Recombinant Escherichia coli O45:K1 Monofunctional biosynthetic peptidoglycan transglycosylase (mtgA)

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Description

Introduction to Recombinant Escherichia coli O45:K1 Monofunctional Biosynthetic Peptidoglycan Transglycosylase (mtgA)

Recombinant Escherichia coli O45:K1 Monofunctional Biosynthetic Peptidoglycan Transglycosylase (mtgA) is a recombinant protein derived from the Escherichia coli O45:K1 strain. This protein is involved in the biosynthesis of peptidoglycan, a crucial component of bacterial cell walls that provides structural integrity and maintains cell shape against osmotic pressure . The mtgA protein is specifically a monofunctional glycosyltransferase, meaning it catalyzes the elongation of glycan chains in peptidoglycan without cross-linking them .

Structure and Function of mtgA

The recombinant mtgA protein is expressed in Escherichia coli and consists of 242 amino acids, with an N-terminal His tag for purification purposes . As a glycosyltransferase, mtgA plays a role in the assembly of peptidoglycan during the bacterial cell cycle, particularly at the division site . It interacts with other components of the divisome, such as PBP3, FtsW, and FtsN, to facilitate peptidoglycan synthesis during cell division .

Role in Peptidoglycan Synthesis

Peptidoglycan synthesis involves the polymerization of glycan chains and the cross-linking of peptide chains. mtgA specifically catalyzes the elongation of glycan chains, contributing to the formation of the peptidoglycan layer. This process is essential for maintaining bacterial cell shape and integrity .

Research Findings

Research on mtgA has highlighted its importance in the cell cycle of Escherichia coli. Studies have shown that mtgA localizes at the division site and interacts with key proteins involved in septal peptidoglycan synthesis . The interaction of mtgA with PBP3, FtsW, and FtsN suggests a collaborative role in synthesizing new peptidoglycan during cell division .

Data Table: Characteristics of Recombinant mtgA

CharacteristicsDescription
Protein Length242 amino acids
Expression HostEscherichia coli
TagN-terminal His tag
FunctionGlycan chain elongation in peptidoglycan synthesis
LocalizationDivision site during cell division
Interacting ProteinsPBP3, FtsW, FtsN

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your preferred format in order notes for customized fulfillment.
Lead Time
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Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to collect the contents. 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 standard glycerol concentration is 50% and serves as a guideline.
Shelf Life
Shelf life depends on various factors including storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized formulations have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is essential for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during the manufacturing process.
The tag type is determined during production. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
mtgA; ECS88_3592; Biosynthetic peptidoglycan transglycosylase; Glycan polymerase; Peptidoglycan glycosyltransferase MtgA; PGT
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-242
Protein Length
full length protein
Species
Escherichia coli O45:K1 (strain S88 / ExPEC)
Target Names
mtgA
Target Protein Sequence
MSKSRLTVFSFVRRFLLRLMVVLAIFWGGGIALFSVAPVPFSAVMVERQVSAWLHGNFRY VAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEQALAHNERNENRIRGASTIS QQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQR YFHKPASKLTRSEAALLAAVLPNPLRFKVSAPSGYVRSRQAWILRQMYQLGGEPFMQQHQ LD
Uniprot No.

Target Background

Function
A peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Database Links
Protein Families
Glycosyltransferase 51 family
Subcellular Location
Cell inner membrane; Single-pass membrane protein.

Q&A

What is the genomic context of mtgA in E. coli O45:K1:H7 strains?

The mtgA gene in E. coli O45:K1:H7 strains exists within a specific genomic context that differs significantly from reference strains. In the emerging pathogenic clone represented by strain S88 (O45:K1:H7), the O-antigen gene cluster sequence differs from that of O45 in the reference strain E. coli 96-3285. While these two O45 polysaccharides likely share some epitopes, they represent two different antigens . The unique functional organization of the O-antigen gene clusters and the low DNA sequence homology suggest these loci originated from a common ancestor but underwent multiple recombination events. Phylogenetic analysis of flanking gene sequences indicates that the S88 antigen O45 gene cluster may have been acquired, at least partially, from another member of the Enterobacteriaceae family . This horizontal gene transfer event appears to have been a key factor in the emergence and virulence of the E. coli O45:K1:H7 clone.

