. Author manuscript; available in PMC: 2018 Aug 30.

Published in final edited form as: Nat Prod Rep. 2017 Aug 30;34(9):1141–1172. doi: 10.1039/c7np00034k

Table 1.

Experimentally characterized P450s of streptomycete origin

P450^a	CYP name^b	Biosynthetic pathway	Function(s)	In vitro^c/in vivo/structure	PDB ID(s)	Ref.
AcmG8	–	Actinomycin G	Hydroxylation (PCP-tethered)^d	–/Y/–		¹⁷²
AknT	–	Aclacinomycin A	Glycosyltransferase (GTase) activator	Y/–/–		^202,203
AmphL	161A3	Amphotericin B	Hydroxylation	–/Y/–		²⁰⁴
AmphN	105H4	Amphotericin B	Hydroxylation/oxidation to acid	–/Y/–		^178,179
AryC	–	Arylomycin	Biaryl ring coupling (C–C)	–/Y/–		²⁰⁵
AurH	151A^e	Aureothin	Hydroxylation/ether formation	Y/Y/Y	3P3L, 3P3O, 3P3X, 3P3Z	^115–118
AveE	171A1	Avermectin	Ether formation	–/Y/–		¹¹⁹
AziB1	–	Azinomycin B	Hydroxylation	Y/–/–		⁷⁴
BecO	1045A3	BE-14106	Hydroxylation	–/Y/–		²⁰⁶
BorI	–	Borrelidin	Hydroxylation/oxidation to aldehyde/oxidation to nitrile	Y/Y/–		⁹⁰
BoxA	105A^e	Xenobiotics	Hydroxylation	Y/–/–		^131,207
CanC^f	105H5	Candicidin	Hydroxylation	–/Y/–		^208–211
ChoP	105C1	Unknown	Unknown	Y/–/–		²¹²
ChryOIII	–	Chrysomycin	Desaturation	–/Y/–		²¹³
CldC	–	Cyslabdan A	Hydroxylation/epoxidation	–/Y/–		²¹⁴
ComI	165E1	Complestatin	Biaryl ring coupling (C–C)	–/Y/–		¹⁶⁵
ComJ	165B5	Complestatin	Biaryl ring coupling (C–O)	–/Y/–		¹⁶⁵
CotB3	–	Cyclooctatin	Hydroxylation	–/Y/–		²¹⁵
CotB4	–	Cyclooctatin	Hydroxylation	–/Y/–		²¹⁵
CSP4	107P3	Xenobiotics	Dealkylation	Y/–/–		²¹⁶
CYP102B1	102B1	Fatty acids	Hydroxylation/epoxidation	Y/Y/–		^31,217
CYP102D1	102D1	Fatty acids	Hydroxylation	Y/–/–		²⁹
CYP105D4	105D4	Xenobiotics	Hydroxylation	Y/–/–		¹³¹
CYP105D5	105D5	Xenobiotics	Hydroxylation	Y/Y/–		^{27,31,32,34,131}
CYP105D6	105D6	Filipin	Hydroxylation	Y/–/Y	3ABB	²¹⁸
CYP105D7	105D7	Pentalenolactone/xenobiotics	Hydroxylation	Y/Y/Y	4UBS	^48,219–224
CYP105F2	105F2	Oleandomycin	Hydroxylation	Y/–/–		²²⁵
CYP105N1	105N1	Coelibactin	Unknown	Y/–/Y	3TYW, 4FXB	^31,226,227
CYP105P1	105P1	Filipin	Hydroxylation	Y/–/Y	3ABA, 3E5J, 3E5K, 3E5L	^218,228
CYP105P2	105P2	Flavones	Hydroxylation	Y/–/Y	5IT1	^40,190,229
CYP107AJ1	107AJ1	Xenobiotics	Dealkylation	Y/–/–		¹⁵⁴
CYP107L2	107L2	Fatty acids	Unknown	Y/–/Y	5CJE, 5CWE	²³⁰
CYP107P1	107P1	Unknown	Unknown	Y/–/–		³¹
CYP107P2	107P2	Xenobiotics	Hydroxylation	Y/–/–		¹⁷¹
CYP107T1	107T1	Unknown	Unknown	Y/–/–		³¹
CYP107U1	107U1	Xenobiotics	Oxidation to ketone	Y/Y/–		^31,231
CYP107W1	107W1	Oligomycin A	Hydroxylation	Y/–/Y	4WPZ, 4WQ0	^232,233
CYP107Y1	107Y1	Xenobiotics	Hydroxylation	Y/–/–		¹⁷¹
