Evidence map›Paper›PMID 33275413›Full record

ArticleACS chemical biology2020

Conformational Dynamics Contribute to Substrate Selectivity and Catalysis in Human Kynureninase.

Christos S Karamitros, Kyle Murray, Yusuke Sugiyama, Yoichi Kumada, Kenneth A Johnson, George Georgiou, Sheena D'Arcy, Everett M Stone

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.2field-weighted citation impact, top 56% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. 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

8 authors at 4 institutions in 2 countries.

Christos S KaramitrosDepartment of Chemical Engineering, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0002-1393-3083
Kyle MurrayDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, Richardson, Texas 75080, United States.
Yusuke SugiyamaDepartment of Molecular Chemistry and Engineering, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Japan.
Yoichi KumadaDepartment of Molecular Chemistry and Engineering, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Japan.
Kenneth A JohnsonDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, United States.
George GeorgiouDepartment of Chemical Engineering, The University of Texas at Austin, Austin, Texas 78712, United States.
Sheena D'ArcyDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, Richardson, Texas 75080, United States.ORCID 0000-0001-5055-988X
Everett M StoneDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0002-2459-9762
Kyoto Institute of Technology · JPLivestrong Foundation · USThe University of Texas at Austin · USThe University of Texas at Dallas · US

Funding

The Role of Dynamics in Regulating Multi-Activity Protein Complexes and ChromatinR35GM133751 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Sheena D'Arcy · 2019 to 2026
$2.9M
NIGMS NIH HHS R35 GM133751
6 · The paper itself

Abstract

Kynureninases (KYNases) are enzymes that play a key role in tryptophan catabolism through the degradation of intermediate kynurenine and 3'-hydroxy-kynurenine metabolites (KYN and OH-KYN, respectively). Bacterial KYNases exhibit high catalytic efficiency toward KYN and moderate activity toward OH-KYN, whereas animal KYNases are highly selective for OH-KYN, exhibiting only minimal activity toward the smaller KYN substrate. These differences reflect divergent pathways for KYN and OH-KYN utilization in the respective kingdoms. We examined the

Indexed as

CatalysisHumansHydrolasesKineticsProtein ConformationSubstrate SpecificityHydrolaseskynureninase

Identifiers

PMID33275413
PMCPMC11104311
OpenAlexW3109332997

What OpenQuestion holds

Textmetadata
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.