Recombinant Streptococcus pyogenes serotype M5 Thymidylate synthase (thyA)

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Cat. No.
BT37695
Source
Yeast
Synonyms
thyA; SpyM51120; Thymidylate synthase; TS; TSase; EC 2.1.1.45
Purity
>85% (SDS-PAGE)
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Cat. No.
BT37695
Source
E.coli
Synonyms
thyA; SpyM51120; Thymidylate synthase; TS; TSase; EC 2.1.1.45
Purity
>85% (SDS-PAGE)
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Cat. No.
BT37695
Source
E.coli
Synonyms
thyA; SpyM51120; Thymidylate synthase; TS; TSase; EC 2.1.1.45
Purity
>85% (SDS-PAGE)
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Cat. No.
BT37695
Source
Baculovirus
Synonyms
thyA; SpyM51120; Thymidylate synthase; TS; TSase; EC 2.1.1.45
Purity
>85% (SDS-PAGE)
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Cat. No.
BT37695
Source
Mammalian cell
Synonyms
thyA; SpyM51120; Thymidylate synthase; TS; TSase; EC 2.1.1.45
Purity
>85% (SDS-PAGE)
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Description

Overview of Thymidylate Synthase (ThyA)

ThyA is a critical enzyme in the de novo synthesis of thymidine 5′-triphosphate (dTTP), catalyzing the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP). In E. coli, ThyA serves as a dual-selectable marker for genetic engineering, enabling both positive and negative selection during recombinogenic modifications . The enzyme’s activity depends on tetrahydrofolate (THF) as a cofactor, which is depleted in the presence of trimethoprim, a dihydrofolate reductase inhibitor .

ThyA in Recombinant Systems

In E. coli, recombinant ThyA has been utilized for seamless DNA modifications in plasmids and bacterial artificial chromosomes (BACs) :

  • Positive Selection: ΔthyA E. coli mutants require exogenous ThyA for growth in thymine-free media.

  • Negative Selection: Functional ThyA-expressing cells are eliminated in media containing thymine and trimethoprim due to THF depletion .

While this system is well-documented in E. coli, its direct application to S. pyogenes M5 ThyA remains unexplored in the provided sources.

Streptococcus pyogenes M5 Research Context

The search results highlight S. pyogenes M5’s virulence factors, including:

  • M5 Protein: A key antigen associated with rheumatic fever due to cross-reactivity with human cardiac myosin .

  • Superantigens: Mitogenic activity in M5 protein preparations is attributed to trace contaminants like streptococcal pyrogenic exotoxin C, not ThyA .

  • Immunomodulatory Enzymes: C5a peptidase and IdeS (IgG-degrading enzyme) are prominent, but ThyA is not mentioned .

Potential Applications of Recombinant ThyA in S. pyogenes

Though absent from the provided data, hypothetical applications of recombinant S. pyogenes ThyA could include:

  • Gene Knockout Systems: Mimicking E. coli’s ThyA selection for targeted mutagenesis.

  • Antibiotic Resistance Studies: Investigating thymidine auxotrophy in vaccine development.

Key Research Gaps

The provided literature lacks direct references to recombinant S. pyogenes M5 ThyA. Current studies focus on:

  • M5 Protein Epitopes: Cross-reactive T-cell and B-cell epitopes linked to autoimmune responses .

  • Antimicrobial Susceptibility: M5 strains remain susceptible to β-lactams and macrolides .

Comparative Table: ThyA Systems vs. S. pyogenes M5 Virulence Factors

FeatureE. coli ThyA S. pyogenes M5 Virulence Factors
Primary FunctiondTTP synthesis, genetic selectionPhagocytosis resistance, immune evasion
Selection MechanismDual (positive/negative)N/A
Role in PathogenicityNon-pathogenicRheumatic fever, scarlet fever
Recombinant UsePlasmid/BAC modificationVaccine development, epitope mapping

Product Specs

Form
Lyophilized powder. Note: We will prioritize shipping the format we have in stock. If you have a specific format requirement, please specify it when ordering, and we will fulfill your request.
Lead Time
Delivery times vary depending on the purchase method and location. Please contact your local distributor for specific delivery information. Note: All proteins are shipped with standard blue ice packs. For dry ice shipping, please contact us in advance, and additional fees will apply.
Notes
Avoid repeated freezing and thawing. Store working aliquots at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect the contents at the bottom. Reconstitute the protein in sterile deionized water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on several factors, including storage conditions, buffer components, storage temperature, and protein stability. Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receiving. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type will be determined during the manufacturing process. If you require a specific tag type, please inform us, and we will prioritize developing it.
Synonyms
thyA; SpyM51120; Thymidylate synthase; TS; TSase; EC 2.1.1.45
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-279
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Streptococcus pyogenes serotype M5 (strain Manfredo)
Target Names
thyA
Target Protein Sequence
MTKADQIFKA NIQKIINEGS LSEQARPKYK DGRTAHSKYI TGAFAEYDLA KGEFPITTLR PIPIKSAIKE LFWIYQDQSN SLDVLEAKYN VHYWNEWEVD QTRTIGQRYG AVVKKHDIIS KILKQLAENP WNRRNVISLW DYEAFEETKG LLPCAFQIMF DVRRVGEDLY LDASLTQRSN DILVAHHINA MQYVALQMMI AKHFGWKIGK FFYFVNNLHI YDNQFDQAQE LLKRQPVASQ PKLVLNVPDG TNFFDIKPDD FELQNYDPVK PQLHFDLAI
Uniprot No.
A2RF20

Target Background

Function
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP), using 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant, producing dihydrofolate (DHF) as a byproduct. This reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Database Links

KEGG: spf:SpyM51120

Protein Families
Thymidylate synthase family, Bacterial-type ThyA subfamily
Subcellular Location
Cytoplasm.

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