CYP107Z13	107Z13	Avermectin	Oxidation to ketone	Y/–/–		^133,234
CYP125A2	125A2	Xenobiotics	Hydroxylation	Y/–/–		¹⁷¹
CYP147F1	147F1	Fatty acids	Hydroxylation	Y/–/–		^235–237
CYP154A1	154A1	Dipentaenone/xenobiotics	Cycloaddition/dealkylation	Y/Y/Y	1ODO	^{30–32,188,207,238}
CYP154C1	154C1	Pikromycin/methymycin/neomethymycin	Hydroxylation	Y/–/Y	1GWI	^31,32,239
CYP154C3	154C3	Xenobiotics	Hydroxylation	Y/–/–		⁴⁵
CYP155A1	155A1	Unknown	Unknown	Y/–/–		³¹
CYP156A1	156A1	Unknown	Unknown	Y/–/–		³¹
CYP156B1	156B1	Unknown	Unknown	Y/–/–		³¹
CYP157A1	157A1	Unknown	Unknown	Y/–/–		³¹
CYP157B1	157B1	Unknown	Unknown	Y/–/–		³¹
CYP157C1	157C1	Unknown	Unknown	Y/–/–		^31,151
CYP157C4	157C4	Xenobiotics	Dealkylation	Y/–/–		²⁴⁰
CYP158A1	158A1	Flaviolin	Biaryl ring coupling (C–C)	Y/–/Y	2DKK, 2NZ5, 2NZA	^31,32,42
CYP158A2	158A2	Flaviolin	Biaryl ring coupling (C–C)	Y/–/Y	1SE6, 1S1F, 1T93, 2D0E, 2D09, 3TZO, 5DE9	^{31,32,42,102,111,112}
CYP159A1	159A1	Unknown	Unknown	Y/–/–		³¹
CYP170A1^f	170A1	Albaflavenone	Hydroxylation/oxidation to ketone/diphosphate ionization	Y/Y/Y	3DBG, 3EL3	^{145–147,241}
CYP170A2	170A2	Albaflavenone	Hydroxylation/oxidation to ketone	–/Y/–		²⁴²
CYP170B1	170B1	Albaflavenone	Hydroxylation/oxidation to ketone	Y/–/–		¹⁴⁷
CYP450Y110	–	Xenobiotics	Hydroxylation	Y/–/–		²⁴³
CYP51^f	170A1	Xenobiotics	Dealkylation	Y/Y/–		²⁴⁴
CYPSvh01^f	105C1	Xenobiotics	Hydroxylation	Y/–/–		²⁴⁵
CYPSvu022	154H^e	Xenobiotics	Hydroxylation	Y/–/–		²⁴⁵
DesVIII	–	Pikromycin	GTase activator	Y/Y/–		^{141–143,246,247}
DnrQ	131A1	Duanorubicin	GTase activator	–/Y/–		^143,246,248
DoxA27952	129A2	Doxorubicin	Hydroxylation/oxidation to ketone	Y/–/–		³⁵
DoxA29050	129A2	Doxorubicin	Hydroxylation/oxidation to ketone	Y/Y/–		^86,249,250
DoxAC5	129A1	Doxorubicin	Hydroxylation/oxidation to ketone	Y/–/–		^251,252
Ema1	107Z12	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema2^f	107Z10	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema3	107Z2v2	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema4^f	107Z5v3	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema5	107Z6	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema6	107Z5v2	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema7	107Z3	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema8	107Z2v1	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema9	107Z11	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema10^f	107Z5v3	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema11	107Z1	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema12	107Z9	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema13	107Z8	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema14^f	107Z10	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema15	107Z5v1	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema16	107Z4	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
