Information on EC 1.14.14.1 - unspecific monooxygenase and Organism(s) Priestia megaterium and UniProt Accession P14779

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BM3

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CYP102A1

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693835, 695046, 704714, 742263, 745559

cytochrome P-450 BM3

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cytochrome P450 BM3

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monooxygenase P450 BM-3

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P450 BM3

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P450-BM3

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3AH15

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6 beta-hydroxylase

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6-beta-testosterone hydroxylase

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Aldehyde oxygenase

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Arachidonic acid epoxygenase

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aromatase

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aryl hydrocarbon hydroxylase

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aryl-4-monooxygenase

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Brain aromatase

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Clone PF26

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Clone PF3/46

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Coumarin 7-hydroxylase

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CYP102

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CYP102 monooxygenase

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CYP102A1

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CYP1A1

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CYP1A2

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CYP1A3

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CYP2A3

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CYP4502F4

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CYP6B1V1/CYP6B1V2/ CYP6B1V3

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CYP6B3V1/CYP6B3V2

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CYP6B4V1/CYP6B4V2

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CYP6B5V1

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CYPIA1

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CYPIA2

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CYPIA4

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CYPIA5

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CYPIB1

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CYPIIA1

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CYPIIA10

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CYPIIA11

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CYPIIA12

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CYPIIA13

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CYPIIA2

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CYPIIA3

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CYPIIA4

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CYPIIA5

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CYPIIA6

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CYPIIA7

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CYPIIA8

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CYPIIA9

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CYPIIB1

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CYPIIB10

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CYPIIB11

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CYPIIB12

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CYPIIB19

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CYPIIB2

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CYPIIB20

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CYPIIB3

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CYPIIB4

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CYPIIB5

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CYPIIB6

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CYPIIB9

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CYPIIC1

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CYPIIC10

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CYPIIC11

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CYPIIC12

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CYPIIC13

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CYPIIC14

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CYPIIC15

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CYPIIC16

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CYPIIC17

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CYPIIC18

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CYPIIC19

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CYPIIC2

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CYPIIC20

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CYPIIC21

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CYPIIC22

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CYPIIC23

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CYPIIC24

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CYPIIC25

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CYPIIC26

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CYPIIC27

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CYPIIC28

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CYPIIC29

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CYPIIC3

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CYPIIC30

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CYPIIC31

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CYPIIC37

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CYPIIC38

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CYPIIC39

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CYPIIC4

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CYPIIC40

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CYPIIC41

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CYPIIC42

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CYPIIC5

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CYPIIC6

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CYPIIC7

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CYPIIC8

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CYPIIC9

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CYPIID1

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CYPIID10

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CYPIID11

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CYPIID14

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CYPIID15

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CYPIID16

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CYPIID17

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CYPIID18

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CYPIID19

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CYPIID2

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CYPIID3

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CYPIID4

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CYPIID5

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CYPIID6

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CYPIID9

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CYPIIE1

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CYPIIF1

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CYPIIF3

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CYPIIF4

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CYPIIG1

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CYPIIH1

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CYPIIH2

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CYPIIIA1

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CYPIIIA10

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CYPIIIA11

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CYPIIIA12

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CYPIIIA13

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CYPIIIA14

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CYPIIIA15

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CYPIIIA16

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CYPIIIA17

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CYPIIIA18

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CYPIIIA19

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CYPIIIA2

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CYPIIIA21

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CYPIIIA24

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CYPIIIA25

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CYPIIIA27

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CYPIIIA28

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CYPIIIA29

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CYPIIIA3

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CYPIIIA30

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CYPIIIA31

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CYPIIIA5

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CYPIIIA6

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CYPIIIA7

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CYPIIIA8

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CYPIIIA9

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CYPIIJ1

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CYPIIJ2

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CYPIIJ3

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CYPIIJ5

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CYPIIJ6

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CYPIIK1

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CYPIIK3

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CYPIIK4

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CYPIIL1

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CYPIIM1

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CYPIVA4

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CYPIVA8

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CYPIVB1

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CYPIVC1

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CYPIVF1

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CYPIVF11

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CYPIVF12

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CYPIVF4

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CYPIVF5

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CYPIVF6

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CYPIVF8

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CYPVIA1

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CYPVIB1

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CYPVIB2

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CYPVIB4

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CYPVIB5

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CYPVIB6

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CYPVIB7

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CYPXIX

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CYPXIXA1

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CYPXIXA2

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CYPXIXA3

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cytochrome P-450 BM3

Cytochrome P450-D2

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DAH1

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DAH2

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Debrisoquine 4-hydroxylase

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Estrogen synthetase

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flavocytochrome P450BM-3

arachidonic acid metabolism

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390111

flavoprotein monooxygenase

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flavoprotein-linked monooxygenase

