Evidence map›Paper›PMID 22869039›Full record

ReviewCellular and molecular life sciences : CMLS2013

Structure and function of biotin-dependent carboxylases.

Liang Tong

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 211 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
211citing papers in PubMed, 2 pooled it
7.9field-weighted citation impact, top 2% 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

211 citing papers in PubMed, 2 syntheses or guidelines pooled it, 445 citations in OpenAlex.

  1. Pooled it
  2. The Surfactin-Like Lipopeptides FromFrontiers in bioengineering and biotechnology · 2021
    Pooled it
  3. Trial
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Exploring the Link Between Biotin Metabolism andPathogens (Basel, Switzerland) · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

151 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Liang TongDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA. ltong@columbia.edu
Columbia University · US

Funding

Structural biology of enzymes in fatty acid metabolismR01DK067238 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2004 to 2012
$2.6M
NIDDK NIH HHS DK067238NIDDK NIH HHS R01 DK067238
6 · The paper itself

Abstract

Biotin-dependent carboxylases include acetyl-CoA carboxylase (ACC), propionyl-CoA carboxylase (PCC), 3-methylcrotonyl-CoA carboxylase (MCC), geranyl-CoA carboxylase, pyruvate carboxylase (PC), and urea carboxylase (UC). They contain biotin carboxylase (BC), carboxyltransferase (CT), and biotin-carboxyl carrier protein components. These enzymes are widely distributed in nature and have important functions in fatty acid metabolism, amino acid metabolism, carbohydrate metabolism, polyketide biosynthesis, urea utilization, and other cellular processes. ACCs are also attractive targets for drug discovery against type 2 diabetes, obesity, cancer, microbial infections, and other diseases, and the plastid ACC of grasses is the target of action of three classes of commercial herbicides. Deficiencies in the activities of PCC, MCC, or PC are linked to serious diseases in humans. Our understanding of these enzymes has been greatly enhanced over the past few years by the crystal structures of the holoenzymes of PCC, MCC, PC, and UC. The structures reveal unanticipated features in the architectures of the holoenzymes, including the presence of previously unrecognized domains, and provide a molecular basis for understanding their catalytic mechanism as well as the large collection of disease-causing mutations in PCC, MCC, and PC. This review will summarize the recent advances in our knowledge on the structure and function of these important metabolic enzymes.

Indexed as

Acetyl-CoA CarboxylaseAnimalsBiotinCarbon-Carbon LigasesCarbon-Nitrogen LigasesFatty Acid Synthase, Type IIHumansMethylmalonyl-CoA DecarboxylaseModels, MolecularProtein ConformationPyruvate CarboxylaseAcetyl-CoA CarboxylaseBiotinbiotin carboxylasebiotin carboxyl carrier proteinCarbon-Carbon LigasesCarbon-Nitrogen LigasesFatty Acid Synthase, Type IIgeranoyl-CoA carboxylasemethylcrotonoyl-CoA carboxylaseMethylmalonyl-CoA DecarboxylasePyruvate Carboxylaseurea carboxylase (hydrolyzing)

Identifiers

PMID22869039
PMCPMC3508090
OpenAlexW2107345961

What OpenQuestion holds

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LicenceTDM
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.