Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76. - Wikidata - wikimedia - TriplyDB

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

http://www.wikidata.org/entity/Q42515909

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Structure of the processive rubber oxygenase RoxA from Xanthomonas sp Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase EPR and Mössbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase.Structure and reaction mechanism in the heme dioxygenases.Heme enzyme structure and function.Evidence for a ferryl intermediate in a heme-based dioxygenase.Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase Molecular basis for the substrate stereoselectivity in tryptophan dioxygenase.Complete reaction mechanism of indoleamine 2,3-dioxygenase as revealed by QM/MM simulations.Substrate stereo-specificity in tryptophan dioxygenase and indoleamine 2,3-dioxygenase.Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable.The mechanism of substrate inhibition in human indoleamine 2,3-dioxygenase The first step of the dioxygenation reaction carried out by tryptophan dioxygenase and indoleamine 2,3-dioxygenase as revealed by quantum mechanical/molecular mechanical studies The modulation of enzyme indoleamine 2,3-dioxygenase from dendritic cells for the treatment of type 1 diabetes mellitus.Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopy Oxidative degradation of 2,6-dibromophenol using anion-exchange resin supported supramolecular catalysts of iron(III)-5,10,15,20-tetrakis (p-hydroxyphenyl)porphyrin bound to humic acid prepared via formaldehyde and urea-formaldehyde polycondensation

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Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

http://www.wikidata.org/entity/Q42515909

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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2009年學術文章

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name

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

@en

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

@nl

type

label

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

@en

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

@nl

prefLabel

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

@en

Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

@nl

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Journal of the American Chemical Society

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Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76.

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Dipanwita Batabyal

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Syun-Ru Yeh

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P2860

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

Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function

Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis

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

Structural determinants of the stretching frequency of CO bound to myoglobin

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

Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis

Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism

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

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3260-3270

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10.1021/JA807969A

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9

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131

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19209904

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4535339

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