CYP1A1

Cytochrome P450 1A1

524 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

59.209 kDa

MMSMFRLSIPISASELLLASTVFCLVLWVVKAWQPRLPKGLKSPPGPWGWPVLGNVLTLGKSPHLALSRLSQRYGDVLQIRIGSTPVLVLSGLDTIRQALVRQGDDFKGRPDLYSFSLVTDGQSLTFSPDSGPVWAARRRLAQNALKSFSIASDPASSCSCYLEEHVSKEAEVLLSRLQEQMAEVGRFDPYRYIVVSVANVICAMCFSKRYDHDDQELLSLVNLSNEFGEGVASANPLDFFPILRYLPNPALDFFKDLNKRFYSFMQKMVKEHYKTFEKGQIRDVTDSLIEHCQDKRLDENANIQLSDEKIVNVVLDLFGAGFDTVTTAISWSLLYLVTNPNVQKKIQKELDTVIGRARQPRLSDRPQLPYMEAFILETFRHASFVPFTIPHSTTRDTSLSGFYIPKGRCVFVNQWQINHDQKLWGNPSEFQPERFLTLDGTINKALSEKVILFGLGKRKCIGETIARLEVFLFLAILLQQVEFSVPEGTKVDMTPIYGLTMKHARCEHFQVRVRTEGAESPAA

CYP1A1

Cytochrome P450 1A1

524 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

59.136 kDa

MSSIYGLLNFMSATELLLAITVFCLGFWVVRALRTQVPKGLKTPPGPWGLPILGHVLTLGKNPHLSLTKLSKQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDFYSFTLITNGKSMTFNPDCGPVWAARRRLAQDALKSFSIALDPASASSCYLEEYVIKEADYLISKFQKLMAEVGHFDPDRYLVVSVTNVICAMCFGQRYDHDDQELLSIVNLSNEFGKVTGSGYPPDFIPILRYLPNSSLDAFKDLNKKFYSFMQKSVKEHYRTFEKGHIRDITDSLIEHCQDKSLDENANVQLSDDRVINIIVDLFGAGFDTVTTAISWSLMYLVTNPGVQRKIQEELDTVIGRSRRPRLCDRSQLPYLEAFILETFRHSSFLPFTIPHSTTRDTSLCGFYIPKGHCVFVNQWQINHNQELWGDPNKFRPERFLTSSGTLDKVLSGKVTLFGLGKRKCIGETIGRLEVFLFLAILLQQIEFTVSPGEKVDMTPIYGLTLKHARCEYFQAQTRSSGPQHPQA

Cyp1a1

Cytochrome P450 1A1

524 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

59.23 kDa

MPSMYGLPAFVSATELLLAVTVFCLGFWVVRATRTWVPKGLKTPPGPWGLPFIGHMLTVGKNPHLSLTRLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVRQGDDFKGRPDLYSFTLITNGKSMTFNPDSGPVWAARRRLAQNALKSFSIASDPTSASSCYLEEHVSKEANYLVSKLQKVMAEVGHFDPYKYLVVSVANVICAICFGQRYDHDDQELLSIVNLSNEFGEVTGSGYPADFIPVLRYLPNSSLDAFKDLNDKFYSFMKKLIKEHYRTFEKGHIRDITDSLIEHCQDRKLDENANVQLSDDKVITIVLDLFGAGFDTVTTAISWSLMYLVTNPRVQRKIQEELDTVIGRDRQPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTTRDTSLNGFYIPKGCCVFVNQWQVNHDRELWGDPNEFRPERFLTPSGTLDKRLSEKVTLFGLGKRKCIGETIGRSEVFLFLAILLQQIEFKVSPGEKVDMTPTYGLTLKHARCEHFQVQMRSSGPQHLQA

Cyp1a1

Cytochrome P450 1A1

524 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions (By similarity). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (By similarity). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (By similarity). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (By similarity). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (By similarity).

Belongs to the cytochrome P450 family.

