Kinetic mechanism of argininosuccinate synthetase. Academic Article

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.

authors

• Raushel, Frank

published proceedings

• Arch Biochem Biophys

author list (cited authors)

• Raushel, F. M., & Seiglie, J. L.

citation count

• 20

complete list of authors

• Raushel, FM||Seiglie, JL

publication date

• January 1983

publisher

• Elsevier  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Adenosine Triphosphate
• Animals
• Argininosuccinate Synthase
• Aspartic Acid
• Cattle
• Citrulline
• Kinetics
• Ligases
• Liver
• Mathematics

Digital Object Identifier (DOI)

• 10.1016/0003-9861(83)90114-5

start page

• 979

end page

• 985

volume

• 225

issue

• 2

URL

• http://dx.doi.org/10.1016/0003-9861(83)90114-5