Extending the substrate scope of a Baeyer-Villiger monooxygenase by multiple-site mutagenesis.
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Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applicationsStructural and Catalytic Characterization of a Fungal Baeyer-Villiger MonooxygenaseScreening through the PLICable promoter toolbox enhances protein production in Escherichia coli.Ester coupling reactions--an enduring challenge in the chemical synthesis of bioactive natural products.Directed evolution of phenylacetone monooxygenase as an active catalyst for the Baeyer-Villiger conversion of cyclohexanone to caprolactone.Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase.Catalytic mechanism of phenylacetone monooxygenases for non-native linear substrates.Controlling the Regioselectivity of Baeyer-Villiger Monooxygenases by Mutation of Active-Site Residues.Manipulating the stereoselectivity of the thermostable Baeyer-Villiger monooxygenase TmCHMO by directed evolution.Spatial requirement for PAMO for transformation of non-native linear substrates.Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase
P2860
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P2860
Extending the substrate scope of a Baeyer-Villiger monooxygenase by multiple-site mutagenesis.
description
2013 nî lūn-bûn
@nan
2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Extending the substrate scope ...... by multiple-site mutagenesis.
@en
type
label
Extending the substrate scope ...... by multiple-site mutagenesis.
@en
prefLabel
Extending the substrate scope ...... by multiple-site mutagenesis.
@en
P2093
P2860
P50
P1476
Extending the substrate scope ...... e by multiple-site mutagenesis
@en
P2093
Alexander Dennig
Hanna M Dudek
Marco W Fraaije
P2860
P2888
P304
P356
10.1007/S00253-013-5364-1
P407
P577
2013-11-19T00:00:00Z