Ema17	107Z7	Xenobiotics	Hydroxylation/oxidation to ketone	Y/–/–		¹³²
EncR	107R1	Enterocin	Hydroxylation	Y/Y/–		^253,254
FcpC^f	105^e	Xenobiotics	Hydroxylation	Y/–/–		³⁸
FilC	–	Filipin	Hydroxylation	–/Y/–		²⁵⁵
FilD	–	Filipin	Hydroxylation	–/Y/–		²⁵⁵
FosK	–	Fostriecin	Hydroxylation	–/Y/–		²⁵⁶
FscP^f	105H5	Candicidin	Hydroxylation/oxidation to acid	–/Y/–		^209–211
GalD	–	Galbonolide	Hydroxylation or epoxidation	–/Y/–		²⁵⁷
GbnD	–	Galbonolide	Hydroxylation or epoxidation	Y/–/–		²⁵⁸
GdmP	105U1	Geldanamycin	Desaturation	–/Y/–		^92–94,259
GerPI	–	Dihydrochalcomycin	Epoxidation	–/Y/–		²⁶⁰
GerPII	–	Dihydrochalcomycin	Hydroxylation	–/Y/–		²⁶⁰
GfsF	105^e	FD-891	Hydroxylation/epoxidation	Y/Y/–		^261,262
GilOIII	–	Gilvocarcin	Desaturation	–/Y/–		^213,263
GrhO3	105D9	Griseorhodin	Epoxidation	–/Y/–		²⁶⁴
HerG	–	Herboxidiene	Hydroxylation	Y/–/–		^265,266
HerO	–	Heronamide	Hydroxylation	Y/Y/–		⁴⁶
HlsH	107^e	Halstoctacoanolide	Hydroxylation/oxidation to ketone	–/Y/–		¹⁶⁴
HlsI	107^e	Halstoctacoanolide	Hydroxylation	–/Y/–		¹⁶⁴
HmtN	–	Himastatin	Hydroxylation	Y/Y/Y	4E2P	^95,126
HmtS	–	Himastatin	Biaryl ring coupling (C–C)	–/Y/–		⁹⁵
HmtT	–	Himastatin	C–N bond formation	Y/Y/Y	4GGV	^95,126
JulI	–	Julichrome	Biaryl ring coupling (C–C)	Y/Y/–		⁹⁶
LkmF	107A2	Lankomycin	Hydroxylation	–/Y/–		^267,268
LkmK	107AP1	Lankomycin	Hydroxylation	–/Y/–		^267,268
LnmA	107AC1	Leinamycin	Hydroxylation	Y/Y/Y	4Z5P	²⁶⁹
LnmZ	107AG1	Leinamycin	Hydroxylation	Y/Y/Y	4Z5Q	²⁶⁹
LtmK	–	Lactimidomycin	Desaturation	–/Y/–		⁹¹
MeiE	171A2	Meilingmycin	Ether formation	–/Y/–		^173,174
MfnN	–	Marfomycin	Hydroxylation	–/Y/–		²⁷⁰
MgsK	–	iso-Migrastatin	Hydroxylation	–/Y/–		²⁷¹
MonD	124B1	Monensin	Hydroxylation (ACP-tethered)^d	–/Y/–		⁷⁹
NcsB3	154J1	Neocarzinostatin	Hydroxylation	Y /–/–		^272,273
NikF	105K1	Nikkomycin	Hydroxylation	–/Y/–		^167,274
NikQ	162A1	Nikkomycin	Hydroxylation (PCP-tethered)	Y/Y/–		^167,168
NovI	163A1	Novobiocin	Hydroxylation (PCP-tethered)^d	Y/–/–		¹⁶⁶
NysL	161A1	Nystatin	Hydroxylation	Y/Y/–		^180,181,275
NysN	105H1	Nystatin	Hydroxylation/oxidation to acid	–/Y/–		^180,181
NzsA	–	Neocarazostatin	Hydroxylation	Y/Y/–		²⁷⁶
OleP	107D1	Oleandomycin/xenobiotics	Epoxidation/hydroxylation	Y/–/Y	4XE3	^{72,73,131,277,278}
OleP1	235A1	Oleandomycin	GTase activator	–/Y/–		^248,279
ORF-A	107C1	Carbomycin	Epoxidation	Y/–/–		²⁸⁰
