The mechanism of formation of N-formylkynurenine by heme dioxygenases. - Wikidata - wikimedia - TriplyDB

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

http://www.wikidata.org/entity/Q34213607

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Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase Alkene cleavage catalysed by heme and nonheme enzymes: reaction mechanisms and biocatalytic applications.The role of placental tryptophan catabolism Heme enzyme structure and function.Substrate Oxidation by Indoleamine 2,3-Dioxygenase: EVIDENCE FOR A COMMON REACTION MECHANISM Formation of an N-formylkynurenine-derived fluorophore and its use for measuring indoleamine 2,3-dioxygenase 1 activity.Complete reaction mechanism of indoleamine 2,3-dioxygenase as revealed by QM/MM simulations.Indole peroxygenase activity of indoleamine 2,3-dioxygenase Human indoleamine 2,3-dioxygenase is a catalyst of physiological heme peroxidase reactions: implications for the inhibition of dioxygenase activity by hydrogen peroxide.Tryptophan oxygenation: mechanistic considerations.Heme-containing enzymes and inhibitors for tryptophan metabolism.Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: 18O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN.N (1)-Fluoroalkyltryptophan Analogues: Synthesis and in vitro Study as Potential Substrates for Indoleamine 2,3-Dioxygenase.Rate-Determining Attack on Substrate Precedes Rieske Cluster Oxidation during Cis-Dihydroxylation by Benzoate Dioxygenase A short history of heme dioxygenases: rise, fall and rise again.Facile access to chiral ketones through metal-free oxidative C-C bond cleavage of aldehydes by O2.Benzofuranquinones as inhibitors of indoleamine 2,3-dioxygenase (IDO). Synthesis and biological evaluation.Tandem mass spectrometry and infrared spectroscopy as a tool to identify peptide oxidized residues.Stepwise O-Atom Transfer in Heme-Based Tryptophan Dioxygenase: Role of Substrate Ammonium in Epoxide Ring Opening.Immune-modulating enzyme indoleamine 2,3-dioxygenase is effectively inhibited by targeting its apo-form.

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P2860

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

http://www.wikidata.org/entity/Q34213607

description

2011 nî lūn-bûn

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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

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name

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@ast

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@en

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

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type

label

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@ast

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@en

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@nl

prefLabel

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@ast

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@en

The mechanism of formation of N-formylkynurenine by heme dioxygenases.

@nl

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Journal of the American Chemical Society

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The mechanism of formation of N-formylkynurenine by heme dioxygenases

@en

P2093

Christopher G Mowat

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

Gerry A Griffith

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

Graham Eaton

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

Igor Efimov

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

Jaswir Basran

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

Nishma Chauhan

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

Sarah J Thackray

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

P2860

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

Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding

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

The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions

1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase

Rational design of indoleamine 2,3-dioxygenase inhibitors.

Heme-Containing Oxygenases.

Structure and reaction mechanism in the heme dioxygenases.

Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes.

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10.1021/JA207066Z

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