59.393 kDa

MPSVYGFPAFTSATELLLAVTTFCLGFWVVRVTRTWVPKGLKSPPGPWGLPFIGHVLTLGKNPHLSLTKLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVKQGDDFKGRPDLYSFTLIANGQSMTFNPDSGPLWAARRRLAQNALKSFSIASDPTLASSCYLEEHVSKEAEYLISKFQKLMAEVGHFDPFKYLVVSVANVICAICFGRRYDHDDQELLSIVNLSNEFGEVTGSGYPADFIPILRYLPNSSLDAFKDLNKKFYSFMKKLIKEHYRTFEKGHIRDITDSLIEHCQDRRLDENANVQLSDDKVITIVFDLFGAGFDTITTAISWSLMYLVTNPRIQRKIQEELDTVIGRDRQPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTIRDTSLNGFYIPKGHCVFVNQWQVNHDQELWGDPNEFRPERFLTSSGTLDKHLSEKVILFGLGKRKCIGETIGRLEVFLFLAILLQQMEFNVSPGEKVDMTPAYGLTLKHARCEHFQVQMRSSGPQHLQA

cyp1a1

Cytochrome P450 1A1

522 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.344 kDa

MVLMILPIIGSVSVSEGLVAIVTLCLVYMLMKYKHTEIPEGLKRLPGPKPLPIIGNVLEVYNNPHLSLTAMSERYGSVFQIQIGMRPVVVLSGNETVRQALIKQGEDFAGRPDLYSFKFINDGKSLAFSTDKAGVWRARRKLAMSALRSFATLEGTTPEYSCALEEHVCKEGEYLVKQLTSVMDVSGSFDPFRHIVVSVANVICGMCFGRRYSHDDQELLGLVNMSDEFGQVVGSGNPADFIPILRYLPNRTMKRFMDINDRFNNFVQKIVSEHYESYDKDNIRDITDSLIDHCEDRKLDENANIQVSDEKIVGIVNDLFGAGFDTISTALSWAVVYLVAYPEIQERLHQELKEKVGMIRTPRLSDKINLPLLEAFILEIFRHSSFLPFTIPHCTIKDTSLNGYFIPKDTCVFINQWQVNHDPELWKEPSSFNPDRFLSADGTELNKLEGEKVLVFGMDKRRCIGEAIGRNEVYLFLAILLQRLRFQEKPGHPLDMTPEYGLTMKHKRCQLKASMRPWGQEE

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

58.653 kDa

MALMILPFIGSVSVSESLVALTAVCLVYLILKFFRTEIPAGLRQLPGPKPLPIIGNVLEVGSKPHLSLTAMSKRYGDVFQIQIGMRPVVVLSGSETVRQALIKQGDEFSGRPDLYSFTFINDGKSLAFSTDQAGVCGACRKLAYSALRSFSTLDGTTPEYSCMLEEHICKEGECLINQLNTVMKADGSFDPFRHIVVSVANVICGMCFGRRYDHNDQDLLRLVNLSDEFGQVAGSGNPADFINILRFLPSTTMKKFMTINADFNTFVKKIVGEHYATFDKNNIRDITDSLIDHCEDRKLDENCNVQMSDEKIVGIVNDLFGAGFDTVSTALSWSVMYLVAYPDIQERLFQEIKDNVGLDRTPLLSDRSKVPYLEAFILELFRHSSFLPFTIPHCSAKDTSLNGYFIPKDTCVFINQWQINRDPELWKDPSSFNPDRFLSCNGTEVNKQEGEKVMVFGMGKRRCIGEVIARNEVYRGLAILIQRLQFHEMPGELLDMTPEYGLTMKHKRCHLRATMRARNEQ

