Catalysis by the non-heme iron(II) histone demethylase PHF8 involves iron center rearrangement and conformational modulation of substrate orientation

Catalysis by the non-heme iron(II) histone demethylase PHF8 involves iron center rearrangement and conformational modulation of substrate orientation

PHF8 (KDM7B) is a human non-heme 2-oxoglutarate (2OG) JmjC domain oxygenase that catalyzes the demethylation of the di/mono-Nε-methylated K9 residue of histone H3. Altered PHF8 activity is linked to genetic diseases and cancer; thus, it is an interesting target for epigenetic modulation. We describe...

Descrizione completa

Dettagli Bibliografici
Autori principali:	Chaturvedi, SS, Ramanan, R, Lehnert, N, Schofield, CJ, Karabencheva-Christova, TG, Christov, CZ
Natura:	Journal article
Lingua:	English
Pubblicazione:	American Chemical Society 2019

Documenti analoghi

Catalysis by the JmjC histone demethylase KDM4A integrates substrate dynamics, correlated motions and molecular orbital control
di: Ramanan, R, et al.
Pubblicazione: (2020)

Dioxygen binding is controlled by the protein environment in non-heme FeII and 2-oxoglutarate oxygenases: a study on histone demethylase PHF8 and an ethylene-forming enzyme
di: Chaturvedi, SS, et al.
Pubblicazione: (2023)

Can second coordination sphere and long-range interactions modulate hydrogen atom transfer in a non-heme Fe(II)-dependent histone demethylase?
di: Chaturvedi, SS, et al.
Pubblicazione: (2022)

Role of structural dynamics in selectivity and mechanism of non-heme Fe(II) and 2-oxoglutarate-dependent oxygenases involved in DNA repair
di: Waheed, SO, et al.
Pubblicazione: (2020)

Conformational flexibility influences structure–function relationships in nucleic acid N-methyl demethylases
di: Waheed, SO, et al.
Pubblicazione: (2019)

Conformational dynamics underlies different functions of human KDM7 histone demethylases
di: Chaturvedi, S, et al.
Pubblicazione: (2019)

Role of Structural Dynamics in Selectivity and Mechanism of Non-heme Fe(II) and 2‑Oxoglutarate-Dependent Oxygenases Involved in DNA Repair
di: Sodiq O. Waheed, et al.
Pubblicazione: (2020-05-01)

The Histone Demethylase PHF8 Is Essential for Endothelial Cell Migration.
di: Lunda Gu, et al.
Pubblicazione: (2016-01-01)

Oncogenic features of PHF8 histone demethylase in esophageal squamous cell carcinoma.
di: Xiujing Sun, et al.
Pubblicazione: (2013-01-01)

What is the catalytic mechanism of enzymatic histone N-Methyl arginine demethylation and can it be influenced by an external electric field?
di: Ramanan, R, et al.
Pubblicazione: (2021)

What is the catalytic mechanism of enzymatic histone n-methyl arginine demethylation and can it be influenced by an external electric field?
di: Ramanan, R, et al.
Pubblicazione: (2021)

Development of homogeneous luminescence assays for histone demethylase catalysis and binding.
di: Kawamura, A, et al.
Pubblicazione: (2010)

Development of homogeneous luminescence assays for histone demethylase catalysis and binding.
di: Kawamura, A, et al.
Pubblicazione: (2010)

Histone Demethylase PHF8 Is Required for the Development of the Zebrafish Inner Ear and Posterior Lateral Line
di: Jing He, et al.
Pubblicazione: (2020-11-01)

Phf8 histone demethylase deficiency causes cognitive impairments through the mTOR pathway
di: Xuemei Chen, et al.
Pubblicazione: (2018-01-01)

The histone demethylase Phf2 acts as a molecular checkpoint to prevent NAFLD progression during obesity
di: Julien Bricambert, et al.
Pubblicazione: (2018-05-01)

Unusual catalytic strategy by non-heme Fe(ii)/2-oxoglutarate-dependent aspartyl hydroxylase AspH
di: Krishnan, A, et al.
Pubblicazione: (2024)

Recent progress in histone demethylase inhibitors
di: McAllister, T, et al.
Pubblicazione: (2016)

Commentary: The histone demethylase Phf2 acts as a molecular checkpoint to prevent NAFLD progression during obesity
di: Barbara Barbaro, et al.
Pubblicazione: (2018-10-01)

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase
di: Yue, W, et al.
Pubblicazione: (2010)

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase.
di: Yue, W, et al.
Pubblicazione: (2010)

The clinically used iron chelator deferasirox is an inhibitor of epigenetic jumonjiC domain-containing histone demethylases
di: Roatsch, M, et al.
Pubblicazione: (2019)

PHF8/KDM7B: A Versatile Histone Demethylase and Epigenetic Modifier in Nervous System Disease and Cancers
di: Tingyu Fan, et al.
Pubblicazione: (2024-09-01)

Structural and mechanistic enzymology : bringing together experiments and computations /
di: Christov, Christo, et al.
Pubblicazione: (2012)

Structure and mechanism guided identification of histone demethylase inhibitors
di: Schofield, C
Pubblicazione: (2010)

Mechanisms of human histone and nucleic acid demethylases
di: Walport, L, et al.
Pubblicazione: (2012)

Mechanisms of human histone and nucleic acid demethylases.
di: Walport, L, et al.
Pubblicazione: (2012)

Heme: The Lord of the Iron Ring
di: Vanessa Azevedo Voltarelli, et al.
Pubblicazione: (2023-05-01)

PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase.
di: Loenarz, C, et al.
Pubblicazione: (2010)

PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase.
di: Loenarz, C, et al.
Pubblicazione: (2010)

Targeting histone lysine demethylases - Progress, challenges, and the future.
di: Thinnes, C, et al.
Pubblicazione: (2014)

Histone demethylases in autophagy and inflammation
di: Yaoyao Ma, et al.
Pubblicazione: (2025-01-01)

A miniaturized screen for inhibitors of Jumonji histone demethylases.
di: Sakurai, M, et al.
Pubblicazione: (2010)

A miniaturized screen for inhibitors of Jumonji histone demethylases.
di: Sakurai, M, et al.
Pubblicazione: (2010)

Zn-ejection for the selective inhibition of JMJD2 histone demethylases
di: Sekirnik, R, et al.
Pubblicazione: (2012)

Iron Metabolism in the Disorders of Heme Biosynthesis
di: Andrea Ricci, et al.
Pubblicazione: (2022-08-01)

Terminally truncated isopenicillin N synthase generates a dithioester product: evidence for a thioaldehyde intermediate during catalysis and a new mode of reaction for non-heme iron oxidases
di: McNeill, LA, et al.
Pubblicazione: (2017)

Heme, A Metabolic Sensor, Directly Regulates the Activity of the KDM4 Histone Demethylase Family and Their Interactions with Partner Proteins
di: Purna Chaitanya Konduri, et al.
Pubblicazione: (2020-03-01)

Heme and non-heme iron transporters in non-polarized and polarized cells
di: Yasui Yumiko, et al.
Pubblicazione: (2010-06-01)

Like Iron in the Blood of the People: The Requirement for Heme Trafficking in Iron Metabolism
di: Iqbal eHamza, et al.
Pubblicazione: (2014-06-01)