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Structural studies on human 2-oxoglutarate dependent oxygenases.

Michael A McDonough¹, Christoph Loenarz, Rasheduzzaman Chowdhury

¹Chemistry Research Laboratory and the Oxford Centre for Integrative Systems Biology, University of Oxford, Oxford OX1 3TA, UK.

Current Opinion in Structural Biology

|October 5, 2010

Summary

Human enzymes called 2-oxoglutarate and ferrous iron-dependent oxygenases catalyze key reactions. Structural studies reveal their conserved core fold and variable substrate binding, crucial for various biological processes.

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Published on: February 24, 2018

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

2-Oxoglutarate and ferrous iron-dependent oxygenases are vital human enzymes.
They catalyze hydroxylation and demethylation reactions involving diverse substrates like proteins, nucleic acids, and lipids.
These enzymes are critical for collagen synthesis, gene expression, and lipid metabolism.

Purpose of the Study:

To elucidate the structural characteristics of 2-oxoglutarate and ferrous iron-dependent oxygenases.
To understand the conserved mechanisms of co-substrate binding and iron coordination.
To explore the variability in substrate-binding elements.

Main Methods:

Primarily employed crystallographic structural analyses.
Investigated the conserved double-stranded β-helix core fold.
Analyzed the conserved iron-binding residues and the 2-oxoglutarate co-substrate binding site.

Main Results:

All studied oxygenases share a conserved double-stranded β-helix core fold.
A highly conserved triad of iron-binding residues was identified.
The 2-oxoglutarate co-substrate binding site is less conserved, with bidentate binding to iron.
Primary substrate binding elements show variability and can involve mobile elements.

Conclusions:

The conserved structural core facilitates essential enzymatic functions across this enzyme family.
Variability in substrate-binding regions allows for diverse substrate interactions.
Understanding these structural features is key to comprehending their biological roles.