion-oxon
0.0027
-
fenthion
P11509
desulfuration by recombinant human CYPs to fenthion-oxon
0.0044
-
fenthion
P11509
CYP2C19, sulfoxidation to fenthion-sulfoxide
0.006
-
fenthion
P11509
CYP2C9, sulfoxidation to fenthion-sulfoxide
0.008
-
fenthion
P11509
CYP1A1, sulfoxidation to fenthion-sulfoxide
0.01
-
fenthion
P11509
sulfoxidation to fenthion-sulfoxide
0.012
-
fenthion
P11509
CYP2C9, desulfuration by recombinant human CYPs to fenthion-oxon
0.089
-
fenthion
P11509
CYP3A4, desulfuration by recombinant human CYPs to fenthion-oxon
0.131
-
fenthion
P11509
CYP3A4, sulfoxidation to fenthion-sulfoxide
0.018
-
fenthion-sulfoxide
P11509
CYP2C19
0.0386
-
hexadecanoic acid
-
CYP102A7, at pH 7.5, highest activity
0.0551
-
linoleic acid
-
CYP102A7, at pH 7.5
0.023
-
myristic acid
-
isozyme CYP52A17, pH 7.4, 35C
0.11
-
myristic acid
-
isozyme CYP52A13, pH 7.4, 35C
0.004
-
NADH
-
mutant A74G/F87V/L188Q/S965D
0.01
-
NADH
-
mutant A74G/F87V/L188Q/W1046S
0.02
-
NADH
-
mutant A74G/F87V/L188Q/W1046A
0.126
-
NADH
Q52TE7, -
pH 7.4, 25C
0.33
-
NADH
-
mutant A74G/F87V/L188Q/R966D
0.54
-
NADH
-
mutant A74G/F87V/L188Q/R966M
1.43
-
NADH
-
mutant A74G/F87V/L188Q
0.002
-
NADPH
-
mutants A74G/F87V/L188Q/W1046A and A74G/F87V/L188Q/W1046S
0.0025
-
NADPH
-
mutant A74G/F87V/L188Q
0.0034
-
NADPH
Q52TE7, -
pH 7.4, 25C
0.02
-
NADPH
-
mutant A74G/F87V/L188Q/S965D
0.05
-
NADPH
-
mutant A74G/F87V/L188Q/R966M
0.13
-
NADPH
-
mutant A74G/F87V/L188Q/R966D
0.133
-
NADPH
-
pH 8.5
0.075
-
oleic acid
-
isozyme CYP52A17, pH 7.4, 35C
0.084
-
oleic acid
-
isozyme CYP52A13, pH 7.4, 35C
0.0064
-
omega-(p-nitrophenyl)decanoic acid
-
pH 8.0, mutant A74G/F88V/S189Q
0.0245
-
omega-(p-nitrophenyl)decanoic acid
-
pH 8.0, wild-type
0.0065
-
omega-(p-nitrophenyl)dodecanoic acid
-
pH 8.0, mutant A74G/F88V/S189Q
0.0104
-
omega-(p-nitrophenyl)dodecanoic acid
-
pH 8.0, wild-type
0.0319
-
omega-(p-nitrophenyl)octanoic acid
-
pH 8.0, mutant A74G/F88V/S189Q
0.0618
-
omega-(p-nitrophenyl)octanoic acid
-
pH 8.0, wild-type
0.076
-
Oxytetracycline
-
pH 8.5
0.0165
-
palmitoleic acid
-
CYP102A7, at pH 7.5
0.0118
-
stearic acid
-
CYP102A7, at pH 7.5
0.054
-
tetracycline
-
pH 8.5
0.0509
-
tetradecanoic acid
-
CYP102A7, at pH 7.5, highest activity
0.0284
-
minocycline
-
pH 8.5
additional information
-
additional information
-
Km-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds
-
additional information
-
additional information
-
kinetic analysis of recombinant enzymes
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13.9
-
12-methyl-tetradecanoic acid
-
CYP102A7, at pH 7.5
21.1
-
13-methyl-tetradecanoic acid
-
CYP102A7, at pH 7.5
0.048
-
avermectin
-
pH 7.0, 30C, recombinant Ema1
0.3
-
chlortetracycline
-
pH 8.5
122.4
-
cytochrome c
-
CYP102A7, at pH 7.5
0.2
-
demeclocycline
-
pH 8.5
27.7
-
dodecanoic acid
-
CYP102A7, at pH 7.5
0.63
-
doxycycline
-
pH 8.5
25.65
-
hexadecanoic acid
-
CYP102A7, at pH 7.5, highest binding affinity
29.3
-
linoleic acid
-
CYP102A7, at pH 7.5
0.016
-
NADH
-
mutant A74G/F87V/L188Q
6
-
NADH
Q52TE7, -
pH 7.4, 25C
7
-
NADH
-
mutant A74G/F87V/L188Q/S965D
32
-
NADH
-
mutant A74G/F87V/L188Q/R966D
37.83
-
NADH
-
mutant A74G/F87V/L188Q/R966M
46.83
-
NADH
-
mutant A74G/F87V/L188Q
89
-
NADH
-
mutant A74G/F87V/L188Q/W1046A
105.2
-
NADH
-
mutant A74G/F87V/L188Q/W1046A
156
-
NADH
-
mutant A74G/F87V/L188Q/W1046S
0.43
-
NADPH
-
mutant F87A
0.45
-
NADPH
-
wild-type enzyme
0.5
-
NADPH
-
mutant F87G
0.83
-
NADPH
-
mutant A74E/F87V/P386S
1.11
-
NADPH
-
pH 8.5
1.7
-
NADPH
-
mutant A74G/F87V/L188Q
5.67
-
NADPH
-
mutant A74G/F87V/L188Q/S965D
6.5
-
NADPH
-
mutant A74G/F87V/L188Q/W1046A
9.3
-
NADPH
-
mutant A74G/F87V/L188Q/R966M
9.83
-
NADPH
-
mutant A74G/F87V/L188Q/W1046S
12.75
-
NADPH
Q52TE7, -
pH 7.4, 25C
132.2
-
NADPH
-
mutant A74G/F87V/L188Q
183
-
NADPH
-
mutant A74G/F87V/L188Q/R966D
362.8
-
NADPH
-
mutant A74G/F87V/L188Q/R966M
1.3
-
omega-(p-nitrophenyl)decanoic acid
-
pH 8.0, mutant A74G/F88V/S189Q
1.5
-
omega-(p-nitrophenyl)decanoic acid
-
pH 8.0, wild-type
1.3
-
omega-(p-nitrophenyl)dodecanoic acid
-
pH 8.0, mutant A74G/F88V/S189Q
3.1
-
omega-(p-nitrophenyl)dodecanoic acid
-
pH 8.0, wild-type
0.4
-
omega-(p-nitrophenyl)octanoic acid
-
pH 8.0, wild-type
3.5
-
omega-(p-nitrophenyl)octanoic acid
-
pH 8.0, mutant A74G/F88V/S189Q
1.3
-
Oxytetracycline
-
pH 8.5
22.8
-
palmitoleic acid
-
CYP102A7, at pH 7.5
16.18
-
stearic acid
-
CYP102A7, at pH 7.5
0.32
-
tetracycline
-
pH 8.5
59.8
-
tetradecanoic acid
-
CYP102A7, at pH 7.5, highest activity
0.12
-
minocycline
-
pH 8.5
additional information
-
additional information
-
Kcat-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds
-
additional information
-
additional information
