Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Idorenyin S. Ekanem"'
Autor:
Michael G Joyce, George J. Baker, Rajasekhar Neeli, Robin Curtis, Andrew W. Munro, David Leys, Hazel M. Girvan, Olivier Roitel, Adrian J. Dunford, Idorenyin S. Ekanem
Publikováno v:
FEBS Journal. 279:1694-1706
We report the crystal structure of the FAD/NADPH-binding domain (FAD domain) of the biotechnologically important Bacillus megaterium flavocytochrome P450 BM3, the last domain of the enzyme to be structurally resolved. The structure was solved in both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::58a1b54d5a272f45e2267abe7a04bc2a
https://doi.org/10.1111/j.1742-4658.2012.08544.x
https://doi.org/10.1111/j.1742-4658.2012.08544.x
Autor:
Michael G, Joyce, Idorenyin S, Ekanem, Olivier, Roitel, Adrian J, Dunford, Rajasekhar, Neeli, Hazel M, Girvan, George J, Baker, Robin A, Curtis, Andrew W, Munro, David, Leys
Publikováno v:
The FEBS journal. 279(9)
We report the crystal structure of the FAD/NADPH-binding domain (FAD domain) of the biotechnologically important Bacillus megaterium flavocytochrome P450 BM3, the last domain of the enzyme to be structurally resolved. The structure was solved in both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::848e83b1d1c9a314344b0ddffb2d8d27
https://pubmed.ncbi.nlm.nih.gov/22356131
https://pubmed.ncbi.nlm.nih.gov/22356131
Autor:
Michael W. Voice, M. Gordon Joyce, Adrian J. Dunford, Timothy N. Waltham, Paul N. Williams, Robin Curtis, Hazel M. Girvan, Karl Fisher, Andrew W. Munro, Idorenyin S. Ekanem, David Leys, Rajasekhar Neeli
Publikováno v:
Archives of biochemistry and biophysics. 507(1)
Bacillus megaterium P450 BM3 (BM3) is a P450/P450 reductase fusion enzyme, where the dimer is considered the active form in NADPH-dependent fatty acid hydroxylation. The BM3 W1046A mutant was generated, removing an aromatic "shield" from its FAD isoa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e20e90c5c8b8a42e9888633a2ec88468
https://pubmed.ncbi.nlm.nih.gov/20868649
https://pubmed.ncbi.nlm.nih.gov/20868649
Autor:
Andrew W. Munro, W. Ewen Smith, Harriet E. Seward, Hazel M. Girvan, David Leys, Myles R. Cheesman, Idorenyin S. Ekanem, R.E. Littleford, Helen S. Toogood
Publikováno v:
The Biochemical journal. 417(1)
Bacillus megaterium flavocytochrome P450 BM3 is a catalytically self-sufficient fatty acid hydroxylase formed by fusion of soluble NADPH–cytochrome P450 reductase and P450 domains. Selected mutations at residue 264 in the haem (P450) domain of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16d606997ef0949a7e1311a2ac8ba080
https://pubmed.ncbi.nlm.nih.gov/18721129
https://pubmed.ncbi.nlm.nih.gov/18721129