Recombinant Shewanella sediminis Methionyl-tRNA formyltransferase (fmt)
Description
Enzyme Function and Biological Role
Fmt attaches a formyl group from 10-formyldihydrofolate (10-CHO-DHF) or 10-formyltetrahydrofolate (10-CHO-THF) to the amino group of methionyl-tRNA<sup>fMet</sup>, producing formylmethionyl-tRNA<sup>fMet</sup> (fMet-tRNA<sup>fMet</sup>) . This process is essential for:
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Translation initiation: The formyl group acts as a recognition signal for initiation factor IF2 in bacteria .
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Antibiotic targeting: Fmt is absent in humans, making it a potential target for antibacterial drugs like trimethoprim (TMP) .
Source Organism: Shewanella sediminis
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Characteristics:
Recombinant Protein Production
Recombinant Fmt from S. sediminis is produced via genetic engineering, with key details from product datasheets :
| Parameter | Details |
|---|---|
| Product Code | CSB-MP015150STR (purified protein) / CSB-EP015150STR-B (E. coli-expressed) |
| Storage | -20°C; addition of 5–50% glycerol recommended for long-term stability |
| Purity | >85% (verified by SDS-PAGE) |
| Amino Acid Sequence | 270 residues: MKPLNIIFAGTPDFAARHLQALIDSEHNIIGVYSQPDRP...KKPLSVGDIL |
Research Applications
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Antibiotic development: Studies on Fmt inhibitors aim to combat bacterial resistance .
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Mitochondrial translation studies: Human mitochondrial Fmt homologs linked to Leigh syndrome provide insights into metabolic disorders .
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Enzyme engineering: Heterologous expression in E. coli enables functional studies and high-yield production .
Key Research Findings
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In vivo validation: FolD-deficient S. sediminis strains exhibit impaired folate metabolism, corroborating Fmt’s reliance on 10-CHO-THF .
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Biochemical assays: LC-MS/MS confirmed dihydrofolate (DHF) as a by-product of Fmt activity with 10-CHO-DHF .
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Mutational analysis: Residues critical for formylation (e.g., Ser-125, Ser-209 in human homologs) inform mechanistic models .
Product Specs
Target Background
KEGG: sse:Ssed_0034
STRING: 425104.Ssed_0034
