Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor
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Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Δ(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453Snapshots of Enzymatic Baeyer-Villiger Catalysis: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATIONTwo Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSAIdentification of the NAD(P)H Binding Site of Eukaryotic UDP-Galactopyranose MutaseStructural analysis of a novel cyclohexylamine oxidase from Brevibacterium oxydans IH-35AA flavoprotein monooxygenase that catalyses a Baeyer-Villiger reaction and thioether oxidation using NADH as the nicotinamide cofactorThe Substrate-Bound Crystal Structure of a Baeyer–Villiger Monooxygenase Exhibits a Criegee-like ConformationExploring the Structural Basis of Substrate Preferences in Baeyer-Villiger MonooxygenasesMolecular Insight into Substrate Recognition and Catalysis of Baeyer–Villiger Monooxygenase MtmOIV, the Key Frame-Modifying Enzyme in the Biosynthesis of Anticancer Agent MithramycinMutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivityBeyond the Protein Matrix: Probing Cofactor Variants in a Baeyer-Villiger Oxygenation Reaction.Structural and Catalytic Characterization of a Fungal Baeyer-Villiger MonooxygenaseProspecting Biotechnologically-Relevant Monooxygenases from Cold Sediment Metagenomes: An In Silico ApproachCrystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase.Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase.Functional assembly of camphor converting two-component Baeyer-Villiger monooxygenases with a flavin reductase from E. coli.Extending the substrate scope of a Baeyer-Villiger monooxygenase by multiple-site mutagenesis.Stabilization of cyclohexanone monooxygenase by a computationally designed disulfide bond spanning only one residue.Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases.An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylationCharacterization of CpdC, a large-ring lactone-hydrolyzing enzyme from Pseudomonas sp. strain HI-70, and its use as a fusion tag facilitating overproduction of proteins in Escherichia coli.Isolation and initial characterization of a novel type of Baeyer-Villiger monooxygenase activity from a marine microorganismRole of Ser-257 in the sliding mechanism of NADP(H) in the reaction catalyzed by the Aspergillus fumigatus flavin-dependent ornithine N5-monooxygenase SidA.Genome mining in Streptomyces avermitilis: A biochemical Baeyer-Villiger reaction and discovery of a new branch of the pentalenolactone family tree.Molecular Characterization of the Cercosporin Biosynthetic Pathway in the Fungal Plant Pathogen Cercospora nicotianaeInsight into the orientational versatility of steroid substrates-a docking and molecular dynamics study of a steroid receptor and steroid monooxygenase.Mapping the substrate binding site of phenylacetone monooxygenase from Thermobifida fusca by mutational analysis.Directed evolution of phenylacetone monooxygenase as an active catalyst for the Baeyer-Villiger conversion of cyclohexanone to caprolactone.Enzymatic site-selectivity enabled by structure-guided directed evolution.Identification and engineering of the cytochalasin gene cluster from Aspergillus clavatus NRRL 1.A carbonate-forming Baeyer-Villiger monooxygenase.Identification of a putative flavin adenine dinucleotide-binding monooxygenase as a regulator for Myxococcus xanthus development.Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from Cellvibrio sp. BR and Pseudomonas stutzeri NF13.Reply to the Comment by Littlechild and Isupov.Investigating the coenzyme specificity of phenylacetone monooxygenase from Thermobifida fusca.Cloning, expression and characterization of a eukaryotic cycloalkanone monooxygenase from Cylindrocarpon radicicola ATCC 11011.Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA.Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase.Substitution of a Single Amino Acid Reverses the Regiospecificity of the Baeyer-Villiger Monooxygenase PntE in the Biosynthesis of the Antibiotic Pentalenolactone.
P2860
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P2860
Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Crystal structures of cyclohex ...... vements and a sliding cofactor
@ast
Crystal structures of cyclohex ...... vements and a sliding cofactor
@en
Crystal structures of cyclohex ...... vements and a sliding cofactor
@nl
type
label
Crystal structures of cyclohex ...... vements and a sliding cofactor
@ast
Crystal structures of cyclohex ...... vements and a sliding cofactor
@en
Crystal structures of cyclohex ...... vements and a sliding cofactor
@nl
prefLabel
Crystal structures of cyclohex ...... vements and a sliding cofactor
@ast
Crystal structures of cyclohex ...... vements and a sliding cofactor
@en
Crystal structures of cyclohex ...... vements and a sliding cofactor
@nl
P2093
P3181
P356
P1476
Crystal structures of cyclohex ...... vements and a sliding cofactor
@en
P2093
Akihiro Imura
Hiroaki Iwaki
Hélène Bergeron
I Ahmad Mirza
Peter C K Lau
Shaozhao Wang
Stephan Grosse
Yoshie Hasegawa
P304
P3181
P356
10.1021/JA9010578
P407
P577
2009-07-01T00:00:00Z