Evidence map›Paper›PMID 23601642›Full record

ArticleChemistry & biology2013

Free glycine accelerates the autoproteolytic activation of human asparaginase.

Ying Su, Christos S Karamitros, Julian Nomme, Theresa McSorley, Manfred Konrad, Arnon Lavie

Abstract read
In one paragraph

Article in Chemistry & biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Towards a dependable data set of structures for L-asparaginase research.Acta crystallographica. Section D, Structural biology · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Highly Active Thermophilic L-Asparaginase fromInternational journal of molecular sciences · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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 2 countries.

Ying SuDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.
Christos S Karamitros
Julian Nomme
Theresa McSorley
Manfred Konrad
Arnon Lavie
Max Planck Society · DEUniversity of Illinois Chicago · US

Funding

Enzyme-delivery scaffold technology for targeted cancer killing.R21CA155424 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI KAY, BRIAN KENNETH, LAVIE, ARNON · 2011 to 2013
$649k
NCI NIH HHS R21 CA155424
6 · The paper itself

Abstract

Human asparaginase 3 (hASNase3), which belongs to the N-terminal nucleophile hydrolase superfamily, is synthesized as a single polypeptide that is devoid of asparaginase activity. Intramolecular autoproteolytic processing releases the amino group of Thr168, a moiety required for catalyzing asparagine hydrolysis. Recombinant hASNase3 purifies as the uncleaved, asparaginase-inactive form and undergoes self-cleavage to the active form at a very slow rate. Here, we show that the free amino acid glycine selectively acts to accelerate hASNase3 cleavage both in vitro and in human cells. Other small amino acids such as alanine, serine, or the substrate asparagine are not capable of promoting autoproteolysis. Crystal structures of hASNase3 in complex with glycine in the uncleaved and cleaved enzyme states reveal the mechanism of glycine-accelerated posttranslational processing and explain why no other amino acid can substitute for glycine.

Indexed as

AsparaginaseAsparagineBiocatalysisCrystallography, X-RayGlycineHEK293 CellsHumansHydrogen-Ion ConcentrationHydrolysisMolecular Dynamics SimulationProtein Structure, TertiaryRecombinant ProteinsSubstrate SpecificityAsparaginaseAsparagineGlycineRecombinant Proteins

Identifiers

PMID23601642
PMCPMC3633088
OpenAlexW2033250937

What OpenQuestion holds

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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.