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.064 kDa

MALMILPFIGALSVSESLVALVTVCLVYLIIKSFQANIPEGLSRLPGPKPLPIIGNVLEVGSRPYLSLTEMSKRYGNVFQIQIGMRPVVVLSGNETVRQALIKQGDEFAGRPDLYSFRFISEGKSLAFSTDQAGVWRARRKLAYSALRSFSTLEGTTPEYSCVLEEHISKEAEYLIKQLDTVMKADGSFDPFRYIVVSVANVICGMCFGRRYDHHDRELLSLVNLSDEFGQVVGSGNPADFIPILQYLPNKTMKKFVNINDRFISFVQKIVSEHYATFNKDNIRDITDSLIDHCEDRKLDENANVQMSDEKVVGIVNDLFGAGLDTISTALSWSVMYLVAYPEIQERLYQELKENVGLDRTPVLSDRNNLPLLEAFILEIFRHSSFLPFTIPHCTTKDTSLNGYYIPKDTCVFINQWQINHDPELWKEPSSFNPDRFLSADGTEVNKVDGEKVMVFGLGKRRCIGEVIARNEVYMFLAILIQKLHFYNLPGEPLDMTPEYGLTMKHKRCHLRATVRVRSDH

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.063 kDa

MMLMMLPFIGSVSVSESLVAMTTVCLVYLILKFFQTEIPEGLRRLPGPKPLPIIGNVLEMGSRPYLSLTAMSKRYGNVFQIQIGMRPVVVLSGSETVRQALIKQGDDFAGRPDLYSFRFINEGKSLAFSTDKAGIWRARRKLAYSALRSFATLEGTTPEYSCVLEEHVCKEGEYLIKQLNTAMTADGSFDPFRHIVVSVANVICGMCFGRRYDHDDQELVGLVTLSDEFGRVVGSGNPADFIPILQYLPSATMKNFLRINGRFTEFVQKIVTEHYTTFDKDNIRDITDSLIDHCEDRKLDENSNVQMSDEKIVGIVNDLFGAGFDTVSTALSWSVMYLVAHPEIQERLYQEIEDKVGLDRMPLLSDKPNLPFLEAFILEILRHSSFLPFTIPHCTTKDTSLNGYFIPKDTCVFINQWQINHDPEMWKDPSSFNPDRFLSADGSEVNKLDGEKVMAFGMGKRRCIGEVIARNEVYLFLAILIQKLHFLPIPGEKLDMTPEYGLTMKHKRCHLKATMRARNEH

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

58.944 kDa

MALMILPFIGALSVSESLVAVVTVCLVYLIIKSFQDKIPEGLSRLPGPKPLPIIGNVLEVGSRPYLSLTEMGKRYGNVFQIQIGMRPVVVLSGNETVRQALIKQGDEFAGRPDLYSFRFISEGKSLAFSTDQAGVWRARRKLAYSALRSFSTLEGTTPEYSCVLEEHISKEAKYLIQQLDTVMKADGSFDPFRYIVVSVANVICGMCFGRRYDHHDQELLSLVNLSDEFGQVVGSGNPADFIPILQYLPNKTMKKFVSINDRFISFVQKIVSEHYATFNKDNIRDITDSLIDHCEDRKLDENANVQMSDEKVVGIVNDLFGAGFDTISTALSWSVMYLVAYPEIQEXLYQELKENVGLDRTPVLSDRNNLPLLESFILEIFRHSSFLPFTIPHCTTKDTSLNGYYIPKDTCVFINQWQINHDPELWKEPSSFNPDRFLSADGTEVNKVDGEKVMIFGMGKRRCIGEVIARNEVYLFLAILIQKLHFCNLPGEPLDMTPEYGLTMKHKRCQLRATARVRSDH