-
scanning chimeragenesis succeeds in changing bacterial monooxygenase CYP102A1 into an enzyme capable of carrying out the major reaction of insect terpenoid omega-hydroxylase CYP4C7, with a 100fold increase in turnover number
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
anastrozole
-
P450 19A1
0.0008
0.0009
bitertanol
-
7-ethoxyresorufin O-deethylation is inhibited by the fungicide bitertanol, IC50: 800-900 nM
0.00043
-
formestane
-
P450 19A1
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2e-08
-
-
liver microsomes, 7-ethoxycoumarin-O-deethylase activity, in presence of 0.12 mM Cd2+
3e-08
-
-
liver microsomes, 7-ethoxyresorufin-O-deethylase activity, in presence of 0.12 mM Cd2+
3.4e-08
-
-
liver microsomes, 7-ethoxycoumarin-O-deethylase activity, in presence of 0.12 mM Cd2+
3.7e-08
-
-
liver microsomes, aminopyrene-N-demethylation activity, in presence of 0.12 mM Cd2+
4e-08
-
-
liver microsomes, aminopyrene-N-demethylation activity, in presence of 0.12 mM Cd2+
6.6e-08
-
-
liver microsomes, 7-ethoxyresorufin-O-deethylase activity, in presence of 0.12 mM Cd2+
7e-08
-
-
liver microsomes, 7-ethoxyresorufin-O-deethylase activity, in presence of 0.12 mM Cd2+
1.5e-07
-
-
liver microsomes, 7-ethoxycoumarin-O-deethylase activity, in presence of 0.12 mM Cd2+
2.57e-06
-
-
liver microsomes, 7-ethoxyresorufin-O-deethylase activity, in absence of Cd2+
3.81e-06
-
-
liver microsomes, 7-ethoxyresorufin-O-deethylase activity, in absence of Cd2+
3.85e-06
-
-
liver microsomes, 7-ethoxycoumarin-O-deethylase activity, in absence of Cd2+
3.25e-05
-
-
liver microsomes, aminopyrene-N-demethylation activity, in absence of Cd2+
3.77e-05
-
-
liver microsomes, 7-ethoxycoumarin-O-deethylase activity, in absence of Cd2+
0.0002166
-
-
liver microsomes, aminopyrene-N-demethylation activity, in absence of Cd2+
0.001
0.06
-
purified recombinant Ema1 and Ema16 proteins
0.012
-
-
roots, not exposed to anthraquinone-2,6-disulfonic acid; roots, not exposed to anthraquinone-2-sulfonic acid
0.0126
-
-
shoots, exposed to anthraquinone-1,5-disulfonic acid
0.0156
-
-
shoots, not exposed to anthraquinone-1-sulfonic acid
0.0156
-
-
shoots, exposed to anthraquinone-1-sulfonic acid
0.0186
-
-
shoots, not exposed to anthraquinone-1-sulfonic acid
0.021
-
-
roots, exposed to anthraquinone-1,5-disulfonic acid; shoots, exposed to anthraquinone-1-sulfonic acid
0.0246
-
-
shoots, not exposed to anthraquinone-1,5-disulfonic acid
0.025
-
-
roots, not exposed to anthraquinone-1-sulfonic acid
0.025
-
-
shoots, exposed to anthraquinone-1,8-disulfonic acid
0.027
-
-
roots, exposed to anthraquinone-2-sulfonic acid; roots, not exposed to anthraquinone-2-sulfonic acid
0.028
-
-
shoots, exposed to anthraquinone-2-sulfonic acid
0.0288
-
-
roots, exposed to anthraquinone-1,5-disulfonic acid
0.029
-
-
roots, exposed to anthraquinone-1-sulfonic acid
0.029
-
-
roots, exposed to anthraquinone-2,6-disulfonic acid
0.031
-
-
roots, exposed to anthraquinone-1,8-disulfonic acid; roots, exposed to anthraquinone-2-sulfonic acid
0.032
-
-
shoots, exposed to anthraquinone-2-sulfonic acid
0.032
-
-
roots, exposed to anthraquinone-1-sulfonic acid; shoots, exposed to anthraquinone-2,6-disulfonic acid
0.034
-
-
shoots, not exposed to anthraquinone-1,8-disulfonic acid
0.037
-
-
roots, exposed to anthraquinone-2,6-disulfonic acid
0.037
-
-
shoots, not exposed to anthraquinone-2-sulfonic acid
0.038
-
-
roots, not exposed to anthraquinone-2,6-disulfonic acid; shoots, not exposed to anthraquinone-2,6-disulfonic acid
0.039
-
-
shoots, exposed to anthraquinone-2,6-disulfonic acid
0.043
-
-
shoots, exposed to anthraquinone-1-sulfonic acid
0.0498
-
-
roots, exposed to anthraquinone-2-sulfonic acid
0.05
-
-
roots, exposed to anthraquinone-2,6-disulfonic acid
0.056
-
-
shoots, not exposed to anthraquinone-1-sulfonic acid
0.077
-
-
shoots, not exposed to anthraquinone-2,6-disulfonic acid
0.083
-
-
shoots, not exposed to anthraquinone-2-sulfonic acid
0.1
-
-
shoots, exposed to anthraquinone-2,6-disulfonic acid
0.102
-
-
roots, not exposed to anthraquinone-2-sulfonic acid
0.116
-
-
shoots, exposed to anthraquinone-2-sulfonic acid
0.12
-
-
roots, not exposed to anthraquinone-2,6-disulfonic acid
0.122
-
-
shoots, not exposed to anthraquinone-2,6-disulfonic acid
0.139
-
-
shoots, not exposed to anthraquinone-2-sulfonic acid
0.204
-
-
styrene monooxygenase overall reaction, substrate styrene, recombinantpurified refolded StyA with electrochemical FAD reduction, pH 7.5, 30C
0.226
-
-
styrene monooxygenase overall reaction, substrate methylphenylsulfide, recombinant purified refolded StyA with electrochemical FAD reduction, pH 7.5, 30C
0.312
-
-