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Hepatic cytochrome P-450MC1

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HLp

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IIA3

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Isozyme 3A

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Laurate omega-1 hydroxylase

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Lauric acid omega-6-hydroxylase

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LMC1

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Mephenytoin 4-hydroxylase

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microsomal monooxygenase

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microsomal P-450

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OLF2

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Olfactive

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Ovarian aromatase

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oxygenase, flavoprotein-linked mono-

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P(3)450

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P-448

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P-450 PHPAH1

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P-450(M-1)

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P-450-MK2

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P-450AROM

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P-450IB

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P-450IIIAM1

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P-450MC

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P-450MP

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P-450UT

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P1-88

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P24

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P450 17-alpha

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P450 2D-29/2D-35

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P450 CM3A-10

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P450 DUT2

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P450 FA

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P450 FI

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P450 form 3B

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P450 form HP1

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P450 HSM1

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P450 HSM2

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P450 HSM3

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P450 HSM4

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P450 IIB1

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P450 IIC2

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P450 LM4

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P450 LM6

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P450 LMC2

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P450 MD

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P450 MP-12/MP-20

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P450 P49

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P450 PB1

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P450 PB4

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P450 PBC1

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P450 PBC2

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P450 PBC3

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P450 PBC4

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P450 PCHP3

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P450 PCHP7

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P450 TCDDAA

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P450 TCDDAHH

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P450 type B2

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P450 types B0 and B1

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P450(I)

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P450-11A

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P450-15-alpha

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P450-15-COH

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P450-16-alpha

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P450-254C

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P450-3C

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P450-6B/29C

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P450-A3

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P450-AFB

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P450-ALC

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P450-CMF1A

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P450-CMF1B

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P450-CMF2

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P450-CMF3

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P450-DB1

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P450-DB2

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P450-DB3

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P450-DB4

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P450-DB5

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P450-HFLA

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P450-HP

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P450-IIA10

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P450-IIA11

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P450-IIA3.1

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P450-IIA3.2

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P450-IIA4

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P450-KP1

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P450-LM2

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P450-MC1

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P450-MC4

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P450-MK1

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P450-MKJ1

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P450-MKMP13

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P450-MKNF2

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P450-NMB

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P450-OLF1

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P450-OLF3

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P450-P1

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P450-P2/P450-P3

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P450-P3

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P450-PB1 and P450-PB2

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P450-PCN1

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P450-PCN2

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P450-PCN3

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P450-PM4

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P450-PP1

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P450-PROS2

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P4501A1

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P450CB

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P450CMEF

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P450E

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P450EF

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P450F

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P450H

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P450I

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P450IIC5

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P450MT2

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P450RAP

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P450RLM6

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P52

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PB15

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PHP2

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PHP3

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Progesterone 21-hydroxylase

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Prostaglandin omega-hydroxylase

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PTF1

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PTF2

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S-mephenytoin 4-hydroxylase

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Steroid hormones 7-alpha-hydroxylase

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Testosterone 15-alpha-hydroxylase

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Testosterone 16-alpha hydroxylase

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Testosterone 6-beta-hydroxylase

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Testosterone 7-alpha-hydroxylase

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xenobiotic monooxygenase

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hydroxylation

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epoxidation

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Deamination

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redox reaction

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oxidation

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reduction

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sulfoxidation

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hydroxylation

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epoxidation

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N-oxidation

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O-dealkylation

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desulfation

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reduction of azo, nitro, N-oxide groups

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N-dealkylation

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S-dealkylation

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BRENDA

KEGG

Aminobenzoate degradation, Arachidonic acid metabolism, Biosynthesis of secondary metabolites, Caffeine metabolism, Drug metabolism - cytochrome P450, Fatty acid degradation, Linoleic acid metabolism, Metabolism of xenobiotics by cytochrome P450, Microbial metabolism in diverse environments, Retinol metabolism, Steroid hormone biosynthesis, Tryptophan metabolism

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-, -, -, -, -, -, -, -, -

substrate,NADPH-hemoprotein reductase:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)

A group of P-450 heme-thiolate proteins, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4, NADPH---hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.

