DB code: M00154

CATH domain 1.10.630.10 : Cytochrome p450 Catalytic domain
3.40.50.360 : Rossmann fold
-.-.-.- :
-.-.-.- :
E.C. 1.14.14.1 1.6.2.4
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.360 : Rossmann fold S00522 S00343 M00006
1.10.630.10 : Cytochrome p450 S00033 S00031 S00030

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Includes Pfam
P14779 Bifunctional P-450/NADPH-P450 reductase
Cytochrome P450(BM-3)
Cytochrome P450BM-3
Cytochrome P450 102
EC 1.14.14.1
NADPH--cytochrome P450 reductase
EC 1.6.2.4
PF00667 (FAD_binding_1)
PF00258 (Flavodoxin_1)
PF00175 (NAD_binding_1)
PF00067 (p450)
[Graphical View]

KEGG enzyme name
unspecific monooxygenase
(EC 1.14.14.1 )
microsomal monooxygenase
(EC 1.14.14.1 )
xenobiotic monooxygenase
(EC 1.14.14.1 )
aryl-4-monooxygenase
(EC 1.14.14.1 )
aryl hydrocarbon hydroxylase
(EC 1.14.14.1 )
microsomal P-450
(EC 1.14.14.1 )
flavoprotein-linked monooxygenase
(EC 1.14.14.1 )
flavoprotein monooxygenase
(EC 1.14.14.1 )
NADPH---hemoprotein reductase
(EC 1.6.2.4 )
CPR
(EC 1.6.2.4 )
FAD-cytochrome c reductase
(EC 1.6.2.4 )
NADP---cytochrome c reductase
(EC 1.6.2.4 )
NADP---cytochrome reductase
(EC 1.6.2.4 )
NADPH-dependent cytochrome c reductase
(EC 1.6.2.4 )
NADPH:P-450 reductase
(EC 1.6.2.4 )
NADPH:ferrihemoprotein oxidoreductase
(EC 1.6.2.4 )
NADPH---cytochrome P-450 oxidoreductase
(EC 1.6.2.4 )
NADPH---cytochrome c oxidoreductase
(EC 1.6.2.4 )
NADPH---cytochrome c reductase
(EC 1.6.2.4 )
NADPH---cytochrome p-450 reductase
(EC 1.6.2.4 )
NADPH---ferricytochrome c oxidoreductase
(EC 1.6.2.4 )
NADPH---ferrihemoprotein reductase
(EC 1.6.2.4 )
TPNH2 cytochrome c reductase
(EC 1.6.2.4 )
TPNH-cytochrome c reductase
(EC 1.6.2.4 )
aldehyde reductase (NADPH-dependent)
(EC 1.6.2.4 )
cytochrome P-450 reductase
(EC 1.6.2.4 )
cytochrome c reductase (reduced nicotinamide adenine dinucleotidephosphate, NADPH, NADPH-dependent)
(EC 1.6.2.4 )
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome creductase
(EC 1.6.2.4 )
ferrihemoprotein P-450 reductase
(EC 1.6.2.4 )
reduced nicotinamide adenine dinucleotide phosphate-cytochrome creductase
(EC 1.6.2.4 )
reductase, cytochrome c (reduced nicotinamide adenine dinucleotidephosphate)
(EC 1.6.2.4 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P14779 CPXB_BACME RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O. NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein. Cytoplasm (By similarity). FAD. FMN. Heme group.

KEGG Pathways
Map code Pathways E.C.
MAP00982 Drug metabolism - cytochrome P450 1.14.14.1
MAP00983 Drug metabolism - other enzymes 1.14.14.1
MAP00071 Fatty acid metabolism 1.14.14.1
MAP00150 Androgen and estrogen metabolism 1.14.14.1
MAP00232 Caffeine metabolism 1.14.14.1
MAP00361 gamma-Hexachlorocyclohexane degradation 1.14.14.1
MAP00380 Tryptophan metabolism 1.14.14.1
MAP00590 Arachidonic acid metabolism 1.14.14.1
MAP00591 Linoleic acid metabolism 1.14.14.1
MAP00830 Retinol metabolism 1.14.14.1
MAP00980 Metabolism of xenobiotics by cytochrome P450 1.14.14.1