What assay methods are most suitable for characterizing mtgA transglycosylase activity?

Various assay methods can be employed to characterize mtgA transglycosylase activity, each with distinct advantages. For initial screening and qualitative assessment, paper or thin layer chromatography offers high sensitivity but in a stopped assay format . For mechanistic studies requiring visualization of discrete glycan chain lengths, polyacrylamide gel-based techniques are valuable, though they lack sensitivity for longer chain products . HPLC provides medium sensitivity in a stopped format.

For high-throughput inhibitor screening, continuous fluorometric assays are optimal. These include continuous fluorescence monitoring, where a dansyl fluorophore shows increased quantum yield in hydrophobic environments, and FRET-based methods . These approaches have been successfully adapted to multi-well formats, enabling rapid parallel screening of reaction conditions and potential inhibitors. The following table summarizes the key characteristics of each assay type:

Assay typeStopped/ContinuousSensitivitySuitable for inhibitor screens
Paper/thin layer chromatographyStoppedHighNo
Polyacrylamide gelStoppedLowNo
HPLCStoppedMediumNo
Fluorometric: continuous fluorescenceContinuousHighYes
Fluorometric: FRETContinuousHighYes
Moenomycin displacementContinuousHighYes

When studying mtgA specifically, fluorometric continuous assays using dansyl-labeled lipid II are particularly effective, as the presence of the dansyl group prevents transpeptidation, allowing the isolated measurement of transglycosylation activity .

How does bacterial recombination affect the genetic stability of E. coli O45:K1 strains?

Bacterial recombination significantly impacts the genetic stability of E. coli strains, including O45:K1 variants. Recent metagenomic studies of gut bacteria have revealed that recombination introduces >10-fold as much variation as mutation, indicating that genomes of typical circulating strains are almost completely overwritten by recombination events over time . This high rate of genetic exchange poses challenges for evolutionary studies, as individual variants can frequently decouple from the genome-wide phylogeny.

In E. coli O45:K1 strains specifically, evidence suggests that horizontal acquisition of a new O-antigen gene cluster through recombination was a key event in the emergence of the virulent clone . Comparative analysis of O-antigen clusters in different strains indicates multiple recombination events contributed to the current genetic composition. Research methodologies to study these recombination patterns should include comparative genomics, analysis of flanking sequences (particularly gnd), and detailed assessment of population structure to identify barriers to recombination, which may include negative selection on recombined fragments or incompatible restriction-modification systems rather than simple ecological isolation .

How can researchers effectively distinguish between transglycosylase and transpeptidase activities when studying bifunctional PBPs versus monofunctional mtgA?

Distinguishing between transglycosylase and transpeptidase activities requires specific methodological approaches. For studying monofunctional mtgA versus bifunctional PBPs, researchers should consider:

  • Substrate modification: Using dansyl lipid II where the fluorophore is linked to the ε-amino group of the lysine side chain of the pentapeptide via a sulfonamide linkage. This modification prevents transpeptidation from occurring on this molecule while allowing transglycosylation, resulting in a transglycosylation-specific assay .

  • Selective inhibition: When using bifunctional PBPs, researchers can employ penicillin G to inhibit transpeptidase activity while allowing transglycosylase activity to proceed. This approach has been validated in multiple experimental systems, including paper chromatography and gel-based assays .

  • Continuous monitoring: The fluorometric continuous assay based on the increased quantum yield of fluorescence signal from a dansyl fluorophore in a hydrophobic micellar environment allows real-time measurement of transglycosylase activity. As the environment of the fluorophore changes from hydrophobic micelles to the soluble phase following N-acetylmuramidase digestion of glycan chains, the decrease in fluorescence can be attributed to the incorporation of lipid II into glycan chains .

