An Active Site Tyr Residue Guides the Regioselectivity of Lysine Hydroxylation by Nonheme Iron Lysine-4-hydroxylase Enzymes through Proton-Coupled Electron Transfer-Reference-Cited by-同舟云学术

An Active Site Tyr Residue Guides the Regioselectivity of Lysine Hydroxylation by Nonheme Iron Lysine-4-hydroxylase Enzymes through Proton-Coupled Electron Transfer

Published:2024-04-18 Issue:17 Volume:146 Page:11726-11739
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Cao Yuanxin¹²,Hay Sam¹²^ORCID,de Visser Sam P.¹³^ORCID

Affiliation:

1. Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom

2. Department of Chemistry, The University of Manchester, Oxford Road, Manchester M13 9PL, United Kingdom

3. Department of Chemical Engineering, The University of Manchester, Oxford Road, Manchester M13 9PL, United Kingdom

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.3c14574

Reference127 articles.

1. Development of a High-Throughput Lysyl Hydroxylase (LH) Assay and Identification of Small-Molecule Inhibitors against LH2

2. Deficiency of lysyl hydroxylase 2 in mice causes systemic endoplasmic reticulum stress leading to early embryonic lethality

3. Lysyl hydroxylase 1 (LH1) deficiency promotes angiotensin II (Ang II)-induced dissecting abdominal aortic aneurysm

4. Lysyl hydroxylases are transcription targets for GATA3 driving lung cancer cell metastasis

5. Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase Family: Novel Prognostic Biomarkers and Tumor Microenvironment Regulators for Lower-Grade Glioma

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