Evidence map›Paper›PMID 15329673›Full record

ArticleThe EMBO journal2004

Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit.

Pamela R Hall, Run Zheng, Lizamma Antony, Marianne Pusztai-Carey, Paul R Carey, Vivien C Yee

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Structural Characterization of Multienzyme Assemblies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  3. Review
  4. Article
  5. Article
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  7. Article
  8. Article
  9. Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013
    Review
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  11. Article
  12. Article
  13. Article
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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

6 authors at 2 institutions in 1 country.

Pamela R HallDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH, USA.
Run Zheng
Lizamma Antony
Marianne Pusztai-Carey
Paul R Carey
Vivien C Yee
Case Western Reserve University · USJohns Hopkins University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN MOLECULAR THERAPEUTICST32GM008803 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI MIEYAL, JOHN J, NIEMAN, MARVIN THOMAS · 2001 to 2023
$4.2M
Transcarboxylase: Strucuture, Flexibility and MechanismR01DK053053 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI CAREY, PAUL R · 1997 to 2006
$1.6M
NIDDK NIH HHS DK053053NIDDK NIH HHS R01 DK053053NIGMS NIH HHS GM08803NIGMS NIH HHS T32 GM008803
6 · The paper itself

Abstract

Transcarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate to yield propionyl-CoA and oxaloacetate. Crystal structures of the 5S metalloenzyme subunit, which catalyzes the second carboxylation reaction, have been solved in free form and bound to its substrate pyruvate, product oxaloacetate, or inhibitor 2-ketobutyrate. The structure reveals a dimer of beta(8)alpha(8) barrels with an active site cobalt ion coordinated by a carbamylated lysine, except in the oxaloacetate complex in which the product's carboxylate group serves as a ligand instead. 5S and human pyruvate carboxylase (PC), an enzyme crucial to gluconeogenesis, catalyze similar reactions. A 5S-based homology model of the PC carboxyltransferase domain indicates a conserved mechanism and explains the molecular basis of mutations in lactic acidemia. PC disease mutations reproduced in 5S result in a similar decrease in carboxyltransferase activity and crystal structures with altered active sites.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesButyratesCarboxyl and Carbamoyl TransferasesCatalytic DomainCrystallography, X-RayEnzyme InhibitorsHumansMolecular Sequence DataMultienzyme ComplexesMutagenesis, Site-DirectedOxaloacetic AcidPropionibacteriumProtein BindingProtein Conformationalpha-ketobutyric acidBacterial ProteinsButyratesCarboxyl and Carbamoyl TransferasesEnzyme InhibitorsMethylmalonyl-CoA carboxytransferaseMultienzyme ComplexesOxaloacetic AcidProtein SubunitsPyruvate CarboxylasePyruvic Acid

Identifiers

PMID15329673
PMCPMC517613
OpenAlexW2159807514

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.