styrene monooxygenase overall reaction, substrate 4-chlorostyrene, recombinant purified refolded StyA with electrochemical FAD reduction, pH 7.5, 30C; styrene monooxygenase overall reaction, substrate 4-methylstyrene, recombinant purified refolded StyA with electrochemical FAD reduction, pH 7.5, 30C
0.376
-
-
styrene monooxygenase overall reaction, substrate dihydronaphthalene, recombinant purified refolded StyA with electrochemical FAD reduction, pH 7.5, 30C
60
-
-
FAD-reducing activity, recombinant purified refolded StyAB, pH 7.5, 30C
additional information
-
-
effect of toxification on hepatic metabolism and biotransformation enzyme levels, quantitative analysis, overview
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
toward p-chlorothioanisole
7.2
-
-
assay at
7.4
-
Q52TE7, -
assay at
7.4
-
-
inactive at pH 8.49.4
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
whole cell assay
7.5
-
-
assay at
7.5
-
-
assay at
8.4
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
recombinant Escherichia coli cell expressing the enzyme, below 7.0 or over 8.0 the enzyme activity decreases drastically, pH profile, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
25
Q52TE7, -
assay at
30
-
-
toward p-chlorothioanisole
30
-
-
whole cell assay
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
38
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
-
recombinant Escherichia coli cell expressing the enzyme, at higher temperatures over 30C, the activity decreases significantly, temperature profile, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.17
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
CYP1A1 and CYP1A2
Manually annotated by BRENDA team
-
especially in proximal tubule, lower expression in the preglomerular microvessel, glomerulus and thick ascending limb
Manually annotated by BRENDA team
Q38Q84, Q38Q85, Q38Q86, Q38Q87
-
Manually annotated by BRENDA team
-
hepatic mixed-function oxidase
Manually annotated by BRENDA team
A7UDB5, A7UDB6
;
Manually annotated by BRENDA team
A7UDB5, A7UDB6
-
Manually annotated by BRENDA team
Q2I129
predominantly, 17times higher expression than in testis
Manually annotated by BRENDA team
Q2I129
much less
Manually annotated by BRENDA team
Orobanche ramosa, Sorghum sp.
-
-
Manually annotated by BRENDA team
Q2I129
barely, almost undetectable
Manually annotated by BRENDA team
-
CYP1A1, CYP1A2 and CYP1B1
Manually annotated by BRENDA team
additional information
-
isozyme tissue-specific expression analysis, regulation by PPAR
Manually annotated by BRENDA team
additional information
Q5KQH7
expression of Eui is tightly regulated during plant development with the stagespecific eui phenotypes, overview
Manually annotated by BRENDA team
additional information
Q2I129
genes differentially expressed during the sex change process
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in n-hexadecane-grown cells
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324
-
in n-hexadecane-grown cells
-
Manually annotated by BRENDA team
-
the majority of human P450s are targeted to the endoplasmic reticulum by a leader sequence that forms a transmembrane helix that anchors microsomal P450s to the cytoplasmic surface of the endoplasmic reticulum
Manually annotated by BRENDA team
Q5KQH7
the EUI protein is anchored on the endoplasmic reticulum towards the cytoplasm
Manually annotated by BRENDA team
-
16 different cytochrome P-450 have been isolated from mouse liver of which each contains numerous different forms of P-450
-
Manually annotated by BRENDA team
-
P450s generally exhibit membrane targeting sequences that precede the catalytic domain
-
Manually annotated by BRENDA team
-
in glucose-grown cells
-
Manually annotated by BRENDA team
-
predominantly in hepatic fractions
-
Manually annotated by BRENDA team
Q38Q84, Q38Q85, Q38Q86, Q38Q87
-
-
Manually annotated by BRENDA team
A7UDB5, A7UDB6
;
-
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324
-
in glucose-grown cells
-
-
Manually annotated by BRENDA team
-
light mitochondrial fraction, in glucose-grown cells
Manually annotated by BRENDA team
Aspergillus terreus MTCC 6324
-
light mitochondrial fraction, in glucose-grown cells
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44000
-
-
gel filtration
57900
-
A7UDB5, A7UDB6
sequence analysis
58500
-
A7UDB5, A7UDB6
sequence analysis
87190
-
-
sequence analysis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 52000, SDS-PAGE
?
Q52TE7, -
x * 89000, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 110000, SDS-PAGE
?
-
x * 58200, amino acid sequence calculation
?
-
x * 50000-52000, CYP4A isoforms, SDS-PAGE
?
-
x * 120000, SDS-PAGE
?
