Adenylate kinase bound to the chromatophore membranes of Rhodobactor spheroides G1C.
Transformation of adenylates (AMP, ADP and ATP) by washed chromatophore membranes of Rhodobactor spheroides G1C in the dark and in the light indicated the functions of ATPase (ADP + Pi in equilibrium ATP) and of an adenylate kinase (2ADP in equilibrium AMP + ATP). The activity of adenylate kinase of the chromatophores was not inhibited by AP5A, and persisted even after sonication in the presence of EDTA or CaCl2; the results suggested the presence of an adenylate kinase bound to the chromatophore membrane. In search of the enzyme, the supernatant after sonication of the chromatophores in the presence of EDTA was subjected to a molecular sieve and then to ion-exchange HPLC; a fraction with high specific adenylate kinase activity, containing a very sharp peak at 55 kDa, was isolated. Preliminary characterization indicated that it is different from the well-documented water-soluble 33 kDa adenylate kinase.
Koyama
Y
Y
Nakano
T
T
Utsumi
H
H
Yamamoto
S
S
D000263:Adenylate Kinase / Q000378:metabolism*; D001419:Bacteria / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002856:Chromatophores / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D010770:Phosphotransferases / Q000378:metabolism*
D010770:Phosphotransferases; D000263:Adenylate Kinase