Identification of the kinetic mechanism of succinyl-CoA synthetase

Biosci Rep. 2013 Jan 18;33(1):145-63. doi: 10.1042/BSR20120069.

Abstract

The kinetic mechanism of SCS [succinyl-CoA (coenzyme A) synthetase], which participates in the TCA (tricarboxylic acid) cycle, ketone body metabolism and haem biosynthesis, has not been fully characterized. Namely, a representative catalytic mechanism and associated kinetic parameters that can explain data on the enzyme-catalysed reaction kinetics have not been established. To determine an accurate model, a set of putative mechanisms of SCS, proposed by previous researchers, were tested against experimental data (from previous publication) on SCS derived from porcine myocardium. Based on comparisons between model simulation and the experimental data, an ordered ter-ter mechanism with dead-end product inhibition of succinate against succinyl-CoA is determined to be the best candidate mechanism. A thermodynamically constrained set of parameter values is identified for this candidate mechanism.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acyl Coenzyme A / chemistry*
  • Animals
  • Computer Simulation
  • Enzyme Stability
  • Kinetics
  • Myocardium / enzymology
  • Osmolar Concentration
  • Phosphorylation
  • Protein Binding
  • Sensitivity and Specificity
  • Succinate-CoA Ligases / chemistry*
  • Succinic Acid / chemistry*
  • Swine
  • Thermodynamics

Substances

  • Acyl Coenzyme A
  • Succinic Acid
  • succinyl-coenzyme A
  • Succinate-CoA Ligases