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00032 C00061 C00016 C03024 C00007 C01371 C00162 C01598 C06604 C00005 C00080 C99999 C00923 C03161 C00001 C01335 C05102 C05643 C06606 C00283 C00006 C99999 C00924
E.C. 1.14.14.1
1.6.2.4
1.6.2.4
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.6.2.4
1.6.2.4
1.6.2.4
1.6.2.4
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.14.14.1
1.6.2.4
1.6.2.4
1.6.2.4
Compound Heme FMN FAD Reduced flavoprotein O2 RH Fatty acid Melatonin Parathion NADPH H+ Oxidized hemoprotein Ferricytochrome Oxidized flavoprotein H2O ROH alpha-Hydroxy fatty acid 6-Hydroxymelatonin Paraoxon Hydrogen sulfide NADP+ Reduced hemoprotein Ferrocytochrome
Type aromatic ring (with nitrogen atoms),carboxyl group,heavy metal amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),peptide/protein others lipid fatty acid amide group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms) aromatic ring (only carbon atom),nitro group,phosphate group/phosphate ion,sulfide group amide group,amine group,nucleotide others aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,peptide/protein aromatic ring (with nitrogen atoms),carboxyl group,heavy metal amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),peptide/protein H2O lipid carbohydrate,fatty acid amide group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms) aromatic ring (only carbon atom),nitro group,phosphate group/phosphate ion sulfhydryl group amide group,amine group,nucleotide aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,peptide/protein aromatic ring (with nitrogen atoms),carboxyl group,heavy metal
ChEBI 17627
26355
17621
16238
15379
26689
27140
16796
27928
16474
15378
15377
2198
27827
16136
18009
PubChem 643976
643975
977
896
991
5884
1038
22247451
962
1864
9395
18779926
402
5886
1bu7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bu7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvyA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HEM-EDO Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Bound:EDO_1003 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvyB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HEM-EDO Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Bound:EDO_1004 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fagA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Bound:PAM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fagB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Bound:PAM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fagC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Bound:PAM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fagD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Bound:PAM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fahA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fahB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jmeA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jmeB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jpzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Analogue:140 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jpzB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Analogue:140 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1p0vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1p0vB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1p0wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1p0wB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1p0xA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1p0xB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2bmhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2bmhB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hpdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2hpdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bvyF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:FMN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Analogue:HEM-EDO (chain A) Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00179 & literature [11], [34]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bu7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1bu7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1bvyA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1bvyB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1fagA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1fagB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1fagC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1fagD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1fahA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 400(Heme iron binding) mutant T268A
1fahB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 400(Heme iron binding) mutant T268A
1jmeA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393H
1jmeB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393H
1jpzA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1jpzB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1p0vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393A
1p0vB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393A
1p0wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393W
1p0wB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393W
1p0xA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393Y
1p0xB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding) mutant F393Y
2bmhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
2bmhB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
2hpdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
2hpdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 268 CYS 400(Heme iron binding)
1bvyF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[11]
Fig.4, p.14737-147399
[16]
Fig.1, p.414
[17]
Fig.5, Fig.6, p.13820-13822
[18]
[20]
p.143-145
[21]
Fig.9, p.8408-8412
[27]
[29]
Fig.5, p.1867
[34]
p.13463-13464
[39]

