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Literature summary for 2.1.1.107 extracted from

  • Wang, Z.; Li, S.; Li, J.; Li, J.; Rong, L.; Cheng, B.; Fan, J.
    Engineering uroporphyrinogen III methyltransferase as a red fluorescent reporter in E. coli (2014), Enzyme Microb. Technol., 61-62, 1-6 .
    View publication on PubMed

Application

Application Comment Organism
analysis uroporphyrinogen III methyltransferase (UMT) is a reporter owing to the catalytic products in the cells that emit strong red fluorescence under UV light. The gene encoding the functional barley UMT (bUMT) is engineered by error-prone PCR and the application of UMT as a red fluorescent reporter in Escherichia coli is broadened. A variant, termed mbUMT, is selected and emitts stronger cell fluorescence than the wild type bUMT expressed in different Escherichia coli strains, under different promoters and induction conditions respectively. The constructed mbUMT with a C-terminal ssrA tag is degraded in cells by the protease ClpXP encoded by Escherichia coli chromosome, whereas the bUMT is expressed as active aggregates. Before they are exported to the periplasm, both proteins catalyze the substrate in the cytoplasm and emit cell fluorescence. The results suggest that the evolved bUMT is a better candidate to monitor in vivo degradation by Escherichia coli ClpXP Hordeum vulgare

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hordeum vulgare

Organism

Organism UniProt Comment Textmining
Hordeum vulgare F2CPW6
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Source Tissue

Source Tissue Comment Organism Textmining
seedling leaves Hordeum vulgare
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Synonyms

Synonyms Comment Organism
uroporphyrinogen III methyltransferase
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Hordeum vulgare