Redirecting P450 EryK Specificity by Rational Site-Directed Mutagenesis

Autor: Beatrice Vallone, Linda Celeste Montemiglio, Chiara Ardiccioni, G. Avella, Alberto Macone, Carmelinda Savino

Publikováno v: Biochemistry (Easton) 52 (2013): 3678–3687. doi:10.1021/bi400223j
info:cnr-pdr/source/autori:Montemiglio, LC [ 1,2 ] ; Macone, A [ 1,2 ] ; Ardiccioni, C [ 3,4 ] ; Avella, G [ 1,2 ] ; Vallone, B [ 1,2 ] ; Savino, C [ 1,2]/titolo:Redirecting P450 EryK specificity by rational site-directed mutagenesis./doi:10.1021%2Fbi400223j/rivista:Biochemistry (Easton)/anno:2013/pagina_da:3678/pagina_a:3687/intervallo_pagine:3678–3687/volume:52
Biochemistry
Biochemistry, American Chemical Society, 2013, 52 (21), pp.3678-87. ⟨10.1021/bi400223j⟩

The C-12 hydroxylase EryK is a bacterial cytochrome P450, active during one of the final tailoring steps of erythromycin A (ErA) biosynthesis. Its tight substrate specificity, restricted to the metabolic intermediate ErD, leads to the accumulation in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3864dcc64fe3be942f913c9f61962bb0
https://doi.org/10.1021/bi400223j

Unusual Regioselectivity and Active Site Topology of Human Cytochrome P450 2J2

Autor: Pierre Lafite, Patrick M. Dansette, François André, Darryl C. Zeldin, Daniel Mansuy

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2007, pp.10237-10247
Biochemistry, American Chemical Society, 2007, 46 (36), pp.10237-47. ⟨10.1021/bi700876a⟩
Biochemistry, American Chemical Society, 2007, 46 (36), pp.10237-47. 〈10.1021/bi700876a〉
Biochemistry, 2007, pp.10237-10247
Biochemistry, 2007, 46 (36), pp.10237-47. ⟨10.1021/bi700876a⟩

The oxidation of six derivatives of terfenadone by recombinant human CYP2J2 (CYP = cytochrome P450) was studied by high-performance liquid chromatography coupled to mass spectrometry (MS) using tandem MS techniques and by 1H NMR spectroscopy. CYP2J2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62f5295373619791c2e567d42d8697a8
https://hal.archives-ouvertes.fr/hal-00259028

A new gene involved in coenzyme Q biosynthesis in Escherichia coli: UbiI functions in aerobic C5-hydroxylation

Autor: Hajj Chehade, Mahmoud, Loiseau, Laurent, Lombard, Murielle, Pecqueur, Ludovic, Ismail, Alexandre, Smadja, Myriam, Golinelli-Pimpaneau, Béatrice, Mellot-Draznieks, Caroline, Hamelin, Olivier, Aussel, Laurent, Kieffer-Jaquinod, Sylvie, Labessan, Natty, Barras, Frédéric, Fontecave, Marc, Pierrel, Fabien

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (27), pp.20085-92. ⟨10.1074/jbc.M113.480368⟩
Journal of Biological Chemistry, 2013, 288 (27), pp.20085-92. ⟨10.1074/jbc.M113.480368⟩

International audience; Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multip

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6b4f6b11a40315ebf5c93db707fb4b39
https://hal.archives-ouvertes.fr/hal-00904907/file/manuscript.pdf

Early apoptotic reorganization of spliceosomal proteins involves caspases, CAD and rearrangement of NuMA

Autor: Dieker, Jürgen, Iglesias-Guimarais, Victoria, Décossas, Marion, Stevenin, James, Van Der Vlag, Johan, Yuste, Victor J, Muller, Sylviane

Publikováno v: Traffic
Traffic, Wiley, 2012, 13 (2), pp.257-72. ⟨10.1111/j.1600-0854.2011.01307.x⟩
Traffic; International Journal of Intracellular Transport, 13, 2, pp. 257-72
Traffic; International Journal of Intracellular Transport, 13, 257-72

Item does not contain fulltext The reorganization of nuclear structures is an important early feature of apoptosis and involves the activity of specific proteases and nucleases. Well-known is the condensation and fragmentation of chromatin; however,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::105a15f4afb91b64b8484606a2065b2e
https://pubmed.ncbi.nlm.nih.gov/22023725

Identification and induction of cytochrome P450s involved in the metabolism of flavone-8-acetic acid in mice

Autor: Pham, Minh Hien, Rhinn, Hervé, Auzeil, Nicolas, Regazzetti, Anne, Harami, Djamel Eddine, Scherman, Daniel, Chabot, Guy

Publikováno v: Drug Metabolism Letters
Drug Metabolism Letters, Bentham Science Publishers, 2011, 5 (2), pp.73-84

International audience; The metabolism of flavone-8-acetic acid (FAA) has been hypothesized to be partly responsible for its potent anticancer activity in mice. The purpose of this study was to identify the mouse enzymes involved in FAA Phase I metab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6c2f6090986bc1da6f2610a0ca373291
https://www.hal.inserm.fr/inserm-00709942/file/inserm-00709942_edited.pdf