Introduction to Serine Hydroxymethyltransferase (SHMT/glyA)
Serine hydroxymethyltransferase (SHMT), encoded by the glyA gene, is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible conversion of serine to glycine while generating 5,10-methylene tetrahydrofolate (MTHF), a key intermediate in one-carbon metabolism. This reaction is critical for purine, thymidylate, and methionine biosynthesis, making SHMT essential for bacterial survival and virulence.
Recombinant SHMT Production and Applications
Although recombinant P. gingivalis SHMT has not been explicitly documented, methodologies for related enzymes provide a framework:
Table 1: Key Steps in Recombinant Protein Production (Inferred from P. gingivalis Systems)
Step
Methodology
Example from P. gingivalis Proteases
Gene Cloning
PCR amplification of glyA ORF with flanking homology regions
Used for rgpA and kgp mutants
Vector Design
Insertion into plasmids (e.g., pQE60) with antibiotic resistance markers
SHMT activity confirmed via genetic rescue in E. coli ΔglyA
Research Gaps and Future Directions
Structural Insights: No crystal structure of P. gingivalis SHMT exists, though H. pylori SHMT structural studies reveal weak PLP binding and disordered active sites.
Glycosylation: P. gingivalis O-glycosylation modifies periplasmic proteins, but its impact on SHMT remains unexplored.
Therapeutic Targeting: SHMT inhibitors could disrupt folate metabolism, but specific drug design requires further study.
Table 2: SHMT Functional Impact Across Bacterial Species
Organism
SHMT Role
Phenotype of ΔglyA
Relevance to P. gingivalis
H. pylori
MTHF synthesis, glycine auxotrophy
Slow growth, loss of CagA
Suggests SHMT links metabolism to virulence
E. coli
Glycine biosynthesis
Glycine auxotrophy
Highlights conserved metabolic function
P. gingivalis (inferred)
Folate cycle, biofilm symbiosis
Likely impaired growth under nutrient stress
Supported by metabolic cooperativity data
Product Specs
Form
Lyophilized powder. We will preferentially ship the format we have in stock. If you have special format requirements, please note them when ordering.
Lead Time
Delivery times vary by purchase method and location. Consult your local distributor for specific delivery times. All proteins are shipped with normal blue ice packs by default. Request dry ice shipment in advance (extra fees apply).
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute protein in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer ingredients, storage temperature, and protein stability. Liquid form: 6 months at -20°C/-80°C. Lyophilized form: 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing. If you require a specific tag, please inform us, and we will prioritize its development.
Catalyzes the reversible interconversion of serine and glycine, using tetrahydrofolate (THF) as the one-carbon carrier. This is the primary source of one-carbon groups for biosynthesis of purines, thymidylate, methionine, and other biomolecules. Also exhibits THF-independent aldolase activity towards beta-hydroxyamino acids, producing glycine and aldehydes via a retro-aldol mechanism.