Recombinant Yersinia pseudotuberculosis serotype O:1b Serine hydroxymethyltransferase (glyA)
Description
Enzyme Function and Importance
Serine hydroxymethyltransferase (glyA) is a pyridoxal-5'-phosphate-dependent enzyme that facilitates the reversible conversion of serine to glycine and a one-carbon unit (5,10-methylene-tetrahydrofolate). This reaction is central to nucleotide biosynthesis, amino acid metabolism, and folate-dependent processes. In pathogens like Yersinia, glyA may contribute to nutrient acquisition and survival within host tissues .
Relevance to Yersinia pseudotuberculosis Pathogenesis
While glyA is not directly discussed in the provided studies, related metabolic pathways are critical for Y. pseudotuberculosis infection. For example:
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Nutrient adaptation: The bacterium’s ability to modulate glucose and acetate metabolism in human plasma (as shown in ) suggests a reliance on metabolic flexibility, which glyA could support.
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Vaccine development: The engineering of attenuated Y. pseudotuberculosis strains (e.g., Yptb1[pYA5199] in ) highlights the importance of metabolic genes in vaccine design. GlyA’s role in folate metabolism could theoretically influence vaccine efficacy.
Research Gaps
The absence of glyA-specific data in the provided sources underscores a gap in understanding its role in Y. pseudotuberculosis. Key research questions include:
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Does glyA contribute to pathogen persistence in host tissues (e.g., Peyer’s patches, liver)?
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How does glyA interact with other metabolic genes during infection?
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Could glyA serve as a target for antimicrobial therapy or vaccine development?
Potential Experimental Approaches
Future studies could:
Product Specs
Target Background
KEGG: ypi:YpsIP31758_1158
