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Phenylalanine meta‐Hydroxylase: A Single Residue Mediates Mechanistic Control of Aromatic Amino Acid Hydroxylation

Autor: Rebecca J. M. Goss, Joanna C. Sadler, Sabine Grüschow, Peter Sharratt

Publikováno v: Chembiochem
Grüschow, S, Sadler, J C, Sharratt, P J & Goss, R J M 2019, ' Phenylalanine meta-hydroxylase : A single residue mediates mechanistic control of aromatic amino acid hydroxylation ', ChemBioChem, vol. 21 . https://doi.org/10.1002/cbic.201900320

The rare nonproteinogenic amino acid, meta‐l‐tyrosine is biosynthetically intriguing. Whilst the biogenesis of tyrosine from phenylalanine is well characterised, the mechanistic basis for meta‐hydroxylation is unknown. Herein, we report the ana

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6406aa5503c29840328c2fb09a709bb
http://europepmc.org/articles/PMC7027792

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Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases

Autor: Adrie H. Westphal, Willem J. H. van Berkel, Dirk Tischler

Publikováno v: Archives of Biochemistry and Biophysics 702 (2021)
Archives of Biochemistry and Biophysics, 702

4-Hydroxybenzoate 3-hydroxylase (PHBH) is the most extensively studied group A flavoprotein monooxygenase (FPMO). PHBH is almost exclusively found in prokaryotes, where its induction, usually as a consequence of lignin degradation, results in the reg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2428a30690b0e37927cb49f588175dfe
https://pubmed.ncbi.nlm.nih.gov/33684360

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The molecular basis for the intramolecular migration (NIH shift) of the carboxyl group duringpara-hydroxybenzoate catabolism

Autor: Jim C. Spain, Ying Xu, Huan Zhao, Ning-Yi Zhou, Shuangjun Lin

Publikováno v: Molecular Microbiology. 110:411-424

The NIH shift is a chemical rearrangement in which a substituent on an aromatic ring undergoes an intramolecular migration, primarily during an enzymatic hydroxylation reaction. The molecular mechanism for the NIH shift of a carboxyl group has remain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f8ae23651e7f52a32f407e64ba3e6d9
https://doi.org/10.1111/mmi.14094

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Frequent occurrence of triclosan hydroxylation in mammals: A combined theoretical and experimental investigation

Autor: Zongwei Cai, Lin Zhu, Guodong Zhang, Katherine Z. Sanidad, Hongna Zhang, Thomas D. Haggerty, Julie Parsonnet

Publikováno v: Journal of Hazardous Materials. 407:124803

Triclosan (TCS) is a widespread antimicrobial agent with many adverse health risks. Its hepatoxicity invariably points to the activation of constitutive androstane receptor (CAR), which regulates cytochrome P450 (CYP) genes that are critical for oxid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e7db6f07757214cdd37a1bf3f1fe3ac
https://doi.org/10.1016/j.jhazmat.2020.124803

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Mechanistic Studies of TiO2Photocatalysis and Fenton Degradation of Hydrophobic Aromatic Pollutants in Water

Autor: Yuanzheng Gong, Chun Yang, Chuncheng Chen, Wanhong Ma, Jincai Zhao, Hongwei Ji

Publikováno v: Chemistry - An Asian Journal. 11:3568-3574

HO-adduct radicals have been investigated and confirmed as the common initial intermediates in TiO2 photocatalysis and Fenton degradations of water-insoluble aromatics. However, the evolution of HO-adduct radicals to phenols has not been completely c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5c8b583bc7182ab4a959736f07f21b69
https://doi.org/10.1002/asia.201601299

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Substrate Hydroxylation by the Oxido–Iron Intermediate in Aromatic Amino Acid Hydroxylases: A DFT Mechanistic Study

Autor: Elaine Olsson, Aurora Martinez, Knut Teigen, Vidar R. Jensen

Publikováno v: European Journal of Inorganic Chemistry. 2011:2720-2732

Substrate hydroxylation by an FeIV=O cluster model of the active center in aromatic amino acid hydroxylases (AAHs) has been investigated by means of DFT calculations. Whereas benzene was used as a model for the aromatic amino acid substrate, the wate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6222acbd9531925c9607eaaad76bae89
https://doi.org/10.1002/ejic.201001218

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