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.247 kDa

MALIILPFIGSLSVSESLVALITICVVYLILTYSHTKIPAGLQRLPGPKPLPIIGNVLEIGRKPYQTLTALSKRYGPVFQIQIGMRPVVVLSGSETVRQALIKQGEDFSGRPDLYTFQFISDGKSLAFSTDKVGVWRARRKLAYSALRSFSSLESTNQEYSCMLEEHICKEGEYLVKQLNTSMKANGSFDPFRNIVVSVANVICGMCFGRRYDHYDQELVSLVNLSEEFGQVVGTGNLADFIPVLRFLPSTAMKKFLSINDRFDKFVKKIVSEHYATYNKDNIRDITDSLIDHCEDRKLDENCNVQVSDEKIVGIVNDLFGAGFDTVSTGLSWSVMYLVAYPEIQERLYQEIKDSVGTERMPLLSDRPSLPFLDAFILEIFRHSSFLPFTIPHCTTKNTSLNGYFIPKDTCVFINQWQINHDPELWKDPFSFNPERFLSADGTELNRLEGEKVMLFGLGKRRCIGEVIARNEVFLFLAIIIQRLQFHMLPGEPLDMTPEYGLTMKHKRCQLRATMREKNEQ

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

58.887 kDa

MALMVLPFIGPLSVLEGLIALTTVCVVYLLLKHFNKEIPGGLRQLPGPTPLPIIGNLLKLGSKPYLSLTEMSKRFGDVFQIQIGMRPVVVLSGNETVRQALIKQGDDFSGRPDLYSFQFINDGKSLAFSTDQAGVWRARRKLAYSALRSFSSLEGSNAEYSCMLEEHICKETEHLVKEIEKVMKTEGKFDPYRYIVVSVANVICGMCFGRRYDHHDQELVGLVNLSEDFVQVTGSGNPADFIPALRYLPSKAMKKFVEINNRFQSFVQKIVNEHSATYDKDNIRDITDSLIDHCEDRKLDENSNIQMSDEKVVGIVNDLFGAGFDTISTALSWAVGYLVAYPDIEKGLFEEIKENIGLNRNPTISDRSNLPLTDAFILEIFRHSSFLPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQINHDPKLWQDPSSFNPDRFLSEDGSEVNRLDGEKVMVFGLGKRRCIGEVIARNEVFLFLAIMIQKLCFEEMPGEPLDMTPEYGLTMKHKRCNVRASLRLKDGC

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.009 kDa

MMLMMLPFIGSVSVSESLVAMTTMCLVYLILKFFQTEIPEGLLRLPGPKPLPIIGNVLGLGSKPYLSLTDMSKRYGHVFQIQIGMRPVVVLSGSETVRQALIKQGDDFAGRPDLYSFRFINAGKSLAFSTDQAGVWRARRKLAYSALRSFSNLEGTTPEYSCVLEEHICKEGEYLIKQLNTVMKADGSFDPFRHIVVSVANVICGMCFGRRYDHDDQELVGLVTLSDEFGRVVGSGNPADFIPILQYLPSAAMKNFLRINSRFTEFVQKIVTEHYTTFDKDNIRDITDSLIDHCEDRKLDENSNVQMSDEKIVGIVNDLFGAGFDTVSTALSWSVMYLVAHPEIQERLYQEIEDKVGLDRMPLLSDKPNLPFLEAFILEILRHSSFLPFTIPHCTTKDTSLNGYFIPKDTCVFINQWQINHDPELWKDPSSFNPDRFLSADGSEVNKLDGEKVMAFGMGKRRCIGEVIARNEVYLFLAIIIQKLHFLPIPGEKLDMTPEYGLTMKHKRCHLKATMRARNEH

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.061 kDa

MMLMMLPFIGSVSVSESLVAMTTMCLVYLILKFFQTEIPEGLRRLPGPKPLPIIGNVLGLGSKPYLSLTAMSKRYGHVFQIQIGMRPVVVLSGTGTVRQALIKQGDEFAGRPDLYSFRFINAGKSLAFSTDQAGVWRARRKLAYSALRSFSTLEGTTPEYSCVLEEHICKEGEYLIKQLNTVMKADGSFDPFRHIVVSVANVICGMCFGRRYDHDDQELVSLVTLSDEFGRVVGSGNPADFIPILQYLPSAEMKNFLRINEHFTEFVQKIVTEHYTTFNKDNIRDITDSLIDHCEDRKLDENSNVQMSDEKIVGIVNDLFGAGFDTVSTALSWSVMYLVAHPEIQERLYQEIEDKVGLDRMPLLSDKPNLPFLEAFILEILRHSSFLPFTIPHCTTKDTSLNGYFIPKDTCVFINQWQINHDPELWKDPSSFNPDRFLSADGSEVNKLDGEKVMAFGMGKRRCIGEVIARNEVYLFLAIIIQKLHFLPIPGEKLDMTPEYGLTMKHKRCHLKATMRARNEH

