Joint Functions of Protein Residues and NADP(H) in Oxygen Activation by Flavin-containing Monooxygenase
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Snapshots of Enzymatic Baeyer-Villiger Catalysis: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATIONTwo Structures of an N-Hydroxylating Flavoprotein Monooxygenase: ORNITHINE HYDROXYLASE FROM PSEUDOMONAS AERUGINOSAA 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 ConformationMutations 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.How pH Modulates the Reactivity and Selectivity of a Siderophore-Associated Flavin MonooxygenaseHydrogen peroxide elimination from C4a-hydroperoxyflavin in a flavoprotein oxidase occurs through a single proton transfer from flavin N5 to a peroxide leaving groupMechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases.The Origin and Evolution of Baeyer-Villiger Monooxygenases (BVMOs): An Ancestral Family of Flavin Monooxygenases.Role of Ser-257 in the sliding mechanism of NADP(H) in the reaction catalyzed by the Aspergillus fumigatus flavin-dependent ornithine N5-monooxygenase SidA.MICAL, the flavoenzyme participating in cytoskeleton dynamicsHeteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.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.Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms.Inactivation mechanism of N61S mutant of human FMO3 towards trimethylamine.Structural mechanism for bacterial oxidation of oceanic trimethylamine into trimethylamine N-oxide.Exploring the biocatalytic scope of a bacterial flavin-containing monooxygenase.
P2860
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P2860
Joint Functions of Protein Residues and NADP(H) in Oxygen Activation by Flavin-containing Monooxygenase
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@ast
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@en
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@nl
type
label
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@ast
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@en
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@nl
prefLabel
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@ast
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@en
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@nl
P2093
P2860
P356
P1476
Joint Functions of Protein Res ...... lavin-containing Monooxygenase
@en
P2093
Daniel E Torres Pazmiño
Marco W Fraaije
Roberto Orru
P2860
P304
P356
10.1074/JBC.M110.161372
P407
P577
2010-11-05T00:00:00Z