P450_CLA	105M1	Clavulanic acid	Unknown	Y/–/–		²⁸¹
P450_mel	107F1	Melanin	Biaryl ring coupling (C–C)	Y/Y/–		¹⁰³
P450_sca-2	105A3	Xenobiotics	Hydroxylation	Y/–/–		^43,282–285
P450_sky	163B3	Skyllamycin	Hydroxylation (PCP-tethered)^d	Y/Y/Y	4L0E, 4L0F, 4PWV, 4PXH	^76–78
P450_SU-1	105A1	Xenobiotics	Hydroxylation/epoxidation/dealkylation	Y/Y/Y	2ZBX, 2ZBY, 2ZBZ, 3CV8, 3CV9	^{36,131,134–137,139,286–294}
P450_SU-2	105B1	Xenobiotics	Hydroxylation/dealkylation	Y/Y/–		^{36,138,286–289,295}
P450_terf	107L^e	Xenobiotics	Hydroxylation	Y/Y/–		^296,297
PenM	161C3	Pentalenolactone	Oxidative rearrangement	Y/Y/–		¹¹³
PikC	107L1	Pikromycin/methymycin/neomethymycin/xenobiotics	Hydroxylation/oxidation to ketone	Y/Y/Y	2BVJ, 2CA0, 2CD8, 2C6H, 2C7X, 2VZM, 2VZ7, 2WH2, 2WI9, 3ZK5, 3ZPI, 4B7D, 4B7S, 4BF4, 4UMZ	^{47,65–69,298–306}
PimD	161A2	Pimaricin	Epoxidation	Y/Y/Y	2XBK, 2X9P	^50,70,71
PlaO2	–	Phenalinolactone	Nonfunctional	–/Y/–		⁸³
PlaO3	–	Phenalinolactone	Hydroxylation	–/Y/–		⁸²
PlaO4	–	Phenalinolactone	Hydroxylation	–/Y/–		⁸³
PlaO5	–	Phenalinolactone	Hydroxylation	Y/Y/–		⁸³
PldB	107^e	Pladienolide	Hydroxylation	Y/Y/–		³⁰⁷
PlmS2	107L8	Phoslactomycin	Hydroxylation	Y/Y/–		³⁰⁸
PntM	161C2	Pentalenolactone	Oxidative rearrangement	Y/Y/Y	5L1O, 5L1P, 5L1Q, 5L1R, 5L1S, 5L1T, 5L1U, 5L1V, 5L1W	^113,114
ProP450	–	Xenobiotics	Hydroxylation	Y/–/–		^49,309
PsmA	105^e	Pladienolide	Hydroxylation	Y/Y/–		^310,311
PtlI	183A1	Pentalenolactone	Hydroxylation/oxidation to aldehyde	Y/–/–		³¹²
PtmO5	–	Platensimycin	Ether formation	–/Y/–		¹²⁰
Qui15	–	Echinomycin	Hydroxylation (PCP-tethered)^d	–/Y/–		¹⁷⁰
RapJ	122A2	Rapamycin	Hydroxylation	–/Y/–		^313,314
RapN	107G1	Rapamycin	Hydroxylation	–/Y/–		^313,314
RavOIII	–	Ravidomycin	Desaturation	–/Y/–		²¹³
RevI	–	Reveromycin	Hydroxylation	Y/Y/Y	3WVS	³¹⁵
RmnC	–	Raimonol	Hydroxylation	–/Y/–		²¹⁴
SamR0478	–	Stambomycin	Hydroxylation	–/Y/–		³¹⁶
SamR0479	–	Stambomycin	Hydroxylation	–/Y/–		³¹⁶
SanH	105K2	Nikkomycin	Hydroxylation	–/Y/–		^317,318
SanQ	162A2	Nikkomycin	Hydroxylation (PCP-tethered)	–/Y/–		¹⁶⁹
Sclav_p0067	–	(–)-Drimenol	Unknown^g	–/Y/–		³¹⁹
ScnD	–	Pimaricin	Epoxidation	Y/Y/–		^182,183
ScnG	–	Pimaricin	Hydroxylation/oxidation acid	–/Y/–		^182,183
SgcD3	211A1	C-1027	Hydroxylation	–/Y/–		³²⁰
SgvP	107^e	Griseoviridin	C–S bond formation	Y/Y/Y	4MM0	^129,130,189
SKCTCFkbD^f	–	FK506/FK520	Hydroxylation/oxidation to ketone	Y/Y/–		³²¹
Sl5NT	–	Unknown	Nitration	Y/–/–		¹²⁵
SlgO2	–	Streptolydigin	Hydroxylation/oxidation to ketone	–/Y/–		^322,323
SlStaN	244A1	Staurosporine	C–N bond formation	Y/–/–		¹²⁷