References
[1]
Resource
Comments CHARACTERIZATION
Medline ID 92088245
PubMed ID 1727637
Journal Arch Biochem Biophys
Year 1992
Volume 292
Pages 20-8
Authors Boddupalli SS, Pramanik BC, Slaughter CA, Estabrook RW, Peterson JA
Title Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions.
Related PDB
Related UniProtKB P14779
[2]
Resource
Comments
Medline ID
PubMed ID 1334408
Journal Biochem J
Year 1992
Volume 288
Pages 503-9
Authors Miles JS, Munro AW, Rospendowski BN, Smith WE, McKnight J, Thomson AJ
Title Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1544935
Journal J Biol Chem
Year 1992
Volume 267
Pages 5614-20
Authors Tuck SF, Peterson JA, Ortiz de Montellano PR
Title Active site topologies of bacterial cytochromes P450101 (P450cam), P450108 (P450terp), and P450102 (P450BM-3). In situ rearrangement of their phenyl-iron complexes.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1608967
Journal Proc Natl Acad Sci U S A
Year 1992
Volume 89
Pages 5567-71
Authors Boddupalli SS, Hasemann CA, Ravichandran KG, Lu JY, Goldsmith EJ, Deisenhofer J, Peterson JA
Title Crystallization and preliminary x-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8257708
Journal Biochemistry
Year 1993
Volume 32
Pages 13732-41
Authors Shirane N, Sui Z, Peterson JA, Ortiz de Montellano PR
Title Cytochrome P450BM-3 (CYP102): regiospecificity of oxidation of omega-unsaturated fatty acids and mechanism-based inactivation.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-471
Medline ID 93342510
PubMed ID 8342039
Journal Science
Year 1993
Volume 261
Pages 731-6
Authors Ravichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, Deisenhofer J
Title Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.
Related PDB 2hpd
Related UniProtKB P14779
[7]
Resource
Comments
Medline ID
PubMed ID 8463285
Journal J Biol Chem
Year 1993
Volume 268
Pages 7553-61
Authors Klein ML, Fulco AJ
Title Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 7980400
Journal Biochem J
Year 1994
Volume 303
Pages 423-8
Authors Munro AW, Malarkey K, McKnight J, Thomson AJ, Kelly SM, Price NC, Lindsay JG, Coggins JR, Miles JS
Title The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7700866
Journal Protein Eng
Year 1994
Volume 7
Pages 1345-51
Authors Ruan KH, Milfeld K, Kulmacz RJ, Wu KK
Title Comparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID
Journal Acta Crystallogr D Biol Crystallogr
Year 1995
Volume 51
Pages 21-32
Authors Li H., Poulos TL
Title A method for processing diffraction data from twinned protein crystals and its application in the structure determination of an FAD/NADH-binding fragment of nitrate reductase.
Related PDB 2bmh
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7578081
Journal Biochemistry
Year 1995
Volume 34
Pages 14733-40
Authors Yeom H, Sligar SG, Li H, Poulos TL, Fulco AJ
Title The role of Thr268 in oxygen activation of cytochrome P450BM-3.
Related PDB 1fah
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 7578214
Journal Biochim Biophys Acta
Year 1995
Volume 1231
Pages 255-64
Authors Munro AW, Lindsay JG, Coggins JR, Kelly SM, Price NC
Title NADPH oxidase activity of cytochrome P-450 BM3 and its constituent reductase domain.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8829615
Journal Biochem Mol Biol Int
Year 1996
Volume 38
Pages 553-8
Authors Uvarov VYu, Lyashenko AA, Zimin AG
Title Comparative analysis of the secondary structural motifs of P450BM-3 and the regions located upstream of the calmodulin-binding domain in the nitric oxide synthases.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 8942669
Journal Biochemistry
Year 1996
Volume 35
Pages 15029-37
Authors Murataliev MB, Feyereisen R
Title Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9010597
Journal Biochimie
Year 1996
Volume 78
Pages 695-9
Authors Li H, Poulos TL
Title Conformational dynamics in cytochrome P450-substrate interactions.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 8612070
Journal Nat Struct Biol
Year 1996
Volume 3
Pages 414-7
Authors Modi S, Sutcliffe MJ, Primrose WU, Lian LY, Roberts GC
Title The catalytic mechanism of cytochrome P450 BM3 involves a 6 A movement of the bound substrate on reduction.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 9374858
Journal Biochemistry
Year 1997
Volume 36
Pages 13816-23
Authors Daff SN, Chapman SK, Turner KL, Holt RA, Govindaraj S, Poulos TL, Munro AW
Title Redox control of the catalytic cycle of flavocytochrome P-450 BM3.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9048540
Journal Biochemistry
Year 1997
Volume 36
Pages 1567-72
Authors Oliver CF, Modi S, Sutcliffe MJ, Primrose WU, Lian LY, Roberts GC
Title A single mutation in cytochrome P450 BM3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9284282
Journal Biophys J
Year 1997
Volume 73
Pages 1147-59
Authors Arnold GE, Ornstein RL
Title Molecular dynamics study of time-correlated protein domain motions and molecular flexibility: cytochrome P450BM-3.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-471
Medline ID 97185914
PubMed ID 9033595
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 140-6
Authors Li H, Poulos TL
Title The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid.
Related PDB 1fag
Related UniProtKB P14779
[21]
Resource
Comments
Medline ID
PubMed ID 9204888
Journal Biochemistry
Year 1997
Volume 36
Pages 8401-12
Authors Murataliev MB, Klein M, Fulco A, Feyereisen R
Title Functional interactions in cytochrome P450BM3: flavin semiquinone intermediates, role of NADP(H), and mechanism of electron transfer by the flavoprotein domain.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 9500975
Journal Biochem Biophys Res Commun
