Difference between revisions of "Phosphatase Subfamily Acr2"
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''Saccharomyces cerevisiae''. Overexpressed in ''E. coli'', the ACR2 gene of ''Saccharomyces cerevisiae'' (ScACR2) was shown to exhibit arsenate reductase activity and complement the arsenate-sensitive phenotype of an arsC deletion in ''E. coli'' <cite>yeast98 yeast00</cite>. | ''Saccharomyces cerevisiae''. Overexpressed in ''E. coli'', the ACR2 gene of ''Saccharomyces cerevisiae'' (ScACR2) was shown to exhibit arsenate reductase activity and complement the arsenate-sensitive phenotype of an arsC deletion in ''E. coli'' <cite>yeast98 yeast00</cite>. | ||
| − | Fern | + | Fern ''Pteris vittata''. The ACR2 of "Pteris vittata" (PvACR2) can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (''Saccharomyces cerevisiae'') lacking the arsenate reductase gene ACR2 <cite>fern06</cite>. PvACR2 is unique in that the arginine of catalytic motif Cx5R, previously shown to be essential for phosphatase and reductase activity, is replaced with a serine. |
=== Reference === | === Reference === | ||
Revision as of 16:06, 27 May 2014
Phosphatase Classification: Superfamily Cys-based II: Family CDC25: Subfamily Acr2
Prokaryotes and eukaryotes use arsenate reductases of distinct folds. E. coli uses ArsC, which belongs to Superfamily Cys-based III, the same as LMWPTP and SSU72. Eukaryotes, particularly fungi, plants and protists, use ACR2 which have the same fold as CDC25 [1].
Arc2 as arsenate reductase in eukaryotes
Saccharomyces cerevisiae. Overexpressed in E. coli, the ACR2 gene of Saccharomyces cerevisiae (ScACR2) was shown to exhibit arsenate reductase activity and complement the arsenate-sensitive phenotype of an arsC deletion in E. coli [2, 3].
Fern Pteris vittata. The ACR2 of "Pteris vittata" (PvACR2) can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (Saccharomyces cerevisiae) lacking the arsenate reductase gene ACR2 [4]. PvACR2 is unique in that the arginine of catalytic motif Cx5R, previously shown to be essential for phosphatase and reductase activity, is replaced with a serine.
Reference
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