5XA3
Crystal Structure of P450BM3 with Benzyloxycarbonyl-L-prolyl-L-phenylalanine
Summary for 5XA3
| Entry DOI | 10.2210/pdb5xa3/pdb |
| Descriptor | Bifunctional cytochrome P450/NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, DIMETHYL SULFOXIDE, ... (7 entities in total) |
| Functional Keywords | cytochrome p450, oxidoreductase |
| Biological source | Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / VKM B-512) |
| Cellular location | Cytoplasm : P14779 |
| Total number of polymer chains | 4 |
| Total formula weight | 213784.77 |
| Authors | Shoji, O.,Yanagisawa, S.,Stanfield, J.K.,Suzuki, K.,Kasai, C.,Cong, Z.,Sugimoto, H.,Shiro, Y.,Watanabe, Y. (deposition date: 2017-03-10, release date: 2018-02-21, Last modification date: 2023-11-22) |
| Primary citation | Shoji, O.,Yanagisawa, S.,Stanfield, J.K.,Suzuki, K.,Cong, Z.,Sugimoto, H.,Shiro, Y.,Watanabe, Y. Direct Hydroxylation of Benzene to Phenol by Cytochrome P450BM3 Triggered by Amino Acid Derivatives. Angew. Chem. Int. Ed. Engl., 56:10324-10329, 2017 Cited by PubMed Abstract: The selective hydroxylation of benzene to phenol, without the formation of side products resulting from overoxidation, is catalyzed by cytochrome P450BM3 with the assistance of amino acid derivatives as decoy molecules. The catalytic turnover rate and the total turnover number reached 259 min P450BM3 and 40 200 P450BM3 when N-heptyl-l-proline modified with l-phenylalanine (C7-l-Pro-l-Phe) was used as the decoy molecule. This work shows that amino acid derivatives with a totally different structure from fatty acids can be used as decoy molecules for aromatic hydroxylation by wild-type P450BM3. This method for non-native substrate hydroxylation by wild-type P450BM3 has the potential to expand the utility of P450BM3 for biotransformations. PubMed: 28544674DOI: 10.1002/anie.201703461 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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