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) |
|---|---|
| 1.10.630.10 : Cytochrome p450 | S00033 S00031 S00030 |
| 3.40.50.360 : Rossmann fold | S00522 S00343 M00006 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Includes | Pfam |
|---|---|---|---|---|
| P14779 |
Bifunctional P-450/NADPH-P450 reductase
|
Cytochrome P450(BM-3)
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 | NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein. RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O. | Cytoplasm (By similarity). | FAD. FMN. Heme group. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| 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 |
| MAP00982 | Drug metabolism - cytochrome P450 | 1.14.14.1 |
| MAP00983 | Drug metabolism - other enzymes | 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 17627 26355 |
17621 17621 |
16238 16238 |
15379 26689 27140 15379 26689 27140 |
16796 16796 |
27928 27928 |
16474 16474 |
15378 15378 |
15377 15377 |
2198 2198 |
27827 27827 |
16136 16136 |
18009 18009 |
||||||||||||||||
| PubChem |
643976 643976 |
643975 643975 |
977 977 |
896 896 |
991 991 |
5884 5884 |
1038 1038 |
22247451 962 22247451 962 |
1864 1864 |
9395 9395 |
18779926 402 18779926 402 |
5886 5886 |
|||||||||||||||||
| 1bu7A |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1bu7B |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1bvyA |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Bound:PAM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fagB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Bound:PAM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fagC |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Bound:PAM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fagD |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Bound:PAM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fahA |
|
|
|
|
|
Analogue:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fahB |
|
|
|
|
|
Analogue:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1jmeA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1jmeB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1jpzA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:140 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1jpzB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:140 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1p0vA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1p0vB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1p0wA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1p0wB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1p0xA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1p0xB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2bmhA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2bmhB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2hpdA |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 2hpdB |
|
|
|
|
|
Bound:HEM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1bvyF |
|
|
|
|
|
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 |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1bu7B |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1bvyA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1bvyB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1fagA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1fagB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1fagC |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1fagD |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1fahA |
|
|
|
|
|
CYS 400(Heme iron binding) | mutant T268A | |||
| 1fahB |
|
|
|
|
|
CYS 400(Heme iron binding) | mutant T268A | |||
| 1jmeA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393H | ||
| 1jmeB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393H | ||
| 1jpzA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1jpzB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1p0vA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393A | ||
| 1p0vB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393A | ||
| 1p0wA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393W | ||
| 1p0wB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393W | ||
| 1p0xA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393Y | ||
| 1p0xB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | mutant F393Y | ||
| 2bmhA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 2bmhB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 2hpdA |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 2hpdB |
|
|
|
|
|
THR 268 | CYS 400(Heme iron binding) | |||
| 1bvyF |
|
|
|
|
|
|||||
| 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. |
| 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), |
| 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, |
| 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, |
| 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. |
| 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. |
| 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, |
| 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, |
| 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, |
| 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. |
| 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, |
| 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. |
| 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 C-terminal NADPH-cytochrome-P450 reductase comprises flavodoxin-like domain, Whilst the N-terminal structure of cytochrome P450 BM-3 domain has been determined, This enzyme catalyzes the following reactions (see [17] and [21]): (A) Hydride transfer from NADPH to FAD, (B) Hydride transfer from FADH2 to FMN, (C) Electron transfer from FMNH2 to P450 (or heme): (D) Oxygenation of substrate by O2, |
| Created | Updated |
|---|---|
| 2004-10-20 | 2009-02-26 |