Aspergillus terreus MTCC 6324
-
x * 110000, SDS-PAGE
-
?
Bacillus licheniformis DSM13
-
x * 120000, SDS-PAGE
-
?
Claviceps purpurea P1
-
x * 58200, amino acid sequence calculation
-
dimer
-
StyA
dimer
-
StyA
-
monomer
-
x * 44000, SDS-PAGE and deduced from gene sequence
additional information
-
secondary and tertiary structures of CYPs, a short hydrophilic linker region between the transmembrane domain and the catalytic domain which begins with the proline rich sequence motif, overview, function-structure relationship
additional information
-
structure-function relationship
additional information
-
structure alteration due to organic solvents, analysis by molecular dynamics simulation study using the X-ray P450 BM-3 crystal structure, PDB code 1BU7
additional information
-
the enzyme is a membrane-bound heme protein, that consists of a protoporphyrin IX and an apoprotein, which confers the substrate specificity
additional information
-, Q4G2S1, Q4G2S2, Q4G2S3, Q4L230, Q4L231
structural analysis; structural analysis; structural analysis; structural analysis; structural analysis; structural analysis of all cytochrome P450 monooxygenases
additional information
-
the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain
additional information
Q70KH6
overall three-dimensional architecture of AurH and structure comparison, structure-function relationship analysis by computational docking, site-directed mutagenesis, and chemical analyses, overview
additional information
Phanerochaete chrysosporium BKM-F-1767
-
structural analysis; structural analysis; structural analysis; structural analysis; structural analysis; structural analysis of all cytochrome P450 monooxygenases
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
lipoprotein
-
the enzyme contains 0.02 mg lipid/mg protein, lipid composition analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of the complex between the heme- and FMN-binding domains of the enzyme, crystals are grown at room temperature by liquid-liquid free interface diffusion in a capillary, the flavodoxin-like flavin domain is positioned at the proximal face of the heme domain
-
crystallization of the wild-type and mutant CYP102A1 with and without bound substrates and one including theFMNbinding domain
-
molecular dynamics simulations on two CYP102A1 mutants in complex with (-)-alpha-pinene to explore the molecular mechanism of substrate recognition and to predict regioselectivity.
P14779
purified frecombinant mutant nezyme H226Y in complex with bifonazole, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
homology model based on bacterial CYP102 and insect CYP6B4
-
four crystal structures of AurH variants in different conformational states and in complex with the P450 inhibitor ancymidol, X-ray diffraction structure determination and analysis at 1.54 A resolution
Q70KH6
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
results in a loss of coupling efficiency in the reaction with tetradecanoic acid
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27.5
-
-
half-life of CYP102A7 at room temperature approximately 100 min. Increased activity (115%) after incubation at 27.5C, higher temperatures result in a steady loss of activity against tetradecanoic acid. No activity after incubation at 60C
46
-
-
10 min, half-life, wild-type CYP102A1
50
-
-
in absence of NADPH, the enzyme retains about 85% of the CYP functional activity
61
-
-
10 min, half-life, engineered CYP102A1 heme domain which utilizes H2O2 as electron donor
additional information
-
-
melting temperatures of the CYP102A1 monooxygenase and the CYP102A1 reductase domain differ by about 15C: whereas Tm for the monooxygenase domain is 63C, it is only 48C for the reductase domain
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
not stable in NaCl above 150 mM
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DMSO
-
stable, and activity increases in presence of up to 25% DMSO (v/v)
DMSO
-
inactivation mechanism, the mutant F87A is more sensitive to DMSO than the wild-type enzyme due to the absence of the phenyl ring in the mutant which promotes interactions of the DMSO molecule with the heme iron resulting in water displacement by DMSO at the catalytic heme center, box by stacking equilibrated boxes of solvent molecules to, modeling of DMSO in the active site channel, overview
additional information
-
inactivation mechanism of monooxygenase P450 BM-3 by organic cosolvents: a molecular dynamics simulation study using the X-ray P450 BM-3 crystal structure, PDB code 1BU7
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, partially purified enzyme in ammoniums sulfate-containing solution, quite stable
-
0-3C, purified enzyme, fully active when for up to 2 weeks, but loss of 20-40% activity every time the preparation is frozen and thawed
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CYP102A7 purified by immobilised metal affinity chromatography using the N-terminally attached His6-tag, 6.6fold, ca. 95% pure
-
several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes
-
recombinant protein, purified protein gives a yellow solution
-
native enzyme partially by microsome preparation
-
partially by microsome preparation
-
partially by microsome preparation
-
recombinant enzyme from Escherichia coli by anion exchange chromatography and gel filtration to homogeneity
-
native enzyme partially by microsome preparation
-
partially by microsome preparation
-
partially by preparation of subcellular fractions
-
partial
-
CYP1A2 with NADPH-cytochrome P450 reductase preparation of endoplasmic reticulum membranes from microsomes, formation into lipid vesicles. the lipid composition of purified lipid vesicles affects CYP1A2 substrate metabolism and NADPH-cytochrome P450 reductase-CYP1A2 binding
-
recombinant mutant H226Y from Escherichia coli by ion exchange chromatography and ultracentrifugation
-
recombinant StyB from Escherichia coli strain BL21 after refolding from inclusion bodies
-
partially by microsome preparation
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography
Q52TE7, -
gel filtration
-
native enzyme partially by microsome preparation
-
partially by microsome preparation
-
Ni-NTA column chromatography, gel filtration
-
recombinant His-tagged Ema1 and Ema16 from Escherichia coli to near-homogeneity by a two-step purification procedure
-
recombinant His-tagged PikC from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
partially by microsome preparation, and further by detergent solubilization, ammonum sulfate fractionation, anion exchange chromatography, gel filtration, and preparative disc electrophoresis
-
