ArticleScientific reports2019
Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- An Integrated Engineering Approach to Intensify the Biocatalytic Metaraminol Synthesis.ChemSusChem · 2026Article
- Investigating operational stability and causes of cofactor release in fold type I amine transaminase.Protein science : a publication of the Protein Society · 2026Article
- Exploring the Stability and Substrate Profile of Transaminase from Silicibacter pomeroyi with Ancestral Sequence Reconstruction.Chembiochem : a European journal of chemical biology · 2025Article
- From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the BacteriumBiomolecules · 2024Article
- Review
- Biocatalysis enables the scalable conversion of biobased furans into various furfurylamines.Nature communications · 2024Article
- Biocatalytic cascade to polysaccharide amination.Biotechnology for biofuels and bioproducts · 2024Article
- Construction and yield optimization of a cinnamylamine biosynthesis route in Escherichia coli.Biotechnology for biofuels and bioproducts · 2022Article
- Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition.Communications biology · 2020Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the main factors hampering the implementation in industry of transaminase-based processes for the synthesis of enantiopure amines is their often low storage and operational stability. Our still limited understanding of the inactivation processes undermining the stability of wild-type transaminases represents an obstacle to improving their stability through enzyme engineering. In this paper we present a model describing the inactivation process of the well-characterized (S)-selective amine transaminase from Chromobacterium violaceum. The cornerstone of the model, supported by structural, computational, mutagenesis and biophysical data, is the central role of the catalytic lysine as a conformational switch. Upon breakage of the lysine-PLP Schiff base, the strain associated with the catalytically active lysine conformation is dissipated in a slow relaxation process capable of triggering the known structural rearrangements occurring in the holo-to-apo transition and ultimately promoting dimer dissociation. Due to the occurrence in the literature of similar PLP-dependent inactivation models valid for other non-transaminase enzymes belonging to the same fold-class, the role of the catalytic lysine as conformational switch might extend beyond the transaminase enzyme group and offer new insight to drive future non-trivial engineering strategies.
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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.