62213-32-5

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(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2

myrtenol + [oxidized NADPH-hemoprotein reductase] + H2O

(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2

pinene oxide + [oxidized NADPH-hemoprotein reductase] + H2O

3 entries

(-)-alpha-pinene + [reduced NADPH-hemoprotein reductase] + O2

verbenol + [oxidized NADPH-hemoprotein reductase] + H2O

3 entries

(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2

myrtanal + [oxidized NADPH-hemoprotein reductase] + H2O

(-)-beta-pinene + [reduced NADPH-hemoprotein reductase] + O2

pino-carveol + [oxidized NADPH-hemoprotein reductase] + H2O

1-indanone + [reduced NADPH-hemoprotein reductase] + O2

(S)-3-hydroxy-1-indanone + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

1-tetralone + [reduced NADPH-hemoprotein reductase] + O2

(S)-4-hydroxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

3,7-dimethyl-1-octanol + [reduced NADPH-hemoprotein reductase] + O2

6-hydroxy-3,7-dimethyl-1-octanol + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

6-methoxy-1-tetralone + [reduced NADPH-hemoprotein reductase] + O2

(S)-4-hydroxy-6-methoxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

7-methoxy-1-tetralone + [reduced NADPH-hemoprotein reductase] + O2

(S)-4-hydroxy-7-methoxy-1-tetralone + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

farnesol + [reduced NADPH-hemoprotein reductase] + O2

?

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

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?

geraniol + [reduced NADPH-hemoprotein reductase] + O2

8-hydroxygeraniol + 10-hydroxygeraniol + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

indane + [reduced NADPH-hemoprotein reductase] + O2

(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

lauric acid + [reduced NADPH-hemoprotein reductase] + O2

?

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

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?

methyl 10,11-epoxyfarnesoate + [reduced NADPH-hemoprotein reductase] + O2

?

the major product of C(78-82,F87L,328-330) during 10,11-epoxymethylfarnesoate oxidation is determined to be the 12-hydroxy isomer

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?

methyl farnesoate + O2 + NADPH

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the major product of C(78-82,F87L,328-330) during methylfarnesoate oxidation is determined to be the 12-hydroxy isomer

-

?

p-xylene + O2 + [reduced NADPH-hemoprotein reductase]

2,5-dimethylphenol + H2O + [oxidized NADPH-hemoprotein reductase]

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745559

-

?

palmitic acid + [reduced NADPH-hemoprotein reductase] + O2

?

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

-

?

tetralin + [reduced NADPH-hemoprotein reductase] + O2

(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O

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-

?

beta-ionone + [reduced NADPH-hemoprotein reductase] + O2

4-hydroxy-beta-ionone + [oxidized NADPH-hemoprotein reductase] + H2O

-

-

?

cytochrome c + NADH + H+ + O2

?

-

-

r

cytochrome c + O2 + NADH

?

-

-

r

styrene + O2 + H2O2

(R)-styrene oxide + (S)-styrene oxide + H2O

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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)+

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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

-

?

additional information

?

-

5 entries

indane + [reduced NADPH-hemoprotein reductase] + O2

(S)-3-hydroxy-indane + [oxidized NADPH-hemoprotein reductase] + H2O

-

-

?

tetralin + [reduced NADPH-hemoprotein reductase] + O2

(S)-4-hydroxy-tetralin + [oxidized NADPH-hemoprotein reductase] + H2O

-

-

?

NADPH

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cytochrome c

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FAD

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bound, binding structure, overview

FMN

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bound, binding structure, overview

NAD(P)H

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additional information

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Fe2+

in a catalytic cytochrome P450 ferric heme center

672648

Fe2+

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a heme-containing P450 monooxygenase

H2O2

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at high concentrations

0.004 - 1.43

NADH

12 entries

0.002 - 0.13

NADPH

5 entries

additional information

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Km-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds

390110

-

0.016 - 156

NADH

8 entries

0.43 - 362.8

NADPH

12 entries

additional information

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additional information

3 entries

molecular dynamics simulations on two CYP102A1 mutants in complex with (-)-alpha-pinene to explore the molecular mechanism of substrate recognition and to predict regioselectivity.

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

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390111

crystallization of the wild-type and mutant CYP102A1 with and without bound substrates and one including theFMNbinding domain

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A328F

site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme

A328K

site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme

A328R

site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme

A328Y

site-directed mutagenesis, the mutant shows altered enantioselectivity compared to the wild-type enzyme

A74G/F87G/L188Q

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 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/L188Q

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

672648

R47S/Y51W/ I401M

use for electrochemical conversion of p-xylene to 2,5-dimethylphenol

745559

A74E/F87V/P386S

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site-directed mutagenesis, the mutant shows altered regioselectivity and activity, and cofactor specificity compared to the wild-type mutant

A74G/F87V/L188Q

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site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant

A74G/F87V/L188Q/R966D