ATP-citrate lyase as a substrate of protein histidine phosphatase in vertebrates.
The first protein histidine phosphatase from vertebrates discovered recently was found in a variety of tissues, however, a physiological substrate protein was missing. Phosphorylation of liver extracts in the presence of EDTA, followed by SDS-PAGE and autoradiography showed labeling of three proteins. Acid- and alkaline-treatment revealed the existence of N-phosphates. Addition of histidine phosphatase exclusively resulted in dephosphorylation of a 110kDa protein (denaturing conditions). Gelfiltration revealed its native molecular mass of approximately 450kDa. That protein was purified and identified as ATP-citrate lyase. The results are in favor of histidine phosphatase playing an important yet unidentified role in metabolic processes.
Klumpp
Susanne
S
Institut für Pharmazeutische and Medizinische Chemie, Westfälische Wilhelms-Universität, Hittorfstr. 58-62, D-48149, Münster, Germany. klumpp@uni-muenster.de
Bechmann
Gunther
G
Mäurer
Anette
A
Selke
Dagmar
D
Krieglstein
Josef
J
D001275:ATP Citrate (pro-S)-Lyase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D006639:Histidine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity
D006639:Histidine; D001275:ATP Citrate (pro-S)-Lyase; D010749:Phosphoprotein Phosphatases; C005436:phosphohistidine