Evidence map›Paper›PMID 39651260›Full record

ArticlebioRxiv : the preprint server for biology2024

Structural Basis for Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum.

Santhosh Gatreddi, Julian Urdiain-Arraiza, Benoit Desguin, Robert P Hausinger, Jian Hu

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Santhosh GatreddiDepartment of Microbiology, Genetics, and Immunology, Michigan State University, MI 48824.
Julian Urdiain-ArraizaLouvain Institute of Biomolecular Science and Technology (LIBST), Université catholique de Louvain, B-1348 Louvain-La-Neuve, Belgium.
Benoit DesguinLouvain Institute of Biomolecular Science and Technology (LIBST), Université catholique de Louvain, B-1348 Louvain-La-Neuve, Belgium.
Robert P HausingerDepartment of Microbiology, Genetics, and Immunology, Michigan State University, MI 48824.
Jian HuDepartment of Biochemistry and Molecular Biology, Michigan State University, MI 48824.

Funding

Nickel-pincer nucleotide enzymesR01GM128959 · NIGMS · MICHIGAN STATE UNIVERSITY · PI ROBERT P HAUSINGER · 2019 to 2026
$2.7M
Transport, substrate specificity and regulation mechanisms of the ZIP transition metal transportersR35GM140931 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HU, JIAN · 2021 to 2025
$1.7M
NIGMS NIH HHS R01 GM128959NIGMS NIH HHS R35 GM140931
6 · The paper itself

Abstract

The LarA family consists of diverse racemases/epimerases that interconvert the diastereomers of a variety of α-hydroxyacids by using a nickel-pincer nucleotide (NPN) cofactor. The hidden redox reaction catalyzed by the NPN cofactor makes LarA enzymes attractive engineering targets for applications. However, how a LarA enzyme binds its natural substrate and recognizes different α-hydroxyacids has not been elucidated. Here, we report three high-resolution structures of the enzyme-substrate complexes of a broad-spectrum LarA enzyme from

Identifiers

PMID39651260
PMCPMC11623692

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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.