  • Multi-technique validation: Combining stopped assays (like gel-based techniques that visualize discrete glycan chain lengths) with continuous assays (fluorometric methods) provides comprehensive characterization of transglycosylase activity. This is particularly valuable when comparing monofunctional mtgA with bifunctional PBPs.

These approaches enable researchers to precisely characterize mtgA activity without interference from transpeptidation reactions that would occur with native substrates in bifunctional enzymes.

What are the optimal expression and purification strategies for obtaining active recombinant E. coli O45:K1 mtgA?

Obtaining active recombinant E. coli O45:K1 mtgA requires careful consideration of expression and purification strategies due to its membrane-associated nature and specific activity requirements. While the search results don't provide specific protocols for mtgA, we can derive methodological approaches based on successful strategies for similar enzymes:

  • Expression system selection: For membrane-associated enzymes like mtgA, E. coli BL21(DE3) or C43(DE3) strains (designed for membrane protein expression) with pET-based vectors under IPTG-inducible promoters have shown success. Expression at lower temperatures (16-25°C) rather than 37°C often improves proper folding and activity.

  • Solubilization strategy: Since transglycosylases interact with membrane-bound substrates, detergent selection is critical. A systematic screen of detergents including n-dodecyl-β-D-maltopyranoside (DDM), n-octyl-β-D-glucopyranoside (OG), and CHAPS at concentrations above their critical micelle concentration is recommended.

  • Purification approach: A two-step purification combining affinity chromatography (His-tag) followed by size exclusion chromatography in the presence of the optimal detergent typically yields highly pure, active enzyme. All buffers should contain 10-20% glycerol to stabilize the protein.

  • Activity verification: Fluorometric continuous assays using dansyl-labeled lipid II substrates provide the most sensitive method for confirming transglycosylase activity post-purification . Initial rate determination under standardized conditions allows comparison between different preparations.

  • Storage considerations: Purified mtgA should be stored in small aliquots at -80°C in buffer containing 20% glycerol and the optimal detergent. Multiple freeze-thaw cycles should be avoided as they significantly reduce enzyme activity.

This methodological approach enables consistent preparation of active recombinant mtgA suitable for downstream enzymatic, structural, and inhibitor screening studies.

How does the unique O45 antigen affect the function and accessibility of mtgA in E. coli O45:K1:H7?

The unique O45 antigen in E. coli O45:K1:H7 strains has significant implications for mtgA function and accessibility due to the complex interplay between cell surface structures and peptidoglycan synthesis. Although the search results don't directly address this relationship, we can derive methodological approaches to investigate this question:

  • Comparative enzymology: Researchers should compare mtgA activity in isogenic strains differing only in their O-antigen expression (parent O45:K1:H7 versus O-antigen deletion mutants). Membrane preparations from these strains can be used in standardized in vitro transglycosylase assays, particularly fluorometric continuous assays, to quantify differences in specific activity .

  • Substrate accessibility analysis: Using fluorescently labeled lipid II analogs with varying structural characteristics, researchers can assess whether the O45 antigen creates steric hindrance affecting substrate access to mtgA. Kinetic parameters (Km, Vmax) determined from these assays would reveal different substrate binding or processing capabilities.

  • Cell wall architecture studies: Peptidoglycan isolated from wild-type and O-antigen mutant strains should be analyzed for glycan chain length distribution using polyacrylamide gel-based techniques . Differences in chain length profiles would suggest altered mtgA processivity in the different cellular contexts.

  • In vivo localization studies: Fluorescently tagged mtgA can be used to determine whether the enzyme's subcellular localization differs between strains with different O-antigens. Colocalization with other cell wall synthesis machinery would indicate if the O45 antigen affects the assembly of functional peptidoglycan synthesis complexes.

Research has established that the O45 polysaccharide in strain S88 plays a crucial role in virulence in a neonatal rat meningitis model , but the specific mechanisms involving mtgA activity remain to be elucidated through these methodological approaches.

What are the most effective screening methods for identifying novel inhibitors of E. coli O45:K1 mtgA?

