The Structure of a Retinal-Forming Carotenoid Oxygenase

  title={The Structure of a Retinal-Forming Carotenoid Oxygenase},
  author={Daniel P. Kloer and Sandra Ruch and Salim Al‐Babili and Peter Beyer and Georg E. Schulz},
  pages={267 - 269}
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed β-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this… 
Structural and biological aspects of carotenoid cleavage
This review will focus on the biochemistry of carotenoid oxygenases and the structural determinants of the cleavage reaction, showing how substrate specificity is achieved.
Utilization of Dioxygen by Carotenoid Cleavage Oxygenases*♦
It is demonstrated that bovine RPE65 is not dependent on O2 for its cleavage/isomerase activity and that dioxygenase activity is a feature common among double bond-cleaving CCOs.
Structural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs).
  • A. Daruwalla, P. Kiser
  • Chemistry, Biology
    Biochimica et biophysica acta. Molecular and cell biology of lipids
  • 2019
The Biochemical Basis of Vitamin A Production from the Asymmetric Carotenoid β-Cryptoxanthin.
Vitamin A serves essential functions in mammalian biology as a signaling molecule and chromophore. This lipid can be synthesized from more than 50 putative dietary provitamin A precursor molecules
Structural basis of carotenoid cleavage: from bacteria to mammals.
Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center.
A comprehensive structural and spectroscopic study of three phyletically diverse CCOs provides a robust description of the CCO iron center and its interactions with substrates and substrate mimetics that illuminates commonalities as well as subtle and profound structural differences within the C CO family.
Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase
Analysis of a metazoan-like archaeal CCD from Candidatus Nitrosotalea devanaterra revealed an enzyme, closely related to animal CCDs, that could be isolated in complex with its apocarotenoid product, and revealed the precise molecular interactions governing the enzyme’s unique regioselectivity.
Reaction mechanism of apocarotenoid oxygenase (ACO): a DFT study.
The results suggest that binding of dioxygen to the ferrous ion in the active site promotes one-electron oxidation of carotenoid leading to a substrate radical cation and a Fe-bound superoxide radical.


The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution.
The structure of the enzyme from Alicyclobacillus acidocaldarius has been determined and the membrane-binding interactions of which are described and compared with those of two prostaglandin-H2 synthase isoenzymes, the only other structurally characterized proteins of this type.
Oxidative cleavage of carotenoids catalyzed by enzyme models and beta-carotene 15,15´-monooxygenase
The substrate specificity was investigated, and the reaction mechanism elucidated incubating α-carotene in the presence of highly enriched 17O2 and H218O, which mimics the regiospecific enzymatic cleavage of carotenoids.
Specific oxidative cleavage of carotenoids by VP14 of maize.
A new ABA-deficient mutant of maize has been identified and the corresponding gene, Vp14, has been cloned and the recombinant VP14 protein catalyzes the cleavage of 9-cis-epoxy-carotenoids to form C25 apo-aldehydes and xanthoxin, a precursor of ABA in higher plants.
Identification and Characterization of a Mammalian Enzyme Catalyzing the Asymmetric Oxidative Cleavage of Provitamin A*
In vertebrates both symmetric and asymmetric cleavage pathways exist for carotenes, revealing a greater complexity of carotene metabolism.
The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
The first structure of a mammalian 15-lipoxygenase is reported, comprising a catalytic domain and a previously unrecognized β-barrel domain, which provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.
Characterization of a Novel Carotenoid Cleavage Dioxygenase from Plants*
The characterization of these activities offers the potential to synthesize a variety of interesting, natural products and is the first step in determining the function of this gene family in plants.
Oxidative remodeling of plastid carotenoids.
Cloning and Expression of ,-Carotene 15,15'-Dioxygenase
In the present study, it was possible to enrich the chicken beta,beta-carotene 15,15'-dioxygenase to such an extent that partial amino acid sequence information could be obtained to design degenerate oligonucleotides.
Identification, Expression, and Substrate Specificity of a Mammalian β-Carotene 15,15′-Dioxygenase*
We have identified from mouse the first mammalian β-carotene 15,15′-dioxygenase (β-CD), a crucial enzyme in development and metabolism that governs the de novo entry of vitamin A from plant-derived