Difference between revisions of "Phosphatase Family ArsC"
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| − | [[Phosphatase classification|Phosphatase Classification]]: [[ | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]: [[Phosphatase_Family_ArsC|Family ArsC]] |
Arsenate reductase (ArsC) <cite>Bennett</cite>, is only found in prokaryotes. While known to reduce arsenate to arsenite (a similar reaction to the phosphatase reaction), the B. subtilis gene also has in vitro phosphatase activity. | Arsenate reductase (ArsC) <cite>Bennett</cite>, is only found in prokaryotes. While known to reduce arsenate to arsenite (a similar reaction to the phosphatase reaction), the B. subtilis gene also has in vitro phosphatase activity. | ||
| − | Eukaryotes (particularly fungi, plants and protists) have different arsenate reductase, [[Subfamily_Acr2|Acr2]] of [[ | + | Eukaryotes (particularly fungi, plants and protists) have different arsenate reductase, [[Subfamily_Acr2|Acr2]] of [[Phosphatase_Superfamily_CC3|CC3 superfamily]] <cite>yeo09</cite>. |
== Reference == | == Reference == | ||
<biblio> | <biblio> | ||
#Bennett pmid=11698660 | #Bennett pmid=11698660 | ||
| + | #yeo09 pmid=19382206 | ||
</biblio> | </biblio> | ||
Latest revision as of 20:31, 6 December 2014
Phosphatase Classification: Superfamily CC2: Family ArsC
Arsenate reductase (ArsC) [1], is only found in prokaryotes. While known to reduce arsenate to arsenite (a similar reaction to the phosphatase reaction), the B. subtilis gene also has in vitro phosphatase activity.
Eukaryotes (particularly fungi, plants and protists) have different arsenate reductase, Acr2 of CC3 superfamily [2].
Reference
- Bennett MS, Guan Z, Laurberg M, and Su XD. Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13577-82. DOI:10.1073/pnas.241397198 |
- 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 |
