Engineering towards nitroreductase functionality in ene-reductase scaffolds.

Item

http://www.wikidata.org/entity/Q41378518

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Engineering towards nitroreductase functionality in ene-reductase scaffolds.

@en

type

Item

label

Engineering towards nitroreductase functionality in ene-reductase scaffolds.

@en

prefLabel

Engineering towards nitroreductase functionality in ene-reductase scaffolds.

@en

P1476

Engineering towards nitroreductase functionality in ene-reductase scaffolds.

@en

P2093

Andreas S Bommarius

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

Jonathan T Park

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

Lizzette M Gómez Ramos

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

P2860

12-Oxophytodienoate-10,11-reductase: occurrence of two isoenzymes of different specificity against stereoisomers of 12-oxophytodienoic acid

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme

Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution

The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution

Structures of nitroreductase in three states: effects of inhibitor binding and reduction

Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme

Cysteine as a modulator residue in the active site of xenobiotic reductase A: a structural, thermodynamic and kinetic study

A site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivity

The Structure of Glycerol Trinitrate Reductase NerA fromAgrobacterium radiobacterReveals the Molecular Reason for Nitro- and Ene-Reductase Activity in OYE Homologues

P304

811-818

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

P31

scholarly article

P356

10.1002/CBIC.201402667

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

P433

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

P478

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

P577

2015-02-20T00:00:00Z

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

P698

25703443

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