Interaction in vitro of scallop muscle arginine kinase with filamentous actin.
Scallop muscle arginine kinase binds to F-actin from mollusc and rabbit muscle in vitro. One site of interaction appears to be located in residues 305-325 of a C-terminal fragment (residues 285-375) of actin. The binding is hindered in the presence of arginine, Mg(2+)-ADP and NO3-, which form a dead-end complex with the enzyme. F-actin inhibits the enzyme activity non-competitively with respect to Mg(2+)-ATP. As a function of arginine concentration, the inhibition is of the mixed type, where Km is affected more than Vmax.
Reddy
S R
SR
Department of Zoology, University of Poona, Pune, India.
Houmeida
A
A
Benyamin
Y
Y
Roustan
C
C
D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001120:Arginine / Q000378:metabolism; D001122:Arginine Kinase / Q000378:metabolism*; D005454:Fluorescence Polarization; D007700:Kinetics; D008974:Mollusca; D009132:Muscles / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D001120:Arginine; D001122:Arginine Kinase