Difference between revisions of "Phosphatase Subfamily Acr2"

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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_II|Superfamily Cys-based II]]: [[Phosphatase_Family_CDC25|Family CDC25]]: [[Subfamily_Acr2|Subfamily Acr2]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_II|Superfamily Cys-based II]]: [[Phosphatase_Family_CDC25|Family CDC25]]: [[Subfamily_Acr2|Subfamily Acr2]]
  
=== Arsenate Reductase ===
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Prokaryotes and eukaryotes use arsenate reductases of distinct folds. ''E. coli'' uses ArsC, which belongs to [[Phosphatase_Superfamily_Cys-based_III|Superfamily Cys-based III]], the same as [[Phosphatase_Family_LMWPTP|LMWPTP]] and [[Phosphatase_Family_SSU72|SSU72]]. Eukaryotes, particularly fungi, plants and protists, use ACR2 which have the same fold as [[Phosphatase_Family_CDC25|CDC25]] <cite>yeo09</cite>.
Prokaryotes and eukaryotes use arsenate reductases of distinct folds. ''E. coli'' uses ArsC, which belongs to [[Phosphatase_Superfamily_Cys-based_III|Superfamily Cys-based III]], the same as [[Phosphatase_Family_LMWPTP|LMWPTP]] and [[Phosphatase_Family_SSU72|SSU72]]. In eukaryotes, particularly fungi, plants and protists, ACR2 exhibit arsenate reductase activity <cite>yeo09</cite>
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=== Arc2 as Arsenate Reductase ===
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=== Arc2 as arsenate reductase in eukaryotes ===
The ACR2 gene of ''Saccharomyces cerevisiae'' overexpressed in ''E. coli'' was shown to exhibit arsenate reductase activity and complement the arsenate-sensitive phenotype of an arsC deletion in ''E. coli'' <cite>yeast98 yeast00</cite>.
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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>.
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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 ===
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#yeast98 pmid=9812373
 
#yeast98 pmid=9812373
 
#yeast00 pmid=10801893
 
#yeast00 pmid=10801893
 +
#fern06 pmid=16766666
 
</biblio>
 
</biblio>

Revision as of 16:03, 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

  1. Yeo HK and Lee JY. Crystal structure of Saccharomyces cerevisiae Ygr203w, a homolog of single-domain rhodanese and Cdc25 phosphatase catalytic domain. Proteins. 2009 Aug 1;76(2):520-4. DOI:10.1002/prot.22420 | PubMed ID:19382206 | HubMed [yeo09]
  2. Mukhopadhyay R and Rosen BP. Saccharomyces cerevisiae ACR2 gene encodes an arsenate reductase. FEMS Microbiol Lett. 1998 Nov 1;168(1):127-36. DOI:10.1111/j.1574-6968.1998.tb13265.x | PubMed ID:9812373 | HubMed [yeast98]
  3. Mukhopadhyay R, Shi J, and Rosen BP. Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase. J Biol Chem. 2000 Jul 14;275(28):21149-57. DOI:10.1074/jbc.M910401199 | PubMed ID:10801893 | HubMed [yeast00]
  4. Ellis DR, Gumaelius L, Indriolo E, Pickering IJ, Banks JA, and Salt DE. A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris vittata. Plant Physiol. 2006 Aug;141(4):1544-54. DOI:10.1104/pp.106.084079 | PubMed ID:16766666 | HubMed [fern06]
All Medline abstracts: PubMed | HubMed