in two steps by nickel chelating column chromatography followed by anion exchange column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into pET21a vector, amplified in Escherichia coli DH5alpha cells and expressed under control of the T7 promoter in Escherichia coli BL21 Star (DE3); into pET21a vector, amplified in Escherichia coli DH5alpha cells and expressed under control of the T7 promoter in Escherichia coli BL21 Star (DE3); into pET21a vector, amplified in Escherichia coli DH5alpha cells and expressed under control of the T7 promoter in Escherichia coli BL21 Star (DE3); into pET21a vector, amplified in Escherichia coli DH5alpha cells and expressed under control of the T7 promoter in Escherichia coli BL21 Star (DE3); into pET21d vector, amplified in Escherichia coli DH5alpha cells and expressed under control of the T7 promoter in Escherichia coli BL21 Star (DE3)
-, Q735A2, Q735B3, Q737F3, Q737I9, Q737J4
plasmid propagation in Escherichia coli DH5alpha, heterologous expression of CYP102A1, CYP102A2, CYP102A3 and CYP102A7 from vector pET 28a(+) in Escherichia coli BL21 (DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli BL21 (DE3) using the pET281 expression system
P14779
expression in Escherichia coli in fed-batch fermentation
-
homologous peptide fragments of terpene omega-hydroxylase CYP4C7 from Diploptera punctata inserted into CYP102A1
-
expression in Escherichia coli in fed-batch fermentation
-
expression in Escherichia coli
-
both isozymes CYP52A13, CYP52A17
-
gene cloA, localization in the ergot alkaloid gene cluster, DNA and amino acid sequence determination and analysis, complementation of enzyme-deficient mutant DELTAP450-1
-
baculovirus-infected insect cells expressing single c-DNA-derived CYPs; baculovirus-infected insect cells expressing single c-DNA-derived CYPs; baculovirus-infected insect cells expressing single c-DNA-derived CYPs; baculovirus-infected insect cells expressing single c-DNA-derived CYPs; baculovirus-infected insect cells expressing single c-DNA-derived CYPs; baculovirus-infected insect cells expressing single c-DNA-derived CYPs
P11509
coexpression of CYP1A2 with the Y459H and V492E mutant POR alleles in tBTC1A2_POR cell-models
-
expression analysis of human CYPS, overvuew, expression in Escherichia coli without the N-terminal leader sequence
-
expression in V79 Chinese hamster fibroblasts and Hep-G2 cells, coexpression with N(O)-acetyltransferase or sulfotransferase 1A1-1
-
expression of recombinant human P4502B6 and yeast reductase fused enzyme in transgenic tobacco plants, integration into the tobacco genome, functional expression of CYP1A1 and CYP1A1-yeast reductase fused enzyme in transgenic potato plants, genetic transformation is mediated by Agrobacterium tumefaciens
-
microsomes derived from baculovirus infected insect cells expressing CYP1A2; microsomes derived from baculovirus infected insect cells expressing CYP2B6; microsomes derived from baculovirus infected insect cells expressing CYP2C8; microsomes derived from baculovirus infected insect cells expressing CYP2C9, CYP2C19, CYP2E1, CYP3A4, or CYP19; microsomes derived from baculovirus infected insect cells expressing CYP2D6; microsomes derived from baculovirus infected insect cells expressing CYP3A5; microsomes derived from baculovirus infected insect cells expressing CYP3A7
P24462
recombinant cDNA P450s coexpressed with cytochrome P450 reductase in insect cell microsomes
-
recombinant expression in Escherichia coli
-
V79-hCYP2E1 (constructed by transfection of CYP2E1-expressing vector pSV together with vector pSV2neo containing a G418-selective marker into V79-Mz cells) and SULT1A1 expression vector introduced into this cell line
-
;
A7UDB5, A7UDB6
CYP82E2, DNA and amino acid sequence determination and analysis, microarray-based strategy to identify genes that are differentially regulated between closely related tobacco lines that accumulate either nicotine, termed nonconverters, or nornicotine, termed converters, as the predominant alkaloid in the cured leaf, expression in Saccharomyces cerevisiae strain WAT11, overexpression in transgenic tobacco plants; CYP82E3, DNA and amino acid sequence determination and analysis, microarray-based strategy to identify genes that are differentially regulated between closely related tobacco lines that accumulate either nicotine, termed nonconverters, or nornicotine, termed converters, as the predominant alkaloid in the cured leaf, expression in Saccharomyces cerevisiae strain WAT11, overexpression in transgenic tobacco plants; CYP82E4v1, DNA and amino acid sequence determination and analysis, microarray-based strategy to identify genes that are differentially regulated between closely related tobacco lines that accumulate either nicotine, termed nonconverters, or nornicotine, termed converters, as the predominant alkaloid in the cured leaf, expression in Saccharomyces cerevisiae strain WAT11, overexpression in transgenic tobacco plants; CYP82E4v2, DNA and amino acid sequence determination and analysis, microarray-based strategy to identify genes that are differentially regulated between closely related tobacco lines that accumulate either nicotine, termed nonconverters, or nornicotine, termed converters, as the predominant alkaloid in the cured leaf, expression in Saccharomyces cerevisiae strain WAT11
Q38Q84, Q38Q85, Q38Q86, Q38Q87
expression of mutant H226Y in Escherichia coli
-
gene eui, i.e. elongated uppermost internode, map-based cloning, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of EUI in Saccharomyces cerevisiae strain WAT11 microsomes, expression of a chimeric EUIGFP in onion epidermic cells with localization in the cytoplasm on the surface of the endoplamic reticulum
Q5KQH7
DNA and amino acid sequence determination and analysis, and genetic structure and organization analysis of several genes, classification of 12 families and 23 subfamilies, two representative multigene P450 families CYP63 and CYP505, i.e. P450foxy, complex structural features of the P450 genes in this genome, including microexons, of 2-10 amino acids, and frequent small introns of 45-55 base pairs, tandem gene clusters, alternative splicing and functional diversity, phylogenetic analysis of the gene families, detailed overview; DNA and amino acid sequence determination and analysis, and genetic structure and organization analysis, phylogenetic analysis, overview; DNA and amino acid sequence determination and analysis, and genetic structure and organization analysis, phylogenetic analysis, overview; DNA and amino acid sequence determination and analysis, and genetic structure and organization analysis, phylogenetic analysis, overview; DNA and amino acid sequence determination and analysis, and genetic structure and organization analysis, phylogenetic analysis, overview; DNA and amino acid sequence determination and analysis, and genetic structure and organization analysis, phylogenetic analysis, overview
