ArticleMethods in enzymology2022
Preparation of carotenoid cleavage dioxygenases for X-ray crystallography.
Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 4 citations in OpenAlex.
- Characterisation of a phylogenetically distinct PL25 family ulvan lyase from a seaweed biomass enriched metagenome.The FEBS journal · 2026Article
- Spectroscopy and crystallography define carotenoid oxygenases as a new subclass of mononuclear non-heme FeThe Journal of biological chemistry · 2025Article
- Carotenoid cleavage enzymes evolved convergently to generate the visual chromophore.Nature chemical biology · 2024Article
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3 authors at 2 institutions in 1 country.
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Abstract
Carotenoid cleavage dioxygenases (CCDs) constitute a superfamily of enzymes that are found in all domains of life where they play key roles in the metabolism of carotenoids and apocarotenoids as well as certain phenylpropanoids such as resveratrol. Interest in these enzymes stems not only from their biological importance but also from their remarkable catalytic properties including their regioselectivity, their ability to accommodate diverse substrates, and the additional activities (e.g., isomerase) that some of these enzyme possess. X-ray crystallography is a key experimental approach that has allowed detailed investigation into the structural basis behind the interesting biochemical features of these enzymes. Here, we describe approaches used by our lab that have proven successful in generating single crystals of these enzymes in resting or ligand-bound states for high-resolution X-ray diffraction analysis.
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