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.122 kDa

MVLMILPFVGPVSVSESLVAIITMCLVYMILKFFRTEIPEGLCQLPGPKPLPIIGNVLEVGRNPYLSLTAMSKRYGDVFQIQIGMRPVVVLSGSETVRQALIKQGDDFAGRPDLYSFRFINDGKSLAFSTDQAGVWRARRKLAYSALRSFSTLEGTTPEYSCALEEHVSKEAEYLVKQLNTVMETDGSFDPFRHIVVSVANVICGMCFGRRYDHNNQELLNLVNLSDEFGQVVASGNPADFIPILQYLPSTSMKKFVSINDRFNAFVQKIVSEHYTTFDKDNIRDITDSLIDHCEDRKLDENSNVQMSDEKVVGIVNDLFGAGFDTISTALSWSVMYLVAYPEIQERLYQEMKESVGLDRTPCLSDKPKLPFLEAFILEIFRHSSFLPFTIPHCSSKDTSLNGYFIPKDTCVFINQWQINHDPELWKDPSSFNPDRFLNTDGTELNKLEGEKMMVFGLGKRRCIGEVIARNEVFLFLAILVQNLRFHAKPGEPLDMTPEYGLTMKHKRCHLRAAMRSRNEE

cyp1a1

Cytochrome P450 1A1

521 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

59.02 kDa

MVLMILPVIGSVSVSEGLVAMITMCLAYLILRLFRTEIPEGLLQLPGPKPLPIIGNVLEVGRNPYLSLTAMSKRYGDVFQIQIGMRPVVVLSGSETVRQALIKQGDXFAGRPDLYSFRFINDGKSLAFSTDQAGVWRARRKLAYSALRSFATLEGTTPEYSCALEEHVSKEAEYLVKQLHTVMEADGSFDPFRHIVVSVANVICGMCFGRRYDHNHQELLNLVNLSDEFGQVVASGNPADFIPILQYLPSTTMKKFLNINDRFNTFVQKIVSEHYTTFDKDNIRDITDSLIDHCEDRKLDENSNVQMSDEKIVGIVNDLFGAGFDTISTALSWSVMYLVAYPEIQERLYQEMNETVGPDRTPCLSDKPKLPFLEAFILETFRHSSFLPFTIPHCTSKDTSLNGYFIPKDTCVFINQWQINHDAELWKDPSSFNPDRFLNADGTEVNKLEGEKMMVFGMGKRRCIGEVIARSEVFLFLAILVQNLRFHSMPGEPLDMTPEYGLTMKHKRCQLRAAMRARNEE

cyp1a1

Cytochrome P450 1A1

520 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

58.744 kDa

MVLMILPFIGSVSVSESLVALTTVCLVYLILKFFRTEIPEGLHRLPGPKPLPLIGNVLEVGNKPYLSLTAMSKRYGDVFRFRLGMRPSGCLSGSETVRKALIKQGDEFAGRPDLYSFRFINDGKSLAFSTDKAGVWRALRKLAYSALRSFSSLEESTPRDSCVLEEHSAKEGEYLYSNMLNAVMKVTGSFDPFRHIVVSVANVICGMCFGRRYGHNDQELLSLVNLSDPFGQVVGSGNPADFIPVLQFLPSTTMKNFMDINARFNKFVQKIVSEHYTTYDKDNIRDITDSLIDHCEDRKLDENANVQMSDEKIVGIVNDLFGAGFDTISTALSWSVMYLVAYPEIEERLYQELKENVGLDRTPLLCDRPNLPFLEAFILEIFRHSSFLPFTIPHCTSKDTSLNGYFIPKDTCVFINQWQINHDPELWKDPSSFNPDRFLSADGTELNKLEGEKVMVFGLGKRRCIGEVIARNGVFLFLAIIVQKLHFKTLPGEPLDMTPEYGLTMKHKRCHLRATMRASE

