Kinetic mechanism of bovine liver argininosuccinate lyase. Academic Article

abstract

• The kinetic mechanism of bovine liver argininosuccinate lyase has been determined at pH 7.5, 25 degrees C. Fumarate and arginine are both noncompetitive inhibitors versus argininosuccinate. The dead-end inhibitor, succinate, is competitive versus fumarate and argininosuccinate, but noncompetitive versus arginine. Citrulline is competitive versus arginine and noncompetitive versus argininosuccinate and fumarate. The results are consistent with a random mechanism with the formation of two dead-end complexes: E . argininosuccinate . fumarate and E . argininosuccinate . arginine. No evidence was obtained for nonlinear reciprocal plots. The equilibrium constant was found to be 3.7 mM.

authors

• Raushel, Frank

published proceedings

• Arch Biochem Biophys

author list (cited authors)

• Raushel, F. M., & Nygaard, R.

citation count

• 18

complete list of authors

• Raushel, FM||Nygaard, R

publication date

• January 1983

publisher

• Elsevier  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Animals
• Arginine
• Argininosuccinate Lyase
• Cattle
• Fumarates
• Hydrogen-Ion Concentration
• Kinetics
• Liver
• Lyases
• Substrate Specificity

Digital Object Identifier (DOI)

• 10.1016/0003-9861(83)90130-3

start page

• 143

end page

• 147

volume

• 221

issue

• 1

URL

• http://dx.doi.org/10.1016/0003-9861(83)90130-3