Recombinant Burkholderia multivorans Phosphoserine aminotransferase (serC)
Description
Introduction to Phosphoserine Aminotransferase (serC)
Phosphoserine aminotransferase (serC) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible conversion of 3-phosphohydroxypyruvate to L-phosphoserine in the serine biosynthesis pathway. This pathway is critical for cellular metabolism, supporting protein synthesis, folate metabolism, and nucleotide production .
In Burkholderia multivorans, a member of the Burkholderia cepacia complex (BCC), serC is hypothesized to play a role in amino acid metabolism and virulence. Recombinant serC refers to the enzyme produced via heterologous expression systems (e.g., Escherichia coli) for biochemical and structural studies .
Functional and Genomic Context of serC in Burkholderia
The serC gene is conserved across Burkholderia species, with homologs identified in pathogenic and environmental strains. Key findings include:
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Essentiality: In Burkholderia pseudomallei, serC disruption via signature-tagged mutagenesis resulted in attenuated virulence in murine models and auxotrophy in minimal media, underscoring its metabolic importance .
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Metabolic Role: Burkholderia multivorans genome-scale metabolic reconstructions highlight serine biosynthesis as integral to energy production and amino acid transport .
Table 1: serC Homologs in Burkholderia Species
Research Gaps and Future Directions
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Functional Characterization: Detailed kinetic and structural studies of recombinant B. multivorans serC are needed to elucidate species-specific adaptations.
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Gene Regulation: The role of serC in biofilm formation or antimicrobial tolerance remains unexplored in B. multivorans, despite biofilm-associated proteomic shifts in related species like B. thailandensis .
Product Specs
Target Background
KEGG: bmj:BMULJ_00977
STRING: 395019.BMULJ_00977