Year 1998
Volume 243
Pages 811-5
Authors Hudeeek J, Baumruk V, Anzenbacher P, Munro AW
Title Catalytically self-sufficient P450 CYP102 (cytochrome P450 BM-3): resonance Raman spectral characterization of the heme domain and of the holoenzyme.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 9843385
Journal Biochemistry
Year 1998
Volume 37
Pages 15799-807
Authors Noble MA, Quaroni L, Chumanov GD, Turner KL, Chapman SK, Hanzlik RP, Munro AW
Title Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 10222011
Journal Anal Biochem
Year 1999
Volume 269
Pages 359-66
Authors Schwaneberg U, Schmidt-Dannert C, Schmitt J, Schmid RD
Title A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 9888815
Journal Biochemistry
Year 1999
Volume 38
Pages 751-61
Authors Davydov DR, Hui Bon Hoa G, Peterson JA
Title Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 10521277
Journal Biochemistry
Year 1999
Volume 38
Pages 13699-706
Authors Deng TJ, Proniewicz LM, Kincaid JR, Yeom H, Macdonald ID, Sligar SG
Title Resonance Raman studies of cytochrome P450BM3 and its complexes with exogenous ligands.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 10593892
Journal J Biol Chem
Year 1999
Volume 274
Pages 36097-106
Authors Sevrioukova IF, Hazzard JT, Tollin G, Poulos TL
Title The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 10447203
Journal J Biomol Struct Dyn
Year 1999
Volume 16
Pages 1189-203
Authors Chang YT, Loew GH
Title Molecular dynamics simulations of P450 BM3--examination of substrate-induced conformational change.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-458 AND 459-649
Medline ID 99162523
PubMed ID 10051560
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 1863-8
Authors Sevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL
Title Structure of a cytochrome P450-redox partner electron-transfer complex.
Related PDB 1bu7 1bvy
Related UniProtKB P14779
[30]
Resource
Comments
Medline ID
PubMed ID 11164266
Journal J Biotechnol
Year 2000
Volume 84
Pages 249-57
Authors Schwaneberg U, Appel D, Schmitt J, Schmid RD
Title P450 in biotechnology: zinc driven omega-hydroxylation of p-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 10924137
Journal Biochemistry
Year 2000
Volume 39
Pages 9419-29
Authors Haines DC, Sevrioukova IF, Peterson JA
Title The FMN-binding domain of cytochrome P450BM-3: resolution, reconstitution, and flavin analogue substitution.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 11027150
Journal Biochemistry
Year 2000
Volume 39
Pages 12699-707
Authors Murataliev MB, Feyereisen R
Title Functional interactions in cytochrome P450BM3. Evidence that NADP(H) binding controls redox potentials of the flavin cofactors.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 11368173
Journal Arch Biochem Biophys
Year 2001
Volume 387
Pages 117-24
Authors Cowart LA, Falck JR, Capdevila JH
Title Structural determinants of active site binding affinity and metabolism by cytochrome P450 BM-3.
Related PDB
Related UniProtKB
[34]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-470
Medline ID 21552924
PubMed ID 11695892
Journal Biochemistry
Year 2001
Volume 40
Pages 13456-65
Authors Haines DC, Tomchick DR, Machius M, Peterson JA
Title Pivotal role of water in the mechanism of P450BM-3.
Related PDB 1jpz
Related UniProtKB P14779
[35]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11695889
Journal Biochemistry
Year 2001
Volume 40
Pages 13430-8
Authors Ost TW, Munro AW, Mowat CG, Taylor PR, Pesseguiero A, Fulco AJ, Cho AK, Cheesman MA, Walkinshaw MD, Chapman SK
Title Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.
Related PDB 1jme
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 12427012
Journal Biochemistry
Year 2002
Volume 41
Pages 13514-25
Authors Kariakin A, Davydov D, Peterson JA, Jung C
Title A new approach to the study of protein-protein interaction by FTIR: complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 12020135
Journal Bioorg Chem
Year 2002
Volume 30
Pages 107-18
Authors Rock DA, Boitano AE, Wahlstrom JL, Rock DA, Jones JP
Title Use of kinetic isotope effects to delineate the role of phenylalanine 87 in P450(BM-3).
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 12237219
Journal J Inorg Biochem
Year 2002
Volume 91
Pages 515-26
Authors Fuziwara S, Sagami I, Rozhkova E, Craig D, Noble MA, Munro AW, Chapman SK, Shimizu T
Title Catalytically functional flavocytochrome chimeras of P450 BM3 and nitric oxide synthase.
Related PDB
Related UniProtKB
[39]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 14653735
Journal J Am Chem Soc
Year 2003
Volume 125
Pages 15010-20
Authors Ost TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S
Title Oxygen activation and electron transfer in flavocytochrome P450 BM3.
Related PDB 1p0v 1p0w 1p0x
Related UniProtKB

Comments
This protein is composed of two enzymatic domain, the N-terminal doman of cytochrome P450 BM-3 (EC 1.14.14.1) and the C-terminal domain of NADPH-cytochrome-P450 reductase (EC 1.6.2.4).
The C-terminal NADPH-cytochrome-P450 reductase comprises flavodoxin-like domain, FAD-binding domain.
Whilst the N-terminal structure of cytochrome P450 BM-3 domain has been determined, the C-terminal enzyme structure is only partially determined (only flavodoxin-like domain; PDB 1bvy).
This enzyme catalyzes the following reactions (see [17] and [21]):
(A) Hydride transfer from NADPH to FAD, giving NADP+ and FADH2:
(B) Hydride transfer from FADH2 to FMN, giving FAD and FMNH2:
(C) Electron transfer from FMNH2 to P450 (or heme):
(D) Oxygenation of substrate by O2, producing hydroxylated product and water (H2O) at P450:

Created Updated
2004-10-20 2009-02-26