Evidence map›Paper›PMID 38896437›Full record

ArticleChembiochem : a European journal of chemical biology2024

Characterization of HphA: The First Enzyme in the Homologation Pathway of l-Phenylalanine and l-Tyrosine.

Laura E Stewart, Skyler L Owens, Shopno R Ahmed, Rebecca M Lang Harman, Shogo Mori

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In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

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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

5 authors.

Laura E StewartDepartment of Chemistry and Biochemistry, Augusta University, 1120 15th Street, Augusta, GA 30912, USA.
Skyler L OwensDepartment of Chemistry and Biochemistry, Augusta University, 1120 15th Street, Augusta, GA 30912, USA.
Shopno R AhmedDepartment of Chemistry and Biochemistry, Augusta University, 1120 15th Street, Augusta, GA 30912, USA.
Rebecca M Lang HarmanDepartment of Chemistry and Biochemistry, Augusta University, 1120 15th Street, Augusta, GA 30912, USA.
Shogo MoriDepartment of Chemistry and Biochemistry, Augusta University, 1120 15th Street, Augusta, GA 30912, USA.ORCID https://orcid.org/0000-0003-4518-7270

Funding

The origins of amino acid selectivity in the homologation pathwayR15GM151721 · NIGMS · AUGUSTA UNIVERSITY · PI MORI, SHOGO · 2023 to 2023
$424k
Department of Chemistry and Biochemistry (formally Chemistry and Physics) at Augusta University, Research Scholarship and Creative Activity Program in the Division of Sponsored Programs Administration at Augusta University RSCA00020National Institute of General Medical Sciences of the National Institutes of Health R15 GM151721NIGMS NIH HHS R15 GM151721
6 · The paper itself

Abstract

Homologation of amino acids is the insertion or deletion of a methylene group to their side chain, which is a relatively uncommon chemical transformation observed in peptide natural product (NP) structure. Homologated amino acids can potentially make the NP more stable in a biological system, but its biosynthesis is yet to be understood. This study biochemically characterized the first of three unexplored enzymes in the homologation pathway of l-phenylalanine and l-tyrosine. Previously proposed reactions catalyzed by HphA were confirmed by reversed-phase high-performance liquid chromatography and tandem mass spectrometry analysis. The substrate profile and kinetic parameters showed high selectivity for the natural substrates and their close analogs. The comparability of HphA to homologous enzymes in primary metabolic pathways, 2-isopropylmate synthase and homocitrate synthase which are involved in l-leucine and l-lysine biosynthesis, respectively, was validated by bioinformatical and site-directed mutagenesis studies. The knowledge obtained from this study has deepened the understanding of the homologation of amino acids, which can lead to future combinatorial biosynthesis and metabolic engineering studies.

Indexed as

PhenylalanineTyrosineKineticsSubstrate SpecificityPhenylalanineTyrosineAnabaenopeptinsBiosynthesisEnzymologyHomologationNatural products

Identifiers

PMID38896437
PMCPMC11382533

What OpenQuestion holds

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Registered trials

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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.