Implementing an effective screening campaign for novel mtgA inhibitors requires a multi-tiered approach:

  • Primary screening: The fluorometric continuous assay represents the most effective high-throughput method for primary screening. This assay, based on the increased quantum yield of fluorescence from a dansyl fluorophore in a hydrophobic environment, has been successfully converted to a multi-well format enabling rapid parallel screening . The initial rate of decreased fluorescence (as the fluorophore moves from hydrophobic micelles to the aqueous phase following glycan chain formation) provides a direct measure of transglycosylase inhibition.

  • Counterscreen design: To eliminate false positives that interfere with the fluorescence signal rather than inhibiting mtgA, a secondary biochemical assay should be employed. For this purpose, the paper chromatography approach using radiolabeled lipid II offers high sensitivity and orthogonal detection methodology .

  • Mechanistic classification: For compounds showing inhibitory activity, a moenomycin displacement assay can determine if they bind to the same site as this known transglycosylase inhibitor . This approach helps categorize inhibitors by binding mode.

  • Selectivity assessment: Testing active compounds against a panel of different transglycosylases, including bifunctional PBPs and monofunctional enzymes from different bacterial species, establishes selectivity profiles. This is particularly important for targeting mtgA from pathogenic E. coli O45:K1:H7 strains specifically.

  • Structure-activity relationship studies: For promising compound classes, systematic structural modifications followed by testing in the primary assay can guide medicinal chemistry optimization.

This methodological approach enables efficient identification and characterization of novel chemical entities that specifically inhibit mtgA function, potentially leading to new antibacterial strategies targeting the emerging pathogenic E. coli O45:K1:H7 clone.

How can researchers accurately measure the kinetic parameters of mtgA-catalyzed transglycosylation reactions?

Accurate determination of kinetic parameters for mtgA-catalyzed transglycosylation reactions requires careful experimental design and analysis:

  • Substrate preparation: Radiolabeled or fluorescently labeled lipid II must be synthesized with high purity and characterized by mass spectrometry. For studying mtgA specifically, dansyl-labeled lipid II is preferred as it prevents transpeptidation while allowing transglycosylation .

  • Enzyme standardization: Enzyme preparations should be characterized for purity (>95% by SDS-PAGE) and specific activity under standardized conditions. Protein concentration should be accurately determined using methods that are not affected by detergent presence.

  • Reaction condition optimization: Buffer composition, pH, temperature, divalent cation concentration, and detergent type/concentration should be systematically optimized. For transglycosylases, the critical micelle concentration of detergents significantly affects enzyme activity.

  • Initial rate determination: Using the fluorometric continuous assay, initial rates should be measured at varying substrate concentrations under conditions where less than 10% of substrate is consumed. At least 7-8 substrate concentrations spanning 0.2-5× Km should be tested in triplicate .

  • Data analysis: Non-linear regression analysis using enzyme kinetics software (e.g., GraphPad Prism) should be employed to fit the data to appropriate models (Michaelis-Menten, Hill equation, etc.). For transglycosylases, substrate inhibition is sometimes observed at high concentrations of lipid II.

  • Product characterization: To confirm that the measured activity represents processive transglycosylation rather than single-round reactions, polyacrylamide gel-based techniques should be used to visualize the distribution of glycan chain lengths .

Following this methodological approach ensures reliable determination of kinetic parameters (Km, Vmax, kcat) for mtgA-catalyzed reactions, enabling meaningful comparisons between different enzyme variants or under different reaction conditions.

What methodologies are best suited for analyzing the role of mtgA in the enhanced virulence of E. coli O45:K1 strains?

To rigorously analyze mtgA's role in E. coli O45:K1 virulence, researchers should employ a multi-faceted approach:

  • Gene knockout and complementation: Precise deletion of mtgA in E. coli O45:K1:H7 strains (such as S88) using CRISPR-Cas9 or lambda Red recombination, followed by complementation with wild-type and mutant variants. This genetic manipulation should be confirmed by whole-genome sequencing to verify no off-target effects occurred.

  • In vitro phenotypic characterization: Comparative analysis of growth rates, cell morphology, and antibiotic susceptibility between wild-type, mtgA-knockout, and complemented strains. Peptidoglycan composition should be analyzed using HPLC to quantify changes in muropeptide profiles.