SMAFkbD	–	FK506/FK520	Hydroxylation/oxidation to ketone	–/Y/–		³²⁴
SMg15NT	–	Unknown	Nitration	Y/–/–		¹²⁵
SoCYP158A2	158A2	Phenol/indole	Hydroxylation	Y/–/–		³²⁵
SoyC	105D1	Xenobiotics	Hydroxylation/epoxidation/dealkylation/desaturation	Y/–/–		^37,326–333
Srm13	–	Spiramycin	Hydroxylation/oxidation to aldehyde	–/Y/–		^334,335
StaF	165A4	A47934	Biaryl ring coupling (C–O) (PCP-tethered)	Y/Y/Y	5EX8, 5EX9	^99,106,107
StaG	165D1	A47934	Biaryl ring coupling (C–O)	–/Y/–		⁹⁹
StaH	165B4	A47934	Biaryl ring coupling (C–O) (PCP-tethered)	Y/Y/Y	5EX6	^99,106,107
StaJ	165C5	A47934	Biaryl ring coupling (C–C)	–/Y/–		⁹⁹
StaP	245A1	Staurosporine	Biaryl ring coupling (C–C)/oxidative decarboxylation	Y/–/Y	2Z3T, 2Z3U, 3A1L	^{100,101,108–110,336}
StFkbD^f	–	FK506/FK520	Hydroxylation/oxidation to ketone	Y/Y/–		^337,338
StStaN	244A1	Staurosporine	C–N bond formation	–/Y/–		^100,128
StuD1	–	Thiolactomycin/thiotetronate	Epoxidation (ACP-tethered)^d	–/Y/–		⁸⁰
StuD2	–	Thiolactomycin/thiotetronate	Hydroxylation/oxidation to acid	–/Y/–		⁸⁰
Sv5NT	–	Unknown	Nitration	Y/–/–		¹²⁵
TamI^f	–	Tirandamycin	Hydroxylation/oxidation to ketone/epoxidation	Y/Y/–		^84,85
TetrK^f	–	Tetramycin	Hydroxylation	Y/Y/–		³³⁹
ThnC	–	Thienodolin	C–S bond formation	Y/Y/–		³⁴⁰
TmcR	–	Tautomycetin	Hydroxylation/oxidation to ketone	–/Y/–		^341,342
TrdI^f	–	Tirandamycin	Hydroxylation/oxidation to ketone/epoxidation	–/Y/–		³⁴³
TtmD^f	–	Tetramycin	Hydroyxlation	Y/Y/–^g		^339,344
TtnI	–	Tautomycetin	Hydroxylation/oxidation to ketone	–/Y/–		³⁴⁵
TxtC	246A1	Thaxtomin	Hydroxylation	Y/Y/–		³⁴⁶
TxtE	–	Thaxtomin	Nitration	Y/Y/Y	4L36, 4TPO, 4TPN, 5D3U, 5D40	^{122–125,347}
TylHI	105L1	Tylosin	Hydroxylation	–/Y/–		^348–350
TylMIII	–	Tylosin	GTase activator	–/Y/–		^143,246,351
Unk. P450	–	Xenobiotics	Dealkylation	–/Y/–		³⁵²
XiaM	–	Xiamycin	Hydroxylation/oxidation to acid	Y/Y/–		⁸⁹

Commonly used P450 names. Duplicated names are differentiated by adding the first letter of the genus and species, e.g., SlStaN = Streptomyces longisporoflavus StaN.

CYP names identified from reference or the Cytochrome P450 Homepage (drnelson.uthsc.edu).¹⁶³

In this study, heterologous P450 biotransformations are considered in vitro experiments.

P450 acts on a PCP- or ACP-tethered substrate.

Only CYP family or subfamily was given.

CanC = FscP; CYP170A1 = CYP51; CYPSvh01 = FcpC; Ema2 = Ema14; Ema4 = Ema10; StFkbD = SKCTCFkbD; TamI = TrdI; TetrK = TtmD.

The function of Sclav_p0067 is still unknown, but in vivo results support alteration of FPP cyclization by the sesquiterpene synthase Sclav_p0068.³¹⁹