Controlling the Regioselectivity of Baeyer-Villiger Monooxygenases by Mutation of Active-Site Residues.

about

Manipulating the stereoselectivity of the thermostable Baeyer-Villiger monooxygenase TmCHMO by directed evolution.Exploring the Substrate Scope of Baeyer-Villiger Monooxygenases with Branched Lactones as Entry towards Polyesters.Biocatalytic oxidation reactions - a Chemist's perspective.

P2860

Q50052452-C12BC31B-7074-4527-B555-5292D6716FD8 Q50097257-EADDBEDF-846E-4AE4-BC9B-B2B0AA09B901 Q53835321-14188371-7692-4C81-84BE-2896EEFBD362

P2860

Controlling the Regioselectivity of Baeyer-Villiger Monooxygenases by Mutation of Active-Site Residues.

Item

http://www.wikidata.org/entity/Q48144179

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@en

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@nl

type

Item

label

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@en

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@nl

prefLabel

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@en

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@nl

P1476

Controlling the Regioselectivi ...... ation of Active-Site Residues.

@en

P2093

Kathleen Balke

http://www.w3.org/2001/XMLSchema#string

Marcus Bäumgen

http://www.w3.org/2001/XMLSchema#string

P2860

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 17453

Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor

Snapshots of Enzymatic Baeyer-Villiger Catalysis: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION

The Substrate-Bound Crystal Structure of a Baeyer–Villiger Monooxygenase Exhibits a Criegee-like Conformation

Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis

Finding the switch: turning a baeyer-villiger monooxygenase into a NADPH oxidase

Einwirkung des Caro'schen Reagens auf Ketone

Microbial Baeyer-Villiger oxidation: stereopreference and substrate acceptance of cyclohexanone monooxygenase mutants prepared by directed evolution.

Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis.

One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution.

P304

1627-1638

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/CBIC.201700223

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Uwe T. Bornscheuer

P577

2017-05-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28504873

http://www.w3.org/2001/XMLSchema#string

Controlling the Regioselectivity of Baeyer-Villiger Monooxygenases by Mutation of Active-Site Residues.

about

P2860

P2860

Controlling the Regioselectivity of Baeyer-Villiger Monooxygenases by Mutation of Active-Site Residues.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698