Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.50 extracted from

  • Makhoba, X.; Burger, A.; Coertzen, D.; Zininga, T.; Birkholtz, L.; Shonhai, A.
    Use of a chimeric Hsp70 to enhance the quality of recombinant Plasmodium falciparum S-adenosylmethionine decarboxylase protein produced in Escherichia coli (2016), PLoS ONE, 11, e0152626 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis coexpression of S-adenosylmethionine decarboxylase with chimeric protein KPf, which is made up of the ATPase domain of Escherichia coli DnaK and the substrate binding domain of Plasmodium falciparum Hsp70, and DnaK in Escherichia coli cells. The recombinant protein exhibits improved activity compared to protein coexpressed with overexpressed DnaK Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum A0A1D3TG90
-
-