Recombinant Bifidobacterium adolescentis Peptide deformylase (def)

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Description

Introduction to Peptide Deformylase (PDF)

Recombinant Enzymes in Bifidobacterium adolescentis: A Focus on Characterized Systems

EnzymeClass/FamilyFunctionRecombinant ExpressionKey FindingsSources
β-Glucosidases (BaBgl1A, BaBgl3A, BaBgl3B)GH1, GH3Hydrolysis of β-1,2; β-1,3; β-1,4 linkages in oligosaccharides/ginsenosidesE. coli BL21 (DE3)BaBgl1A: Exclusive β-1,2 activity; BaBgl3B: β-1,4 specificity. Bioconversion of Rb1/Rd ginsenosides.
α-L-Arabinofuranosidase (axhD3)GH43Cleavage of α-L-arabinofuranoside bonds in xylanE. coliReleases C3-linked arabinose from xylose residues in xylan; part of xylanolytic pathways.
Reducing-End Xylose-Releasing Exo-Oligoxylanase (RexA)GH8Releases xylose from reducing ends of oligoxylansE. coliExo-activity confirmed via substrate specificity assays; shares catalytic residues with Bacillus halodurans Rex.
GH13 Family EnzymesGH13Amylase, pullulanase, cyclomaltodextrinase activitiesNot explicitly recombinantHigh abundance in B. adolescentis genomes; critical for starch metabolism.

Gaps in Research on B. adolescentis PDF

Despite the importance of PDF in bacterial physiology, no studies in the provided sources address:

  • Genomic Identification: Presence of PDF-encoding genes in B. adolescentis.

  • Recombinant Production: Expression systems, purification strategies, or catalytic characterization.

  • Functional Role: Contribution to protein maturation or stress responses in B. adolescentis.

Hypothesis: PDF may be conserved in B. adolescentis due to its universal role in bacteria, but targeted studies are lacking.

Genetic Diversity and Enzymatic Specialization

  • Pan-Genome Analysis: B. adolescentis exhibits high genetic diversity, with core genes enriched in carbohydrate metabolism (e.g., GH13, GH45 families) .

  • Carbohydrate Utilization: Strains like PRL2023 show enhanced growth on inulin, pullulan, and fructooligosaccharides, driven by specialized GH enzymes .

Stress Adaptation and Morphology

  • Morphological Plasticity: B. adolescentis maintains a bifid shape intrinsically, while other species adopt rod forms under stress .

  • Membrane Potential: Exposure to eukaryotic cells or inflammatory conditions reduces membrane potential, indicating stress responses .

Product Specs

Form
Lyophilized powder. We will ship the in-stock format preferentially. If you have special format requirements, please note them when ordering.
Lead Time
Delivery time varies by purchase method and location. Consult your local distributor for specifics. All proteins are shipped with blue ice packs by default. Request dry ice in advance; extra fees apply.
Notes
Avoid repeated freezing and thawing. Working aliquots are stable at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute 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 glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer, 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 arrival. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during manufacturing. If you require a specific tag, please inform us and we will prioritize its development.
Synonyms
def; BAD_1293Peptide deformylase; PDF; EC 3.5.1.88; Polypeptide deformylase
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-218
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)
Target Names
def
Target Protein Sequence
MFGHNSKVDL ELNREVEKLI KTGGKEKIMP IVQAGEPVLR QQTIAYDGQL SRKTLDKLID TMRTTMLEAP GVGLAATQIG LGLALAVVED HVCEGDDGDP REAAEFPFHA IINPSYEPIG TETRSFYEGC LSFDGYQAVR KRWLDITARW QDEDGNKHEE HLHGWPARIF QHETDHLSGE LYIDQAEIRS LTTNENLEDF WCEDPVPTEA AAELGFEL
Uniprot No.

Target Background

Function
Removes the formyl group from the N-terminal methionine of newly synthesized proteins. Requires at least a dipeptide for efficient activity. N-terminal L-methionine is required, but other positions have broad specificity.
Database Links
Protein Families
Polypeptide deformylase family

Q&A

Experimental Design for Studying Recombinant Bifidobacterium adolescentis Peptide Deformylase (def)

Q: How can researchers design experiments to study the effects of recombinant Bifidobacterium adolescentis peptide deformylase (def) in a controlled environment? A: To study the effects of recombinant Bifidobacterium adolescentis peptide deformylase (def), researchers can use a combination of in vitro and in vivo experiments. In vitro studies can involve expressing the recombinant enzyme in a suitable host (e.g., E. coli) and assessing its activity using biochemical assays. In vivo studies might involve using animal models to evaluate the impact of the enzyme on gut microbiota composition and host health. Additionally, co-cultivation assays with other gut bacteria can help understand cross-feeding strategies and metabolic interactions .