CYP1A1

Cytochrome P450 1A1

519 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

59.23 kDa

MWIMFSVFGLPIPISATELLLASAVFCLVFWVVRTWRPRVPQGLKSPPEPWGWPCLGHVLTLGKNPHVVLSQLSQRYGDVLQIRIGCTPVLVLSGLDTIRQALVRQGDDFKGRPDLYSFTLVSDGQSMTFNPDSGPVWAARRRLAQNALKSFSTASDPASLSSCYLEEHVSKEAEYLLGKFQELMSGPGRFDPYRYVVVSVANVICAICFGRRYDHDDQEFLSLINLSNEFGEITASGNPADFIPVLRYLPNTALDLFKDLNRRFYVFVQKIVKEHYKTFEKGHIRDITDSLIEHCQDKRLDENANIQLSDEKIINVVMDLFGAGFDTVTTAISWSLLYLVTSPRVQKKIQEELDTVIGRARWPQLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTTRDTNLNGFYIPKGXCVFVNQWQINHDQKLWEDPSEFRPERFLTTDGTVNKVLSEKVIIFGLGKRQCIGEIIARLEVFLFLAILLHQVEFHVTPGVKVDMTPLYGLTMKHARCEHFQVRIRS

CYP1A1

Cytochrome P450 1A1

518 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

58.278 kDa

MVSDFGLPTFISATELLLASAVFCLVFWVAGASKPRVPKGLKRLPGPWGWPLLGHVLTLGKNPHVALARLSRRYGDVFQIRLGSTPVVVLSGLDTIKQALVRQGDDFKGRPDLYSFSFVTKGQSMIFGSDSGPVWAARRRLAQNALNSFSVASDPASSSSCYLEEHVSQEAENLISKFQELMAAVGHFDPYRYVVMSVANVICAMCFGRRYDHDDQELLSLVNLNDEFGKVAASGSPADFFLILRYLPNPALDTFKDLNERFYSFTQERVKEHCRSFEKGHIRDITDSLIKHYRVDRLDENANVQVSDEKTVGIVLDLFGAGFDTVTTAISWSLMYLVTKPRIQRKIQEELDAVVGRARRPRFSDRPQLPYLEAVIMETFRHTSFLPFTIPHSTTRDTSLGGFYIPKGRCVFVNQWQNNHDPELWGDPEAFRPERFLTPSGAVDKALTEKVLLFGLGKRKCIGETIGRLEVFLFLATLLQQVEFSVSPGTTVDMTPIYGLTMKHARCEHFQAKLRFEA

CYP1A1

Cytochrome P450 1A1

517 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

58.707 kDa

MMLSVFGLSVPISATELLLASFVFCLVFWVVRAWQPRVPKGLKSPPGPWGWPLLGHVLTLGKNPHLVLARLSQHYGDVLQIRIGSTPVLVLSGLDTIRQALVRQGDDFKGRPNLYSFTLISEGQSMSFSPDSGPVWAARRRLAQNALKSFSIASDPASSSSCYLEDHVSKEAEYLIGKFQELMAKVGHFDPYRYVVVSVANVICAMCFGRRYDHDDQELLSIVNLSNEFGDGTASGNPVDFFPILRYLPNPALDFFKDVNEKFSIFIHKMVKEHYKTFEKGHIRDITDSLIEHCQDKRLDENANIQLSDEKIVNVVSDLFGAGFDTVTTAISWCLMYLVTSPNVQEKIQKELDTVIGRERQPRLSDRLQLPYMEAFILEMFRHTSFVPFTIPHSTTKDTSLSGFYIPKERCVFVNQWQINHDQKLWGDPSEFRPERFLTPDGTINKALSEKVILFGLGKRKCIGETIARLEVFLFLAILLQQVEFSVPQGTKVDMTPIYGLTMKHARCEHFQVRMRT

