Stepwise O-Atom Transfer in Heme-Based Tryptophan Dioxygenase: Role of Substrate Ammonium in Epoxide Ring Opening.

about

Stepwise O-Atom Transfer in Heme-Based Tryptophan Dioxygenase: Role of Substrate Ammonium in Epoxide Ring Opening.

Item

http://www.wikidata.org/entity/Q53839714

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh

2018年學術文章

@zh-hant

name

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@en

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@nl

type

Item

label

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@en

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@nl

prefLabel

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@en

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@nl

P1476

Stepwise O-Atom Transfer in He ...... onium in Epoxide Ring Opening.

@en

P2093

Amanda C Maldonado

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

Brett R Ambler

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

Inchul Shin

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

Wendell P Griffith

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

P2860

Targeting amino acid metabolism in cancer growth and anti-tumor immune response

Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase

The ternary complex of PrnB (the second enzyme in the pyrrolnitrin biosynthesis pathway), tryptophan, and cyanide yields new mechanistic insights into the indolamine dioxygenase superfamily

Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase

Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase

Tryptophan-2,3-dioxygenase (TDO) inhibition ameliorates neurodegeneration by modulation of kynurenine pathway metabolites

EPR and Mössbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase.

Heme-Containing Oxygenases.

Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics.

Endogenous kynurenines as targets for drug discovery and development.

P304

4372-4379

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

P31

scholarly article

P356

10.1021/JACS.8B00262

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

P407

English

P433

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

P478

140

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

P50

Aimin Liu

Ryan A. Altman

Daniel J Wherritt

P577

2018-03-15T00:00:00Z

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

P698

29506384

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

P932

5874177

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