  • Animal infection models: The neonatal rat meningitis model, which has already been validated for studying O45:K1:H7 virulence , should be employed to compare the virulence of mtgA-manipulated strains. Key parameters to assess include bacterial load in blood and CSF, survival rates, and histopathological examination of infected tissues.

  • Host-pathogen interaction studies: Investigation of how mtgA-dependent changes in cell wall structure affect interactions with host immune components, particularly complement activation and phagocytosis. Flow cytometry and microscopy-based assays can quantify these interactions.

  • Transcriptomic and proteomic analysis: RNA sequencing and quantitative proteomics comparing wild-type and mtgA-mutant strains can reveal compensatory mechanisms and downstream effects of mtgA manipulation on global gene expression.

  • Structural analysis of peptidoglycan: Atomic force microscopy and electron microscopy to visualize differences in cell envelope architecture between wild-type and mtgA-mutant strains, correlating structural changes with virulence phenotypes.

Research has established that the O45 polysaccharide plays a crucial role in S88 virulence . By systematically investigating how mtgA affects peptidoglycan structure and function in the context of this O-antigen, researchers can determine whether mtgA represents a potential therapeutic target for combating these emerging pathogenic strains.

How should researchers interpret contradictory results from different transglycosylase assay methods when studying mtgA?

When faced with contradictory results from different assay methods, researchers should implement a systematic analytical approach:

  • Assay-specific limitations analysis: Each transglycosylase assay method has inherent limitations. For example, paper chromatography is highly sensitive but qualitative and stopped , while polyacrylamide gel-based techniques can visualize discrete chain lengths but lack sensitivity for longer polymers . Researchers should explicitly consider how these methodological constraints might affect results.

  • Substrate presentation effects: Different assays present lipid II in various physical states (micelles, liposomes, etc.). For monofunctional transglycosylases like mtgA, the substrate presentation can significantly impact activity. Systematic comparison using the same substrate preparation across different assay formats can identify if contradictions stem from substrate presentation rather than enzyme behavior.

  • Reaction condition standardization: Seemingly contradictory results often stem from subtle differences in reaction conditions. Researchers should standardize buffer composition, pH, ionic strength, temperature, and detergent concentration across methods whenever possible.

  • Sequential product analysis: Transglycosylation involves multiple reaction steps from initial binding through processivity. Different assays may preferentially detect different stages of this process. Using polyacrylamide gels to analyze reaction products at various time points can help resolve contradictions by revealing whether the assays are measuring different aspects of the same reaction .

  • Orthogonal validation: When contradictions persist, introducing a third, orthogonal method can help identify which results are more reliable. For example, if continuous fluorometric assays and gel-based techniques yield different results, mass spectrometry-based analysis of reaction products can provide definitive structural information.

What approaches best measure the impact of recombination events on mtgA structure and function in different E. coli strains?

Measuring the impact of recombination on mtgA requires integrated genomic, structural, and functional approaches:

  • Comparative sequence analysis: Researchers should perform phylogenetic analysis of mtgA sequences across diverse E. coli strains, particularly comparing O45:K1:H7 isolates with other lineages. Recombination detection programs (RDP, GARD, ClonalFrameML) can identify potential recombination breakpoints and donor sequences .

  • Structural mapping of variations: Homology modeling based on available transglycosylase crystal structures allows mapping of sequence variations onto the three-dimensional protein structure. This approach can predict whether recombination-introduced variations affect catalytic sites, substrate binding regions, or protein-protein interaction interfaces.

  • Recombinant enzyme characterization: Expression and purification of mtgA variants representing different recombination histories, followed by comparative enzymatic analysis using fluorometric continuous assays . Key parameters to compare include substrate specificity, processivity (via gel-based assays ), and inhibitor sensitivity profiles.

  • Domain swapping experiments: For mtgA genes showing evidence of mosaic structure due to recombination, domain swapping between variants can pinpoint which regions contribute to functional differences. This approach combines molecular cloning with the enzymatic characterization methods described above.

