Abstract
We characterized the activities of the Myxococcus xanthus ApaH-like phosphatases PrpA and ApaH, which share homologies with both phosphoprotein phosphatases and diadenosine tetraphosphate (Ap4A) hydrolases. PrpA exhibited a phosphatase activity towards p-nitrophenyl phosphate (pNPP), tyrosine phosphopeptide and tyrosine-phosphorylated protein, and a weak hydrolase activity towards ApnA and ATP. In the presence of Mn2+, PrpA hydrolyzed Ap4A into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzed Ap4A into two molecules of ADP. ApaH exhibited high phosphatase activity towards pNPP, and hydrolase activity towards ApnA and ATP. Mn2+ was required for ApaH-mediated pNPP dephosphorylation and ATP hydrolysis, whereas Co2+ was required for ApnA hydrolysis. Thus, PrpA and ApaH may function mainly as a tyrosine protein phosphatase and an ApnA hydrolase, respectively.
| Original language | English |
|---|---|
| Pages (from-to) | 3395-3402 |
| Number of pages | 8 |
| Journal | FEBS Letters |
| Volume | 588 |
| Issue number | 18 |
| DOIs | |
| Publication status | Published - Sep 17 2014 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus. / Sasaki, Masashi; Takegawa, Kaoru; Kimura, Yoshio.
In: FEBS Letters, Vol. 588, No. 18, 17.09.2014, p. 3395-3402.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus
AU - Sasaki, Masashi
AU - Takegawa, Kaoru
AU - Kimura, Yoshio
PY - 2014/9/17
Y1 - 2014/9/17
N2 - We characterized the activities of the Myxococcus xanthus ApaH-like phosphatases PrpA and ApaH, which share homologies with both phosphoprotein phosphatases and diadenosine tetraphosphate (Ap4A) hydrolases. PrpA exhibited a phosphatase activity towards p-nitrophenyl phosphate (pNPP), tyrosine phosphopeptide and tyrosine-phosphorylated protein, and a weak hydrolase activity towards ApnA and ATP. In the presence of Mn2+, PrpA hydrolyzed Ap4A into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzed Ap4A into two molecules of ADP. ApaH exhibited high phosphatase activity towards pNPP, and hydrolase activity towards ApnA and ATP. Mn2+ was required for ApaH-mediated pNPP dephosphorylation and ATP hydrolysis, whereas Co2+ was required for ApnA hydrolysis. Thus, PrpA and ApaH may function mainly as a tyrosine protein phosphatase and an ApnA hydrolase, respectively.
AB - We characterized the activities of the Myxococcus xanthus ApaH-like phosphatases PrpA and ApaH, which share homologies with both phosphoprotein phosphatases and diadenosine tetraphosphate (Ap4A) hydrolases. PrpA exhibited a phosphatase activity towards p-nitrophenyl phosphate (pNPP), tyrosine phosphopeptide and tyrosine-phosphorylated protein, and a weak hydrolase activity towards ApnA and ATP. In the presence of Mn2+, PrpA hydrolyzed Ap4A into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzed Ap4A into two molecules of ADP. ApaH exhibited high phosphatase activity towards pNPP, and hydrolase activity towards ApnA and ATP. Mn2+ was required for ApaH-mediated pNPP dephosphorylation and ATP hydrolysis, whereas Co2+ was required for ApnA hydrolysis. Thus, PrpA and ApaH may function mainly as a tyrosine protein phosphatase and an ApnA hydrolase, respectively.
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UR - http://www.scopus.com/inward/citedby.url?scp=84908681879&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2014.07.031
DO - 10.1016/j.febslet.2014.07.031
M3 - Article
C2 - 25107648
AN - SCOPUS:84908681879
VL - 588
SP - 3395
EP - 3402
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 18
ER -