Recombinant Delftia acidovorans Lipoyl synthase (lipA)

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Description

Lipoyl Synthase (LipA): General Function

LipA catalyzes the insertion of sulfur atoms into octanoyl-ACP to form lipoic acid, a cofactor essential for pyruvate dehydrogenase (PDH) and α-ketoglutarate dehydrogenase complexes . In other bacteria (e.g., Staphylococcus aureus), LipA-mediated lipoylation of PDH’s E2 subunit modulates host immune responses by suppressing Toll-like receptor 2 (TLR2) activation .

LipA in Delftia acidovorans: Indirect Insights

While no studies explicitly describe recombinant Delftia acidovorans LipA, genomic and metabolic research on this bacterium provides clues:

  • Genetic Engineering Potential: D. acidovorans DSM 39 is a well-characterized strain used in genetic engineering for polyhydroxyalkanoate (PHA) production . Recombinant strains have been engineered with lipase genes (e.g., lipH and lipC) to metabolize lipids .

  • Lipoic Acid Metabolism: LipA homologs in related bacteria (e.g., Methylobacterium) are linked to defects in lipoic acid synthesis, impairing metabolic pathways like the citric acid cycle .

Table 1: LipA Characteristics in Bacterial Systems

OrganismFunction of LipAPhenotype of lipA MutantsReference
Staphylococcus aureusLipoylation of E2-PDH; immune suppressionHyper-inflammatory macrophage response
MethylobacteriumLipoic acid synthesisDefective 3-hydroxybutyrate production
  • Immune Modulation: S. aureus LipA suppresses TLR2 activation by releasing lipoyl-E2-PDH, reducing pro-inflammatory cytokine production .

  • Metabolic Defects: Methylobacterium hbd lipA mutants show disrupted lipoic acid synthesis, affecting PHB degradation and R-3-hydroxybutyrate production .

Applications and Relevance to Delftia acidovorans

  • Biopolymer Production: Recombinant D. acidovorans strains engineered with lipase genes produce PHAs from lipid wastes (e.g., slaughterhouse residues) . LipA could theoretically enhance lipid metabolism in such systems.

  • Bioremediation: D. acidovorans degrades organofluorine compounds via dehalogenases , but LipA’s role in these pathways remains unexplored.

Research Gaps and Future Directions

  • Functional Studies: No direct evidence exists for LipA’s role in D. acidovorans. Heterologous expression and purification of recombinant LipA could clarify its enzymatic activity.

  • Industrial Applications: Engineering D. acidovorans with optimized LipA might improve lipid-to-PHA conversion efficiency or enable novel biocatalytic processes.

Product Specs

Form
Lyophilized powder. We will preferentially ship the available format. If you have specific format requirements, please note them when ordering.
Lead Time
Delivery time varies based on purchasing method and location. Consult your local distributor for specifics. All proteins are shipped with normal blue ice packs by default. Request dry ice shipment in advance; extra fees 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. 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 components, temperature, and protein stability. Liquid form: generally 6 months at -20°C/-80°C. Lyophilized form: generally 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon arrival. 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.
Synonyms
lipA; Daci_0410; Lipoyl synthase; EC 2.8.1.8; Lip-syn; LS; Lipoate synthase; Lipoic acid synthase; Sulfur insertion protein LipA
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-326
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Delftia acidovorans (strain DSM 14801 / SPH-1)
Target Names
Target Protein Sequence
MTTNTVVREA QSQAEYNPLA KQKAAAKLSR IPIKVEHGEA LKKPDWIRVK AGSPTTRFYE IKDILRANKL HTVCEEASCP NIGECFGKGT ATFMIMGDKC TRRCPFCDVG HGRPDPLDTN EPLNLAKTIA ELRLKYVVIT SVDRDDLRDG GSGHFVECIK NIRELSPLTQ IEILVPDFRG RDDRALEILK AAPPDVMNHN LETAPRLYKE ARPGSDYQFS LNLLKKFKAL HPKVPTKSGI MVGLGETDEE ILQVMRDMRA HDIDMLTIGQ YLAPSNSHLP VRRYVHPDTF KMFEEEAYKM GFTHAAVGAM VRSSYHADQQ AHAAGV
Uniprot No.

Target Background

Function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, converting octanoylated domains into lipoylated derivatives.
Database Links
Protein Families
Radical SAM superfamily, Lipoyl synthase family
Subcellular Location
Cytoplasm.

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