Histidine-phosphorylation of succinyl CoA synthetase from Trypanosoma brucei

Abstract The insect form of Trypanosoma brucei depends on respiration for its energy requirements. It contains a fully functional mitochondrion with a complete citric acid cycle. Most of its enyzmes have been characterized to date. The current study presents the characterization of the histidine phosphorylation activity of one of the few remaining enzymes, succinyl CoA synthetase. The trypanosomal enyzme was identified by partial purification, followed by direct protein sequencing. It is rapidly phosphorylated, presumably through auto-phosphorylation, using either ATP or GTP as phosphate donors. The phosphorylation occurs exclusively on histidine residues. The histidine-bound phosphate can be donated to suitable phosphate acceptors in a rapid reaction. This phosphotransfer reaction is highly nucleotide selective, as only ADP, but none of the other nucleoside-diphosphates tested, can be used as a phosphate acceptor.