The tdh enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily, sharing structural and functional homology with alcohol dehydrogenases. Its primary role is to oxidize L-threonine, an essential amino acid, into a ketobutyrate intermediate, which contributes to glycine biosynthesis and redox balance . In Burkholderia species, this pathway is linked to metabolic flexibility and stress adaptation, as evidenced by its upregulation under nutrient-limiting conditions .
Survival in Hosts: A transposon mutagenesis study identified tdh (Bcep1341) as essential for Burkholderia cenocepacia’s survival in rat lung infections, highlighting its role in metabolic adaptation .
Biofilm Formation: The enzyme is linked to biofilm architecture and stress resistance, with mutants showing reduced motility and altered cyclic-di-GMP levels .
Vaccine Targets: Surface-exposed tdh homologs (e.g., BCAL2645) have been proposed as immunogenic candidates for Burkholderia vaccines .
Recombinant tdh from Burkholderia vietnamiensis (strain G4) has been expressed in E. coli, yielding >85% pure protein via SDS-PAGE . Its sequence (Uniprot A4JKG7) aligns with cenocepacia homologs, suggesting functional conservation .
| Recombinant Product Details | Value |
|---|---|
| Product Code | CSB-BP023350BPV/CSB-MP023350BPV |
| Host Organism | E. coli |
| Purity | >85% (SDS-PAGE) |
| Storage | -20°C/-80°C |
Diagnostic Tools: Recombinant tdh may serve as a target for serological assays to detect Burkholderia infections in cystic fibrosis patients .
Therapeutic Targets: Inhibitors of tdh could disrupt glycine biosynthesis, offering a novel antimicrobial strategy .
Biotechnology: The enzyme’s substrate promiscuity and thermostability make it suitable for industrial biocatalysis .
KEGG: bcm:Bcenmc03_4535