CYP1A1

Cytochrome P450 1A1

516 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

58.275 kDa

MFSVFGLSIPISATELLLASATFCLVFWVVRAWQPRVPKGLKSPPGPWSWPLIGHVLTLGKSPHLALSRLSQRYGDVLQIRIGCTPVLVLSGLDTIRQALVRQGDDFKGRPDLYSFTLVADGQSMTFNPDSGPVWAARRRLAQNALKSFSIASDPASSSSCYLEEHVSKESEYLIGKFQELMAGSGRFDPYRYVVVSVANVICAMCFGRRYDHESQVLLSVVGLSNEFGAVAASGNPADFIPILRYLPNTALDDFKDLNRRFYIFMQKMLKEHYKTFEKGRIRDITDSLIEHCQGKRLDENANIQLSDEKIVNVVMDLFGAGFDTVTTAISWSLMYLVTSPSVQKKIQEELDTVIGSARQPRLSDRPRLPYLEAFILETFRHSSFLPFTIPHSTTRDTSLNGFYIPKGRCVFVNQWQINHDQKLWDDPSAFWPERFLTADGTINKALSEKVILFGLGKRKCIGETIARWEVFLFLAILLQQVEFRVTPGVKVDMTPVYGLTMKHAHCEHFQAHMRS

CYP1A1

Cytochrome P450 1A1

516 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

58.571 kDa

MSTSAMELLLTATIFCLVLWVVRIFRPQVPKGLKSPPGPWGWPLIGHMLTLGKNPHLALTRLSARYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYSFTFISDGQSMTFNPDSGPVWAARRRLAQSALKSFSVASDPASVSSCYLEEHVKKEAEYLIKKFQELMAGPGHFDPYRYVVVSVANVISAICFGQRYSHDDQQLLELIDLNNEFGEVTGSGNPSDFIPILRYLPSATMDTFKDLNRRFSVFIQKMIKEHYKTFEKGHIRDITDSLIEHCQDRKLDKNANIQISDQKIIGIVLDLFGAGFDTITTAISWSLLYLVMNPRIQKKIQEELDTVIGRERQPQLADRPKLPYMEAFISEVFRYSSFMPFTIPHSTTKDTSLNGFYIPKGCCIFVNQWQINHDQKLWGDPSVFRPERFLSPDGTVDKALSEKVTIFGLGKRRCLGEVIGRWEVFLFLAILLQQLEFSTSPGVKIDMTPIYGLTMKYSRCEHFQAQTRPFVLKCPEA

cyp1a1

Cytochrome P450 1A1

515 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

57.826 kDa

MALMILPLIGSVSVSETLVAMITVCMIYMLMKFLHPDVPEAPPAPGPQALPIIGNVWSWENGLPEPHGHGQRYGDILQIQIGMRSVVVLSGHETVRQALIKQGHDLRPPDLYSFQFINDGKSLAFSTDQAGVWSPPKAGHECPALLFHARGHHAAVLLHVGGACLQGGRLPRQAAVQRHGTDASFDPFRHIVVSVANVICGMCFGRRYGHEDQELLSLVNLTDEFGKVVGSGNLADFIPLLRFLPNATMKRFMAINERFMTFVQKIVTEHYNTYDKDNIRDITDSLIDHCEDRKLDENSNIQMSDEKIVGIVNDLFGAGFDTVSTALSWSVMYLVAHPEIQERLHQEIKDKVGLSRSPVLTDRHNLPILEAFIFEIFRHSSFLPFTIPHCATKDTSLDGYFIPKDTCVFINQWQINHDPELWKEPSTFNPDRFLSADASELNKLAGEKVMLFGMGKRRCIGEMVARNEVFLFLAILVQRLTFHAVPGEPLDMTPEYGLTMKHKRCHLRATVRTTE

cyp1a1

Cytochrome P450 1A1

515 amino acids

Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Belongs to the cytochrome P450 family.

