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Literature summary for 7.2.2.21 extracted from

  • Wu, C.C.; Bal, N.; Perard, J.; Lowe, J.; Boscheron, C.; Mintz, E.; Catty, P.
    A cloned prokaryotic Cd2+ P-type ATPase increases yeast sensitivity to Cd2+ (2004), Biochem. Biophys. Res. Commun., 324, 1034-1040.
    View publication on PubMed

Application

Application Comment Organism
biotechnology expression of enzyme in Saccharomyces cerevisiae strikingly decreases Cd2+ tolerance of yeast cells. Yeast expressing the non-functional mutant D398A can grow on selective medium containing up to 0.1 mM Cd2+, while those expressing the intact enzyme cannot grow in presence of 0.001 mM Cd2+. Enzyme is localized in the endoplasmic reticulum, so hypersensitivity to Cd2+ is due to Cd2+ accumulation in the reticulum lumen. Zn2+ does not protect cells against Cd2+ poisoning Listeria monocytogenes

Protein Variants

Protein Variants Comment Organism
D398A no enzymic activity Listeria monocytogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum recombinant enzyme in Saccharomyces cerevisiae Listeria monocytogenes 5783
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Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
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expression in Saccharomyces cerevisiae
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