-, Q4G2S1, Q4G2S2, Q4G2S3, Q4L230, Q4L231
genetic organization of StyA/StyB from Pseudomonas sp. VLB120, overview. Expression of StyB in Escherichia coli strain BL21 inclusion bodies
-
expression anbalysis at restricted feeding versus ad libitum
-
functional expression of the fused enzyme between rat CYP1A1 and rat or yeast reductase in transgenic tobacco and potato plants mainly in microsomes
-
DNA sequence and genomic organization determination and analysis, usage of directional genome walking method, overexpression of His6-tagged enzyme in Escherichia coli starin BL21(DE3)
Q52TE7, -
expression of wild-type and mutant enzymes in Escherichia coli NovaBlue(DE3)
-
high level and functional expression of P450SMO in Escherichia coli strain BL21, method optimization and evaluation, overview
-
into the pET28a (+) vector and expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
gene family Ema, DNA and amino acid sequence determination and analysis
-
gene family ema, DNA and amino acid sequence determination and analysis, overexpression of His-tagged ema1 and ema16 in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli and Streptomyces lividans
-
gene pikC, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
chimeric oxygenase, in which the P450cam domain is fused to the reductase host domains of a P450RhF from Rhodococcus sp. strain NCIMB 9784. Plasmids containing the P450cam-RhFRed gene (L1-L7) transformed into Escherichia coli BL21-DE3cells
-
gene crtS, DNA and amino acid sequence determination of different strains
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract results in a slight decrease of CYP1A2 (30%) enzymatic activities; in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract results in a slight decrease of CYP2E1 (20%) enzymatic activities, whereas CYP2C9- and CYP3A4-dependent monooxygenase activities are significantly decreased by 40% and 60%, respectively. Andrographolide causes a 30% decrease in CYP2C9- and CYP3A4-dependent monooxygenase activities, which is not significant
-
resveratrol inhibits dioxin-induced expression of CYP1A1, CYP1A2 and CYP1B1 by directly or indirectly inhibiting the recruitment of the transcription factors aryl hydrocarbon receptor and aryl hydrocarbon nuclear translocator to the xenobiotic response elements of the corresponding genes
-
mutations in NADPH-P450 reductase, identified in patients with disordered steroidogenesis/Antley-Bixler syndrome, reduce CYP3A4 activity. NADPH-P450 reductase mutants Y181D, A457H, Y459H, V492E and R616X loose more than 99% of CYP3A4 activity, while NADPH-P450 reductase mutations A287P, C569Y and V608F loose 60-85% activity
-
beta-naphthoflavone (0.05 mM) causes a 9fold increase in CYP1A2-dependent activity and a 25fold increase in CYP1A2 mRNA expression in hepatocyte microsomes; dexamethasone (0.05 mM) and rifampicin (0.01 mM) increase CYP3A4 mRNA expression by a mean of 14fold in hepatocytes
-
V79-hCYP2E1-hSULT1A1 cells contain a higher level of hCYP2E1 protein than the parental V79-hCYP2E1 line (by a factor of 34)
-
0.0001 mM dioxin treatment for 24, 48, and 72 h induces CYP1A1, CYP1A2 and CYP1B1 mRNA levels
-
exposure to both 2,3,7,8-tetrachlorodibenzofuran and 2,3,4,7,8-pentachlorodibenzofuran results in dose-dependent increase of CYP1A2 mRNA due to an underlying aryl hydrocarbon receptor-mediated mechanism; exposure to both 2,3,7,8-tetrachlorodibenzofuran and 2,3,4,7,8-pentachlorodibenzofuran results in dose-dependent increases of CYP1A1 mRNA and CYP1A protein levels due to an underlying aryl hydrocarbon receptor-mediated mechanism. Upregulation of CYP1A mRNA in liver is more consistent to the sum adipose 2,3,7,8-tetrachlorodibenzo-p-dioxin equivalent concentration than to the liver 2,3,7,8-tetrachlorodibenzo-p-dioxin equivalent concentration in minks treated with 2,3,7,8-tetrachlorodibenzofuran or 2,3,4,7,8-pentachlorodibenzofuran
A7UDB5, A7UDB6
some P450 genes are downregulated in nutrient-rich malt extract cultures (2.15- to 13.36fold) or in defined low-nitrogen cultures (2.02- to 4.15fold) in response to nonylphenol
-
significant induction of multiple P450 monooxygenase genes by nonylphenol in nutrient-rich malt extract cultures (2- to 195fold) or under defined low-nitrogen conditions (2- to 6fold)
-
some P450 genes are downregulated in nutrient-rich malt extract cultures (2.15- to 13.36fold) or in defined low-nitrogen cultures (2.02- to 4.15fold) in response to nonylphenol
Phanerochaete chrysosporium BKM-F-1767
-
-
significant induction of multiple P450 monooxygenase genes by nonylphenol in nutrient-rich malt extract cultures (2- to 195fold) or under defined low-nitrogen conditions (2- to 6fold)
Phanerochaete chrysosporium BKM-F-1767
-
-
in hepatocyte cultures, treated with 0.05 mM Andrographis paniculata extract and Andrographolide, CYP2E1 is not significantly decreased (by 30%); in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract and Andrographolide results in a 50% decrease in CYP3A1 expression and activity; in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract and Andrographolide results in a 60% decrease in CYP1A2 expression and activity; in hepatocyte cultures, treatment with 0.05 mM Andrographis paniculata extract and Andrographolide results in a 60% decrease in CYP2C11 expression and activity. After in vivo administration, Andrographis paniculata extract at dose levels of 0.5 g/kg/day (i.e. 5 mg/kg/day Andrographolide equivalents) and at 2.5 g/kg/day (i.e. 25 mg/kg/day Andrographolide equivalents) and Andrographolide at dose levels of 5 and 25 mg/kg/day significantly decrease CYP2C11 activity
P04799, P04800, P05182, P08683
beta-naphthoflavone (0.05 mM) causes a 71fold increase in CYP1A2-dependent activity and a 253fold increase in CYP1A2 mRNA expression in hepatocyte microsomes; dexamethasone (0.05 mM) and rifampicin (0.01 mM) increase CYP2C11 activity by a mean of 1.4fold in hepatocytes; dexamethasone (0.05 mM) increases CYP3A1 activity by a mean of 6fold and dexamethasone (0.05 mM) and rifampicin (0.01 mM) increase CYP3A1 mRNA expression by a mean of 167fold in hepatocytes
P04799, P04800, P05182, P08683
dexamethasone-mediated CYP3A induction
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A74E/F87V/P386S
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity, and cofactor specificity compared to the wild-type mutant
A74G/F87G/L188Q
P14779
site-directed mutagenesis. The introduction of a smaller amino acid at position 87 results in a more active monooxygenase and a different product profile for the oxidation of substrate (-)-alpha-pinene.
