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Enzymatic characteristics of an ApaH‐like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus
Author(s) -
Sasaki Masashi,
Takegawa Kaoru,
Kimura Yoshio
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.07.031
Subject(s) - hydrolase , phosphatase , dephosphorylation , myxococcus xanthus , biochemistry , phosphorylation , tyrosine , enzyme , hydrolysis , chemistry , biology , mutant , gene
We characterized the activities of the Myxococcus xanthus ApaH‐like phosphatases PrpA and ApaH, which share homologies with both phosphoprotein phosphatases and diadenosine tetraphosphate (Ap 4 A) hydrolases. PrpA exhibited a phosphatase activity towards p ‐nitrophenyl phosphate ( p NPP), tyrosine phosphopeptide and tyrosine‐phosphorylated protein, and a weak hydrolase activity towards Ap n A and ATP. In the presence of Mn 2+ , PrpA hydrolyzed Ap 4 A into AMP and ATP, whereas in the presence of Co 2+ PrpA hydrolyzed Ap 4 A into two molecules of ADP. ApaH exhibited high phosphatase activity towards p NPP, and hydrolase activity towards Ap n A and ATP. Mn 2+ was required for ApaH‐mediated p NPP dephosphorylation and ATP hydrolysis, whereas Co 2+ was required for Ap n A hydrolysis. Thus, PrpA and ApaH may function mainly as a tyrosine protein phosphatase and an Ap n A hydrolase, respectively.