Disease relevance of Citryl-coenzyme A

• 2) Synthases from a Gram-negative prokaryote, E. coli, and from an archaebacterium, S. solfataricus, catalyse the reactions of citryl-CoA in kinetics of the Michaelis-Menten type [1].

High impact information on Citryl-coenzyme A

• Citryl-CoA lyase showed low citrate synthase (CS) activity [2].
• Citryl-CoA synthetase and SCS were homologous, but showed different substrate specificity [3].
• Over a broad temperature range, inadequate stabilization of the transition state for citryl-CoA hydrolysis renders this step nearly rate-limiting for the forward reaction of TpCS [4].
• Sequence analyses further suggest that ATP citrate lyase formed by a gene fusion of citryl-CoA synthetase and citryl-CoA lyase and subsequently became involved in a modified version of this pathway [5].
• Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase [6].

Biological context of Citryl-coenzyme A

• For D375E, the hydrolysis of citryl-CoA is rate determining [7].
• The kinetics of this partial reaction show symmetry to those of the citryl-CoA hydrolase reaction [8].
• We have identified a novel mammalian gene that shows significant amino acid sequence homology to the bacterial CitE gene product that is responsible for cleavage of citryl-CoA [9].

Associations of Citryl-coenzyme A with other chemical compounds

• Oxaloacetate inhibits the hydrolysis of citryl-CoA by the fragmented synthases (endoproteinase Lys-C, trypsin) competitively [10].
• Experiments performed with ATP citrate lyase and S-(3,4-dicarboxy-3-hydroxybutyl)-CoA are consistent with citryl-CoA but not with citryl-enzyme being the direct precursor of the products acetyl-CoA and oxaloacetate [11].
• Arguments are presented which indicate that the low steady-state rates of citrate production governing the catalytic interaction of citrate synthase from pig heart with citryl-CoA reflect the formation of a non-productive enzyme.citryl-CoA complex [12].

Gene context of Citryl-coenzyme A

• Mechanism of interaction of citrate synthase with citryl-CoA [12].
• Hysteretic behaviour of citrate synthase. Isotopically chiral citryl-CoA reveals increased number of reversals of the synthase condensation step under steady-state conditions [13].

References