ReviewBiotechnology letters2022
Production of phenylpyruvic acid by engineered L-amino acid deaminase from Proteus mirabilis.
Review in Biotechnology letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
The trial behind it
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Engineered Biocatalysts for the Asymmetric Synthesis of d-Phenylalanines.ACS catalysis · 2025Review
- EngineeringRSC advances · 2024Article
- Effect of hexavalent chromium on growth performance and metabolism in broiler chicken.Frontiers in veterinary science · 2023Article
- Semi-rational engineering membrane binding domain of L-amino acid deaminase fromFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
objectivesThis study aimed to develop an efficient enzymatic strategy for the industrial production of phenylpyruvate (PPA) from L-phenylpyruvic acid (L-Phe).
resultsL-amino acid deaminase from Proteus mirabilis was expressed in Escherichia coli BL21 (DE3) and modified to release product inhibition by employing conformational dynamics engineering. Based on structural analysis, two residues (E145/L341) were identified for reducing interactions between the product and enzyme and increasing flexibility of the protein, thereby facilitating the product release. The mutant M2
conclusionsThe engineered catalyst can significantly reduce product inhibition and facilitate the effective industrial synthesis of PPA.
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Registered trials
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