Evidence map›Paper›PMID 27143479›Full record

ArticleThe Journal of biological chemistry2016

Substrate Specificity of Purified Recombinant Chicken β-Carotene 9',10'-Oxygenase (BCO2).

Carlo Dela Seña, Jian Sun, Sureshbabu Narayanasamy, Kenneth M Riedl, Yan Yuan, Robert W Curley, Steven J Schwartz, Earl H Harrison

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 81 citations in OpenAlex.

  1. Trial
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  4. Review
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  8. Article
  9. Absorption characteristics andRSC advances · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Carotenoid enrichment in eggs: From biochemistry perspective.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2023
    Review
  16. Article
  17. Article
  18. Review
  19. Review
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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

8 authors at 1 institution in 1 country.

Carlo Dela SeñaFrom the Department of Human Nutrition, Ohio State Biochemistry Program.
Jian SunFrom the Department of Human Nutrition.
Sureshbabu NarayanasamyFrom the Department of Human Nutrition.
Kenneth M RiedlDepartment of Food Science and Technology, and.
Yan YuanFrom the Department of Human Nutrition.
Robert W CurleyOhio State Biochemistry Program, College of Pharmacy, The Ohio State University, Columbus, Ohio 43210.
Steven J SchwartzDepartment of Food Science and Technology, and.
Earl H HarrisonFrom the Department of Human Nutrition, Ohio State Biochemistry Program, harrison.304@osu.edu.
The Ohio State University · US

Funding

DIETARY CAROTENOIDS--TRANSPORT IN HUMAN PLASMAR01HL049879 · NHLBI · U.S. DEPARTMENT OF AGRICULTURE · PI HARRISON, EARL HOWARD · 1994 to 2013
$2.5M
Vitamin A Homeostasis: Retinyl Ester StoresR01DK101251 · NIDDK · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI BLANER, WILLIAM S, HARRISON, EARL HOWARD · 2016 to 2018
$1.4M
NHLBI NIH HHS R01 HL049879NIDDK NIH HHS R01 DK101251
6 · The paper itself

Abstract

Provitamin A carotenoids are oxidatively cleaved by β-carotene 15,15'-dioxygenase (BCO1) at the central 15-15' double bond to form retinal (vitamin A aldehyde). Another carotenoid oxygenase, β-carotene 9',10'-oxygenase (BCO2) catalyzes the oxidative cleavage of carotenoids at the 9'-10' bond to yield an ionone and an apo-10'-carotenoid. Previously published substrate specificity studies of BCO2 were conducted using crude lysates from bacteria or insect cells expressing recombinant BCO2. Our attempts to obtain active recombinant human BCO2 expressed in Escherichia coli were unsuccessful. We have expressed recombinant chicken BCO2 in the strain E. coli BL21-Gold (DE3) and purified the enzyme by cobalt ion affinity chromatography. Like BCO1, purified recombinant chicken BCO2 catalyzes the oxidative cleavage of the provitamin A carotenoids β-carotene, α-carotene, and β-cryptoxanthin. Its catalytic activity with β-carotene as substrate is at least 10-fold lower than that of BCO1. In further contrast to BCO1, purified recombinant chicken BCO2 also catalyzes the oxidative cleavage of 9-cis-β-carotene and the non-provitamin A carotenoids zeaxanthin and lutein, and is inactive with all-trans-lycopene and β-apocarotenoids. Apo-10'-carotenoids were detected as enzymatic products by HPLC, and the identities were confirmed by LC-MS. Small amounts of 3-hydroxy-β-apo-8'-carotenal were also consistently detected in BCO2-β-cryptoxanthin reaction mixtures. With the exception of this activity with β-cryptoxanthin, BCO2 cleaves specifically at the 9'-10' bond to produce apo-10'-carotenoids. BCO2 has been shown to function in preventing the excessive accumulation of carotenoids, and its broad substrate specificity is consistent with this.

Indexed as

Amino Acid SequenceAnimalsbeta CaroteneCarotenoidsChickensCryptoxanthinsDioxygenasesHumansRecombinant ProteinsSequence AlignmentSubstrate Specificityalpha-caroteneBCO2 protein, humanbeta-apo-8'-carotenalbeta CaroteneCarotenoidsCryptoxanthinsDioxygenasesRecombinant Proteinscarotenoiddioxygenaseenzymeenzyme purificationlipid metabolismrecombinant protein expressionretinoid

Identifiers

PMID27143479
PMCPMC4938182
OpenAlexW2345426343

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.