Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis
about
A drunken search in crystallization space.Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesisComparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathwaysStructural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450BioI ACP complexCrystal Structures of Cytochrome P450 105P1 from Streptomyces avermitilis: Conformational Flexibility and Histidine Ligation StateP450cam Visits an Open Conformation in the Absence of Substrate ,Structural Characterization of OxyD, a Cytochrome P450 Involved in -Hydroxytyrosine Formation in Vancomycin BiosynthesisCrystal structure of a phenol-coupling P450 monooxygenase involved in teicoplanin biosynthesisThe role of Ile87 of CYP158A2 in oxidative coupling reactionCytochrome P450 OxyBtei catalyzes the first phenolic coupling step in teicoplanin biosynthesisStructure of OxyA tei: completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascadeCrystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound FormMore than just recruitment: the X-domain influences catalysis of the first phenolic coupling reaction in A47934 biosynthesis by Cytochrome P450 StaHVariations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyBiochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934Three clusters of conformational states in p450cam reveal a multistep pathway for closing of the substrate access channel.The Mycobacterium tuberculosis cytochrome P450 system.Complete genome sequence and comparative genomic analyses of the vancomycin-producing Amycolatopsis orientalis.Natural products version 2.0: connecting genes to molecules.Cytochrome P450: what have we learned and what are the future issues?Proximal ligand electron donation and reactivity of the cytochrome P450 ferric-peroxo anionBioprospecting potential of halogenases from Arctic marine actinomycetes.Unusual properties of the cytochrome P450 superfamily.Detection, distribution, and organohalogen compound discovery implications of the reduced flavin adenine dinucleotide-dependent halogenase gene in major filamentous actinomycete taxonomic groups.How nature morphs peptide scaffolds into antibioticsConformational plasticity and structure/function relationships in cytochromes P450.Carrier protein substrates in cytochrome P450-catalysed oxidation.Function of MbtH homologs in nonribosomal peptide biosynthesis and applications in secondary metabolite discovery.Diversity of P450 enzymes in the biosynthesis of natural productsThe biocatalytic repertoire of natural biaryl formation.Progress in Understanding the Genetic Information and Biosynthetic Pathways behind Amycolatopsis Antibiotics, with Implications for the Continued Discovery of Novel Drugs.Oxidative Cyclization in Natural Product BiosynthesisBiosynthesis of chloro-beta-hydroxytyrosine, a nonproteinogenic amino acid of the peptidic backbone of glycopeptide antibiotics.Regio- and stereodivergent antibiotic oxidative carbocyclizations catalysed by Rieske oxygenase-like enzymes.Structural analysis of SgvP involved in carbon-sulfur bond formation during griseoviridin biosynthesis.Sequencing and analysis of the biosynthetic gene cluster of the lipopeptide antibiotic Friulimicin in Actinoplanes friuliensisStructure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-A resolution: insight into the range of P450 conformations and the coordination of redox partner binding.The biosynthesis of vancomycin-type glycopeptide antibiotics--a model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases.Generate a bioactive natural product library by mining bacterial cytochrome P450 patterns.Metabolism of CJ-036878, N-(3-phenethoxybenzyl)-4-hydroxybenzamide, in liver microsomes and recombinant cytochrome P450 enzymes: metabolite identification by LC-UV/MS(n) and (1)H-NMR.
P2860
Q27317052-6426F8E5-BDDD-499E-A990-96B87DB6C291Q27641760-F181C301-5C65-49A4-A191-6524B09EB5EFQ27642846-CD3714A3-B296-4922-B42F-F94E77654C0FQ27652439-470F6094-D89E-447E-AB33-9BEFD94FED59Q27653132-95ADC244-7B19-4132-930D-7B7CAD630468Q27660275-2DF9E426-9690-48E8-9BF5-6E05C1990DE0Q27662097-BCD2D900-F059-4A2A-8AF3-1E918CE77232Q27667347-BF9D3C71-78B6-4B28-9D2A-BB2C11065F99Q27676475-CD77C57A-E87C-4093-AFEC-8EDEA343EE27Q27695990-E2CBA4C4-5206-4A90-BED3-688309AE69E5Q27703740-AC0BAA3E-3580-41B4-B255-82D06F6EBF1FQ27704000-400C9B30-B9CB-454E-AFD6-31179FAA6B89Q27723434-9E0AD94F-F685-40C6-993A-E280D79019EDQ28304165-CF74D59D-0912-4738-AAB5-B516DD5A1F9FQ28817213-641D01CD-B9D1-49E2-9977-48258F94DB66Q30498059-65D8DEC7-2244-4D62-82C8-109A8C634755Q33615471-0EF73E08-5EA3-40B4-ADB3-7079D331C7DDQ33722342-45D3187B-8C53-42C3-BCE8-353DFC0B3560Q34096062-0DD06862-3AE9-417E-8174-2CF9B4D19D80Q35828009-736FA444-C32C-4176-8AA7-69AF451CAC76Q35897516-0FA0FA8D-36AF-4E58-AD28-20FC9CD1817EQ35953004-799F1A5C-92F7-44A0-851C-D556C8546E83Q36512916-5CFA1A86-D24E-4167-B3CD-CDCC8E942DCFQ37256142-6F99297D-27E8-43E7-8C2B-F6B51139533BQ37341890-9EEBD2CB-A531-4CEB-AE3B-F1F20B6A97A5Q37743467-FDB13CF6-1A89-41BA-894F-44CB87477988Q37829645-6E24EB34-4003-4DDE-BD30-0079C3D97AEEQ37914045-32D02DF2-AA55-461E-ABC0-4FB20A54AB56Q38028349-04DADAE8-2A7A-48CC-ADE9-CC0D91FA349BQ38232045-9F5AA03F-5ECA-425B-BD16-ED0A09C57395Q38616773-3A335635-9DF5-412B-8313-5CA636AC5BC7Q39034361-A2E6C1A4-BFAC-47CC-A54D-8993DF9C7AC3Q39964339-8F871934-3BB9-4AFF-9E40-DB8B275F6DA2Q41973980-2705685A-E0F7-433A-A054-7A3B4D86A2C9Q41978986-75F3F977-AB96-4330-A2EC-8A00ABEEF735Q42608852-33901AE2-28EF-4CD2-BBE9-8DDF66CFEBFFQ42625456-71E65E1E-FEF0-40DD-9AFF-23935DE4D691Q45224386-24FD40CF-0295-4711-AB10-CADB9A87ED0AQ45269243-B601EF8A-7AD7-490B-9D09-D5C94469E6A9Q46886062-78217EB1-1EAF-4FBD-BECE-019F4AFFC95F
P2860
Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@ast
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@en
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@nl
type
label
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@ast
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@en
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@nl
prefLabel
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@ast
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@en
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@nl
P2093
P2860
P50
P356
P1476
Crystal structure of OxyB, a c ...... during vancomycin biosynthesis
@en
P2093
Bojan Bister
Daniel Bischoff
Francesca Vitali
Jan W Vrijbloed
John A Robinson
Katja Zerbe
Markus Heck
Severine Rouset
Stefan Pelzer
Weiwen Zhang
P2860
P304
P356
10.1074/JBC.M206342200
P407
P577
2002-12-06T00:00:00Z