Plasmodium parasites have repurposed the heme oxygenase scaffold from its canonical heme-degrading function to fulfill an essential and adaptive role in gene expression within the apicoplast organelle.

Cysteine dioxygenase, a conserved and critical enzyme in sulfur amino acid metabolism, is activated by the hypoxia-inducible transcription factor.

The lack of haem biosynthetic and degradative pathways in ticks offers new strategies to combat these parasites.

2-Oxoglutarate and Fe(II)-dependent dioxygenases from clade C23 are the major source of guanidine in plants and release guanidine from arginine or homoarginine by C5 or C6 hydroxylation, respectively.

By increasing intracellular cysteine levels, NRF2 engages a tumor suppressive metabolic pathway mediated by cysteine dioxygenase 1.

Assays using recombinant HIF prolyl hydroxylases did not support hydroxylation of more than 20 reported non-HIF substrates under conditions where robust HIF hydroxylation was observed.

Multi-omics reveals that Alkb homolog 7 (ALKBH7), α mitochondrial alpha-ketoglutarate dioxygenase of unclear function, regulates glyoxal metabolism, which may explain its role in necrosis and heart attack.

The protein uS12/Rps23 functions extra-ribosomally to control oxygen homeostasis in fission yeast.

Elucidating the 1-naphthylamine degradation pathway in Pseudomonas sp. strain JS3066 and analyzing the catalytic mechanism of the 1-naphthylamine glutamine synthetase deepens the understanding of microbial degradation of polycyclic aromatic amines.

Cells rely on prolyl hydroxylase enzymes to sense low levels of oxygen, but they might act on fewer targets than previously thought.