A74G/F87V/L188Q
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
A74G/F87V/L188Q
P14779
site-directed mutagenesis. The introduction of a smaller amino acid at position 87 results in a more active monooxygenase and a different product profile for the oxidation of substrate (-)-alpha-pinene.
A74G/F87V/L188Q/R966D
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/R966M
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/S965D
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/W1046A
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/F87V/L188Q/W1046S
-
site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme
A74G/L188Q
P14779
site-directed mutagenesis. MD simulations of the double mutant A74G L188Q (GQ) show that the substrate is blocked from accessing the heme oxygen by the side chain of the F87, when it adopts the conformation found in the X-ray structure.
F87A
-
site-directed mutagenesis, the mutant exhibits an altered regioselectivity and substrate specificity compared with wild-type, it has lower tolerance toward DMSO
F87G
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
R47E
-
the mutant enzyme retains significant hydroxylase activity towards saturated fatty acids and shows much increased activity towards C12-C16 alkyl trimethylammonium compounds
A74G/F88V
-
substrate specificity similar to wild-type
A74G/F88V/S189Q
-
substrate spectrum much broader than for wild-type
F116A
-
no enzymatic activity
F116C
-
no enzymatic activity
F116H
-
no enzymatic activity
F116I
-
no enzymatic activity
F116L
-
no enzymatic activity
F116L/F484L
-
no enzymatic activity
F116L/F484Y
-
no enzymatic activity
F116S
-
no enzymatic activity
F116V
-
no enzymatic activity
F116W
-
some enzymatic activity against bergapten, xanthotoxin
F116Y
-
reduced enzymatic activity
F116Y/F484H
-
no enzymatic activity
F116Y/F484Y
-
no enzymatic activity
F206L
-
no enzymatic activity
F484C
-
no enzymatic activity
F484D
-
no enzymatic activity
F484H
-
no enzymatic activity
F484L
-
no enzymatic activity
F484S
-
no enzymatic activity
F484V
-
no enzymatic activity
F484W
-
no enzymatic activity
F484Y
-
no enzymatic activity
H117A
-
no enzymatic activity
H117F
-
no enzymatic activity
H117L/F484Y
-
no enzymatic activity
H117V
-
no enzymatic activity
H117Y
-
no enzymatic activity
H204L
-
activity similar to wild-type
V368A
-
activity similar to wild-type; no enzymatic activity
V368F
-
no enzymatic activity
F87GA
-
site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant
additional information
-
the enzyme is a target for improving the catalytic performance of P450 BM-3 toward nonnatural substrates of industrial importance in the presence of organic solvents or cosolvents for industrial applications
additional information
-
construction of an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH
A74G/S189Q
-
substrate specificity similar to wild-type
additional information
-
construction of a disrution-inactivated, enzyme-deficient mutant DELTAP450-1, that accumulates agroclavine, elymoclavine, and chanoclavine, but not ergopeptines, feeding experiments
additional information
Claviceps purpurea P1
-
construction of a disrution-inactivated, enzyme-deficient mutant DELTAP450-1, that accumulates agroclavine, elymoclavine, and chanoclavine, but not ergopeptines, feeding experiments
-
additional information
-
genetic variations, substantial effects of single nucleotide polymorphisms, e.g. CYP2D6 and CYP2C19 SNPs show large e.ects on metabolism of debrisoquine and (S)-mephenytoin, respectively, overview
additional information
-
transgenic tobacco plants expressing rat CYP1A1 and its fused enzyme with yeast reductase showed tolerance to the herbicide chlorotoluron, some of them are tolerant to the herbicides diuron and atrazine, the transgenic plants also show increased activity against 7-ethoxycoumarin, overview
additional information
Q38Q84, Q38Q85, Q38Q86, Q38Q87
construction of transgenic plants overexpressing the enzyme, analysis of alkaloid spectrum, overview; construction of transgenic plants overexpressing the enzyme, analysis of alkaloid spectrum, overview; construction of transgenic plants overexpressing the enzyme, analysis of alkaloid spectrum, overview
additional information
-
the herbicide chlorotoluron delayed the germination and development of Orobanche ramosa seeds in case of use of transgenic plants tolerant to the herbicide
H226Y
-
site-directed mutagenesis, altered coordination of the Fe2+ ion and binding of inhibitor bifonazole
additional information
Q5KQH7
construction of the recessive elongated uppermost internode tall mutant, which is morphologically normal until its final internode elongates drastically at the heading stage, the stage-specific developmental effect of the eui mutation is used in the breeding of hybrid rice to improve the performance of heading in male sterile cultivars, the eui mutant accumulates exceptionally large amounts of biologically active gibberellins in the uppermost internode, eui mutant plants and Eui-overexpressing transgenic plants show tall and dwarfed phenotypes, and fail to produce seeds, overview
V368L
-
activity similar to wild-type; no enzymatic activity
additional information
-
construction of a fused enzyme between rat CYP1A1 and rat reductase on microsomes in the recombinant yeast cells, which showed enhanced specific activity as compared with the original enzyme system
A86T/T91S/A109F/I179F/I267L
-
site-specific mutagenesis, mutant 70A08 shows 150fold increased dealkylation activity compared to the wild-type enzyme
additional information
-
site-specific mutagenesis and screening for a gain of function mutant of CYP116B3, dealkylation activity of 12 variants chosen from the primary screening, overview. Identification of a mutant 74H10 that shows a 240fold increased deethylation activity toward 7-ethoxycoumarin and a 10fold increased demethylation activity toward 7-methoxycoumarin
T91S/A109L/I179F/I267L
-
site-specific mutagenesis, mutant 74H10 shows 240fold increased dealkylation activity compared to the wild-type enzyme
additional information
-