  • Correlation with population structure: Recent studies have shown widespread strain-level variation in recombination rates within commensal gut species, with barriers to recombination likely driven by negative selection on recombined fragments or incompatible restriction-modification systems . Researchers should analyze whether mtgA variations correlate with these broader patterns of population structure.

This integrated approach enables researchers to determine whether recombination events affecting mtgA have functional consequences that might contribute to the emergence of more virulent strains like E. coli O45:K1:H7 .

What are the most promising directions for developing targeted antibiotics against E. coli O45:K1 mtgA?

Development of targeted antibiotics against mtgA in pathogenic E. coli O45:K1 strains presents several promising research directions:

  • Structure-based drug design: Although the search results don't mention a crystal structure for E. coli O45:K1 mtgA specifically, structural information from homologous transglycosylases can guide computational docking studies to identify novel chemical scaffolds that bind to the enzyme's active site. Virtual screening of compound libraries followed by validation using the fluorometric continuous assay represents a cost-effective initial approach .

  • Natural product exploration: Several natural products inhibit transglycosylases through mechanisms distinct from moenomycin. Systematic screening of microbial extracts using the multi-well fluorometric assay can identify novel inhibitory compounds . Fractionation guided by bioactivity can isolate the active components for structure determination and optimization.

  • Allosteric inhibition strategy: Rather than targeting the conserved active site, researchers should explore potential allosteric sites specific to mtgA. Hydrogen-deuterium exchange mass spectrometry coupled with molecular dynamics simulations can identify these sites, which may offer greater selectivity.

  • Dual-targeting approaches: Compounds that simultaneously inhibit mtgA and other essential processes in E. coli O45:K1 may provide synergistic effects and reduce resistance development. Screening for molecules that inhibit both transglycosylase activity (measured by fluorometric assays ) and O45 antigen synthesis (which plays a crucial role in virulence ) represents a particularly promising direction.

  • Peptidoglycan substrate analogs: Designing non-hydrolyzable analogs of lipid II that competitively inhibit mtgA offers another approach. These analogs should incorporate the dansyl group at the third position of the pentapeptide, which prevents transpeptidation while maintaining binding to transglycosylases.

These research directions capitalize on the unique characteristics of mtgA and the O45:K1 strain, potentially leading to narrow-spectrum antibiotics with reduced impact on beneficial microbiota.

How might mtgA function differ across diverse bacterial populations and environments in the human microbiome?

Understanding how mtgA function varies across bacterial populations requires integration of comparative genomics with metagenomics and functional analyses:

  • Metagenomic profiling: Recent studies have revealed extensive strain-level variation in recombination rates within commensal gut bacteria . Researchers should use strain-resolved metagenomics to identify mtgA variants across human microbiome samples, correlating variants with host factors and microbial community structure.

  • Functional metagenomics: Cloning mtgA genes from metagenomic libraries into expression vectors, followed by high-throughput activity screening using fluorometric assays , can reveal functional diversity that may not be apparent from sequence analysis alone.

  • Environmental adaptation analysis: Comparative analysis of mtgA sequences from bacteria in different host environments (gut, skin, oral cavity) can identify environment-specific adaptations. These analyses should focus on both the catalytic domain and regions involved in protein-protein interactions with other cell wall synthesis machinery.

  • Host-microbe interaction studies: Investigation of how host factors (antimicrobial peptides, bile acids, immune components) affect mtgA expression and activity across different bacterial species. RNA sequencing of bacteria under various host-mimicking conditions can reveal differential regulation patterns.

  • Horizontal gene transfer monitoring: Given that horizontal acquisition of new genetic elements (like the O-antigen gene cluster in E. coli O45:K1:H7 ) can drive the emergence of new pathogenic strains, researchers should monitor recombination events affecting mtgA in longitudinal microbiome samples, especially following antibiotic treatment or pathogen exposure.

Research has shown that bacterial recombination in the human gut microbiome introduces >10-fold more variation than mutation . Understanding how this process affects functional diversity in enzymes like mtgA may provide insights into microbial adaptation and potential targets for microbiome modulation.

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