Evidence map›Paper›PMID 23727499›Full record

ArticleArchives of biochemistry and biophysics2013

Characterization of human β,β-carotene-15,15'-monooxygenase (BCMO1) as a soluble monomeric enzyme.

Thomas Kowatz, Darwin Babino, Philip Kiser, Krzysztof Palczewski, Johannes von Lintig

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Carotenoid modifying enzymes in metazoans.Methods in enzymology · 2022
    Article
  9. Review
  10. Article
  11. Enzymology of vertebrate carotenoid oxygenases.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  12. Structural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs).Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  13. Carotenoid metabolism at the intestinal barrier.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  14. Article
  15. Food science and biotechnology · 2016
    Article
  16. Article
  17. Article
  18. Evidence for compartmentalization of mammalian carotenoid metabolism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Thomas KowatzDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Darwin Babino
Philip Kiser
Krzysztof Palczewski
Johannes von Lintig
Case Western Reserve University · US

Funding

STRUCTURAL STUDIES OF ARRESTINSR01EY009339 · NEI · UNIVERSITY OF WASHINGTON · PI KISER, PHILIP DAVID, PALCZEWSKI, KRZYSZTOF · 1992 to 2025
$16.0M
Carotinoids in VisionR01EY020551 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI VON LINTIG, JOHANNES FRIEDRICH · 2011 to 2024
$4.8M
NEI NIH HHS R01 EY009339NEI NIH HHS R01EY009339NEI NIH HHS R01 EY020551NEI NIH HHS R01EY020551
6 · The paper itself

Abstract

The formal first step in in vitamin A metabolism is the conversion of its natural precursor β,β-carotene (C40) to retinaldehyde (C20). This reaction is catalyzed by the enzyme β,β-carotene-15,15'-monooxygenase (BCMO1). BCMO1 has been cloned from several vertebrate species, including humans. However, knowledge about this protein's enzymatic and structural properties is scant. Here we expressed human BCMO1 in Spodoptera frugiperda 9 insect cells. Recombinant BCMO1 is a soluble protein that displayed Michaelis-Menten kinetics with a KM of 14 μM for β,β-carotene. Though addition of detergents failed to increase BCMO1 enzymatic activity, short chain aliphatic detergents such as C8E4 and C8E6 decreased enzymatic activity probably by interacting with the substrate binding site. Thus we purified BCMO1 in the absence of detergent. Purified BCMO1 was a monomeric enzymatically active soluble protein that did not require cofactors and displayed a turnover rate of about 8 molecules of β,β-carotene per second. The aqueous solubility of BCMO1 was confirmed in mouse liver and mammalian cells. Establishment of a protocol that yields highly active homogenous BCMO1 is an important step towards clarifying the lipophilic substrate interaction, reaction mechanism and structure of this vitamin A forming enzyme.

Indexed as

Animalsbeta-Carotene 15,15'-MonooxygenaseCell LineGene Expression Regulation, EnzymologicHumansLiverMiceRecombinant ProteinsRetinaldehydeSolubilitySpodopteraSubstrate SpecificityTransfectionVitamin ABCO1 protein, humanbeta-Carotene 15,15'-MonooxygenaseRecombinant ProteinsRetinaldehydeVitamin AAll-trans-retinalCytosolicNon-heme iron oxygenaseSymmetric carotenoid cleavageVitamin Aβ,β-Caroteneβ,β-Carotene-15,15′-monooxygenase

Identifiers

PMID23727499
PMCPMC3795993
OpenAlexW2159838461

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.