KINETIC MECHANISM OF ARGININOSUCCINATE SYNTHETASE | Academic Article individual record
abstract

The kinetic mechanism of bovine liver argininosuccinate synthetase has been determined at pH 7.5. The initial velocity and product and dead-end inhibition patterns are consistent with the ordered addition of MgATP, citrulline, and aspartate, followed by the ordered release of argininosuccinate, MgPPi, and AMP. The mechanism is also in accord with the formation of citrulline-adenylate as a reactive intermediate [O. Rochovansky, and S. Ratner, (1967) J. Biol. Chem. 242, 3839-3849]. No evidence was obtained for nonlinear double-reciprocal plots with any of the three substrates.

author list (cited authors)
RAUSHEL, F. M., & SEIGLIE, J. L.
publication date
1983
publisher
Elsevier bv Publisher
keywords
  • Liver
  • Adenosine Triphosphate
  • Citrulline
  • Argininosuccinate Synthase
  • Aspartic Acid
  • Mathematics
  • Cattle
  • Kinetics
  • Animals
  • Ligases
citation count

16