transgenic potato plants expressing CYP1A1 and its fused enzyme with yeast reductase showed tolerance to the herbicide chlorotoluron, some of them are tolerant to the herbicides diuron and atrazine, the transgenic plants also show increased activity against 7-ethoxycoumarin, overview
additional information
Q70KH6
modification of the chemo- and regioselectivity of AurH by site-directed mutagenesis, yielding mutants that catalyze the regioselective six-electron transfer of a nonactivated methyl group to a carboxylic acid via hydroxyl and aldehyde intermediates, overview
additional information
-
construction of an enzyme deletion mutant strain HK954, showing blocked biosynthesis of endogenous macrolactone aglycones
additional information
-
construction and analysis of insertion mutant strains defective in biosynthesis of astaxanthin, the mutants are selected by accumulation of astaxanthin precursors
additional information
Xanthophyllomyces dendrorhous VKPM Y2410
-
construction and analysis of insertion mutant strains defective in biosynthesis of astaxanthin, the mutants are selected by accumulation of astaxanthin precursors
-
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant StyB from inclusion bodies after expression in Escherichia coli strain BL21
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
the enzyme is intersting for regioselective production of compounds
medicine
-
the two major mechanisms that confer resistance to permethrin in Culex mosquitoes are target site insensitivity (i.e. kdr) and enhanced detoxification by cytochrome P450 monooxygenases
synthesis
-
production of epoxides, aliphatic epoxides can be used to synthesize various chiral intermediates for the production of ferroelectric liquid crystals
synthesis
Gordonia rubripertincta B 276, Gordonia rubripertincta B-276
-
production of epoxides, aliphatic epoxides can be used to synthesize various chiral intermediates for the production of ferroelectric liquid crystals
-
agriculture
-
enzyme expressed in Oryza sativa results in high tolerance to herbicides mefenacet, pyributicarb, amiprofos-methyl, trifluralin, pendimethalin, norflurazon, chlorotoluron and five chloroacetamides
biotechnology
P24462
most Cree anti-diabetic plant ethanolic extracts have the potential to affect CYP2C- and 3A4-mediated metabolism, and have the potential to affect the bioavailability and pharmacokinetics of conventional and traditional medicines during concomitant use, thus there is a potential risk of interactions if these traditional medicines are used with conventional therapeutic products, but several extracts may also have the potential to pharmacoenhance the activity of some medicines; most Cree anti-diabetic plant ethanolic extracts have the potential to affect CYP2C- and 3A4-mediated metabolism, and have the potential to affect the bioavailability and pharmacokinetics of conventional and traditional medicines during concomitant use, thus there is a potential risk of interactions if these traditional medicines are used with conventional therapeutic products, but several extracts may also have the potential to pharmacoenhance the activity of some medicines
medicine
-
plasma concentration of 4beta-hydroxycholesterol may be used as an endogenous marker of CYP3A activity. Concentration of 4beta-hydroxycholesterol increases with the number of active CYP3A5 alleles in Koreans, Swedes and Tanzanians
agriculture
-
cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants
biotechnology
Q5KQH7
EUI and the GA metabolism pathway are useful targets for increasing the agronomic value of crops
synthesis
-
production of 6-beta-hydroxy-methyl-simvastatin, simvastatin and derivatives belong to the family of HMG-CoA reductase inhibitors, which are potent cholesterol-lowering therapeutic agents
biotechnology
-
enzymatic activity of P450SMO makes it an attractive biocatalyst for asymmetric synthesis of enantiopure sulfoxides
biotechnology
-
enzymatic activity of P450SMO makes it an attractive biocatalyst for asymmetric synthesis of enantiopure sulfoxides
-
agriculture
-
cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants
biotechnology
-
cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants
agriculture
-
the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology
environmental protection
-
the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology
agriculture
-
the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology
environmental protection
-
the enzyme is of great importance commercially not only from the point of view of herbicide resistance but also in terms of ecotoxicology
biotechnology
-
scanning chimeragenesis can be a useful method for producing new enzymatic products from CYP102A1 and may be used as a new systematic tool for changing substrate selectivity and regiospecificity among any two cytochromes P450 that have a common substrate, to study the interaction between enzymes and the substrate or to create new chimeric proteins for pharmaceutical and industrial uses
additional information
-
the enzyme is a target for improving the catalytic performance of P450 BM-3 toward nonnatural substrates of industrial importance in the presence of organic solvents or cosolvents for industrial applications
additional information
-
right immobilization conditions are important for developing a catalytically active P450 based biosensor
biotechnology
-
cytochrome P450 monooxygenase as a tool for metabolizing of herbicides in plants
additional information
-
the use of genetically engineered herbicide resistant plants is one of the most effective ways for broomrape control, since the parasitic plant damages the agriculturally important tobacco plants in Bulgaria, overview
medicine
-
2fold increase in enzyme activity on diet of total parenteral nutrition plus choline
additional information
-
rhubarb may be the most appropriate plant for the phytotreatment of organic pollutants by cytochrome P450 monooxygenase-catalysed reactions
additional information
Q52TE7, -
the Cyt P450 monooxygenases can be utilized in the bioremediation of pollutants, as these enzymes convert chemically inert compounds to more water-soluble, hydroxylated derivatives, which may be suitable substrates for many other enzymes