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Literature summary for 3.2.1.67 extracted from

  • Drone, J.; Dion, M.; Tellier, C.; Rabiller, C.
    In vivo selection for the enhancement of Thermotoga maritima exopolygalacturonase activity at neutral pH and low temperature (2007), Protein Eng. Des. Sel., 20, 7-14.
    View publication on PubMed

Application

Application Comment Organism
analysis development of an Escherichia coli-based metabolic selection system for the uncovering of new oligogalacturonate-active enzymes. Based on the expression of the specific permease TogMNAB, this system enables the entry of oligogalacturonates into the cytoplasm of Escherichia coli thus providing a modified strain usable for this purpose. This tool is used for the metabolic selection of Thermotoga maritima exopolygalacturonase (TmGalU) mutants enabling the uptake of sodium trigalacturonate as the sole carbon source by the bacterium. In one round of error-prone PCR and selection, mutants of TmGalU with a 4fold increased turnover at pH 7.0 and 2fold more active at 37°C than wild-type enzyme are isolated Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
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Synonyms

Synonyms Comment Organism
exopolygalacturonase
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Thermotoga maritima
TmGalU
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Thermotoga maritima