Data Analysis and Contradiction Resolution

Q: How can researchers analyze and resolve contradictions in data related to the effects of recombinant Bifidobacterium adolescentis peptide deformylase (def) on gut health? A: Analyzing data from studies on recombinant Bifidobacterium adolescentis peptide deformylase (def) involves using statistical methods to assess the significance of observed effects. Contradictions can arise due to differences in experimental design, host models, or environmental conditions. Researchers can resolve these by conducting meta-analyses, adjusting for confounding variables, and ensuring consistency in data collection and analysis methods across studies .

Advanced Research Questions: Mechanisms of Action

Q: What are some advanced research questions regarding the mechanisms of action of recombinant Bifidobacterium adolescentis peptide deformylase (def) in modulating gut microbiota? A: Advanced research questions might include:

  • Mechanism of Enzyme Activity: How does recombinant peptide deformylase (def) from Bifidobacterium adolescentis interact with other enzymes to modulate carbohydrate metabolism in the gut?

  • Immunomodulation: Does the enzyme influence immune responses by interacting with host immune cells or modulating the production of cytokines?

  • Metabolic Pathways: How does the enzyme contribute to the degradation of complex polysaccharides and the production of short-chain fatty acids (SCFAs) in the gut?

Methodological Considerations for Gene Expression Studies

Q: What methodological considerations are important when studying the gene expression of recombinant Bifidobacterium adolescentis peptide deformylase (def) in response to different environmental conditions? A: When studying gene expression, it is crucial to use techniques like quantitative PCR (qPCR) or RNA sequencing to quantify mRNA levels. Additionally, controlling for environmental factors such as temperature, pH, and nutrient availability is essential. Researchers should also consider using appropriate reference genes for normalization and validating results through multiple experimental replicates .

Comparative Analysis with Other Bifidobacterium Species

Q: How can researchers conduct a comparative analysis of the effects of recombinant peptide deformylase (def) from Bifidobacterium adolescentis versus other Bifidobacterium species on gut health? A: A comparative analysis involves using similar experimental setups to assess the effects of recombinant peptide deformylase (def) from different Bifidobacterium species. This can include comparing growth rates, metabolic profiles, and immune responses in host models. Statistical methods such as ANOVA or non-parametric tests can be used to identify significant differences between species .

Integration with Other Microbial Metabolic Pathways

Q: How does recombinant Bifidobacterium adolescentis peptide deformylase (def) integrate with other microbial metabolic pathways in the gut? A: The integration of recombinant peptide deformylase (def) with other microbial pathways can be studied by analyzing co-expression networks and metabolic fluxes. Techniques like metatranscriptomics and metabolomics can provide insights into how this enzyme interacts with other enzymes and pathways to degrade complex carbohydrates and produce beneficial metabolites .

Challenges in Translating Research to Clinical Applications

Q: What challenges do researchers face when translating findings on recombinant Bifidobacterium adolescentis peptide deformylase (def) into clinical applications? A: Challenges include scaling up production of the recombinant enzyme while maintaining its activity, ensuring safety and efficacy in human trials, and navigating regulatory frameworks. Additionally, understanding individual variability in response to the enzyme and developing personalized treatment strategies are crucial steps towards clinical application .

Role of Exopolysaccharides in Immunomodulation

Q: How do exopolysaccharides (EPS) from Bifidobacterium adolescentis interact with recombinant peptide deformylase (def) to modulate immune responses? A: While there is no direct interaction between EPS and recombinant peptide deformylase (def), EPS from Bifidobacterium adolescentis can modulate immune responses by inhibiting Toll-like receptor signaling, which may complement the metabolic effects of the enzyme in maintaining gut health .

Future Research Directions

Q: What are some future research directions for studying recombinant Bifidobacterium adolescentis peptide deformylase (def)? A: Future studies could focus on:

  • Mechanistic Insights: Elucidating the molecular mechanisms by which the enzyme interacts with other gut bacteria and host cells.

  • Therapeutic Applications: Exploring the potential of the enzyme as a therapeutic agent in managing gut-related disorders.

  • Systems Biology Approaches: Using systems biology tools to model and predict the effects of the enzyme on gut microbiota dynamics and host health outcomes .

Example Data Table: Growth of Bifidobacterium adolescentis on Different Carbohydrates

Carbohydrate SourceGrowth (OD Value)
Inulin0.8
Pullulan0.9
Maltotriose1.0
Maltodextrin1.1
Fructooligosaccharides1.0
Lactulose0.8
Cellobiose0.7
Galactose0.6
N-acetyl-D-glucosamine0.5

Note: OD values are examples based on typical growth experiments.

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