58.541 kDa

MVLMILPFIGSVSVSESLVAMITMCLAYLILKFFRTEIPEGLRELPGPKPLPIIGNVLEVGRNPYLSLTAMTAPRTDVFQIQIGMRPVVVLSGNETVRQALIKQGQEFAGRPDLYSFKFINDGKSLAFSTDGPAVWRARRKLAYSALRSFATKEGTTPEYSVRLFEHVSKERYAAISMFMKLMADFDPVRHIVVSVANVICGMCFGRRYDHNNRSWLNLVNPRRDVRKVVASGNPADFIPILQYLPSTTMKKFLNINARFNEFVQKIVSEHYTTFNKDNIRDITDSLIDHCEDEPMDPMPDADDKIVGIVNDLFGAGFDTISTALSWSVMYLVAYPEIQERLYQEMETVMGPDRMPCLSDRTQLTLPEAFILEIFRHSSFLPFTIPHCTTKDTSLNGYFIPKAPCIYIKQWPVIHDDDDVLDPSSFNPDRFLKADGTEVNKLNGEKMMVFGMGKRRCIGEVIARNEVYLFLAILLVQLQFHAMPGEPLDMTPEYGLTMKHKRCHLRAAMRRGTEE

CYP1A1

Cytochrome P450 1A1

512 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997). Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195).

Belongs to the cytochrome P450 family.

58.165 kDa

MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPHLALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQSMSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAGPGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPILRYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANVQLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLSDRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKLWVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEFSVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS

CYP1A1

Cytochrome P450 1A1

512 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

58.155 kDa

MLFRISMSATEFLLASLIFCLVFWVIRASRPRVPKGLKNPPGPWGWPLIGHILTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSGLDTIRQALVQQGDDFKGRPNLYSFTLISNGQSMSFGPDSGPVWAARRRLAQNGLKSFSIASDPASSSSCYLEEHVSKEAEVLISKLQEQMAGPGHFNPYRYVVISVANVICAICFGQRYDHNHQELLSLVNLSNNFGEVVGSGNPADFIPILRYLPNRSLNGFKDLNEKFHSFMQKMIKEHYKTFEKGYIRDITDSLIEHCQEKQLDENANIQLSDEKIVNVVLDLFGAGFDTVTTAISWSLMYLVTNPRVQRKIQEELDTVIGRSRRPRLSDRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKLWVNPSEFLPERFITPDGAIDKVLSEKVILFGLGKRKCIGETIARWEVFLFLAILLQRVEFSVPPGVKVDMTPIYGLTMKHACCEHFQMQLRS

CYP1A1

Cytochrome P450 1A1

512 amino acids

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent).

Belongs to the cytochrome P450 family.

58.129 kDa

MLFRISMSATEFLLASLIFCLVFWVIRASRPRVPKGLKNPPGPWGWPLIGHILTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSGLDTIRQALVQQGDDFKGRPNLYSFTLISNGQSMSFGPDSGPVWAARRRLAQNGLKSFSIASDPASSSSCYLEEHVSKEAEVLISKLQEQMAGPGHFNPYRYVVISVANVICAICFGQRYDHNHQELLSLVNLSNNFGEVVGSGNPADFIPILRYLPNRSLNGFKDLNEKFHSFMQKMIKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANIQLSDEKIVNVVLDLFGAGFDTVTTAISWSLMYLVTNPRVQRKIQEELDTVIGRSRRPRLSDRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKLWVNPSEFLPERFITPDGAIDKVLSEKVILFGLGKRKCIGETIARWEVFLFLAILLQRVEFSVPPGVKVDMTPIYGLTMKHACCEHFQMQLRS