Evidence map›Paper›PMID 35209187›Full record

ArticleMolecules (Basel, Switzerland)2022

Using Steady-State Kinetics to Quantitate Substrate Selectivity and Specificity: A Case Study with Two Human Transaminases.

Alessio Peracchi, Eugenia Polverini

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. 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

2 authors at 1 institution in 1 country.

Alessio PeracchiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.ORCID 0000-0003-3254-4099
Eugenia PolveriniDepartment of Mathematical, Physical and Computer Sciences, University of Parma, 43124 Parma, Italy.
University of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined the ability of two human cytosolic transaminases, aspartate aminotransferase (GOT1) and alanine aminotransferase (GPT), to transform their preferred substrates whilst discriminating against similar metabolites. This offers an opportunity to survey our current understanding of enzyme selectivity and specificity in a biological context. Substrate selectivity can be quantitated based on the ratio of the

Indexed as

Alkyl and Aryl TransferasesAmino AcidsAnimalsBinding SitesCattleEnzyme ActivationHumansKineticsModels, MolecularProtein ConformationStructure-Activity RelationshipSubstrate SpecificityTransaminasesTransferases (Other Substituted Phosphate Groups)Alkyl and Aryl TransferasesAmino Acidsgeranylpyrophosphate olivetolate geranyltransferaseTransaminasesTransferases (Other Substituted Phosphate Groups)UDP-GlcNAc-undecaprenyl phosphate N-acetylglucosaminyl 1-phosphate transferaseenzyme assaysenzyme evolutionlimits of specificitymolecular discriminationsubstrate specificitytransaminases

Identifiers

PMID35209187
PMCPMC8875635
OpenAlexW4212832399

What OpenQuestion holds

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LicenceCC BY
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.