Evidence map›Paper›PMID 39300648›Full record

ArticleMethods in enzymology2024

Spectroscopic and computational studies of a bifunctional iron- and 2-oxoglutarate dependent enzyme, AsqJ.

Shan Xue, Yijie Tang, Igor V Kurnikov, Hsuan-Jen Liao, Jikun Li, Nei-Li Chan, Maria G Kurnikova, Wei-Chen Chang, Yisong Guo

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Article in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

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1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Shan XueDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, United States.
Yijie TangDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, United States.
Igor V KurnikovDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, United States.
Hsuan-Jen LiaoInstitute of Biochemistry and Molecular Biology, College of Medicine, National (Taiwan) University, Taipei, Taiwan.
Jikun LiDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, United States.
Nei-Li ChanInstitute of Biochemistry and Molecular Biology, College of Medicine, National (Taiwan) University, Taipei, Taiwan. Electronic address: nlchan@ntu.edu.tw.
Maria G KurnikovaDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, United States. Electronic address: kurnikova@cmu.edu.
Wei-Chen ChangDepartment of Chemistry, North Carolina State University, Raleigh, NC, United States. Electronic address: wchang6@ncsu.edu.
Yisong GuoDepartment of Chemistry, Carnegie Mellon University, Pittsburgh, PA, United States. Electronic address: ysguo@andrew.cmu.edu.

Funding

Elucidate Mechanisms of Quinolone Alkaloid Biosynthesis via Iron(II)/2-Oxoglutarate Dependent Enzymes: Diverse, but Controlled ReactivityR01GM125924 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI Yisong Guo · 2018 to 2026
$3.3M
NIGMS NIH HHS R01 GM125924
6 · The paper itself

Abstract

Iron and 2-oxoglutarate dependent (Fe/2OG) enzymes exhibit an exceedingly broad reaction repertoire. The most prevalent reactivity is hydroxylation, but many other reactivities have also been discovered in recent years, including halogenation, desaturation, epoxidation, endoperoxidation, epimerization, and cyclization. To fully explore the reaction mechanisms that support such a diverse reactivities in Fe/2OG enzyme, it is necessary to utilize a multi-faceted research methodology, consisting of molecular probe design and synthesis, in vitro enzyme assay development, enzyme kinetics, spectroscopy, protein crystallography, and theoretical calculations. By using such a multi-faceted research approach, we have explored reaction mechanisms of desaturation and epoxidation catalyzed by a bi-functional Fe/2OG enzyme, AsqJ. Herein, we describe the experimental protocols and computational workflows used in our studies.

Indexed as

IronKetoglutaric AcidsCrystallography, X-RayEnzyme AssaysHydroxylationKineticsModels, MolecularIronKetoglutaric AcidsDesaturationEpoxidationFerrylIron and 2-oxoglutarate dependent enzymesMolecular dynamicsMössbauerOxyferrylProtein crystallographyReaction mechanismTransient kinetics

Identifiers

PMID39300648
PMCPMC11415609

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