Premium
Acylphosphate formation by the Menkes copper ATPase
Author(s) -
Solioz Marc,
Camakaris James
Publication year - 1997
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/s0014-5793(97)00770-9
Subject(s) - menkes disease , atpase , chinese hamster ovary cell , copper , p type atpase , atp7a , golgi apparatus , chemistry , biology , enzyme , biochemistry , kinetics , hamster , microbiology and biotechnology , copper metabolism , cell , receptor , organic chemistry , physics , quantum mechanics
The Menkes ATPase is the product of the MNK gene, defective in some inherited human disorders of copper metabolism. We here show the formation of an acylphosphate intermediate by the murine MNK homologue in membranes from normal and copper resistant Chinese hamster ovary cells. In the latter, fivefold higher levels of acylphosphate were formed. Challenging these cells with copper, which induces relocation of the MNK ATPase from the trans ‐Golgi network to the plasma membrane, did not influence acylphosphate formation. The kinetics of phosphorylation, metal dependence, and sensitivity to inhibitors were investigated. The results show that the MNK ATPase is an active P‐type ATPase and provide a direct functional test for this enzyme.