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- W2778594603 abstract "Almost all organic compounds which construct life are derived from carbon dioxide (CO2) assimilated by autotrophic organisms. The reductive tricarboxylic acid (RTCA) cycle functions as a carbon dioxide fixation pathway, distinct from Calvin cycle, in a green sulfur bacterium Chlorobium limicola. ATP-citrate lyase (ACL) is one of the key enzymes of this cycle. The enzyme of C.limicola (Cl-ACL) was encoded in two adjacent open reading frames, aclB (1197 bp) and aclA (1827bp), whose products showed significant similarity to the N- and C-terminal regions of the human enzyme, respectively. Heterologous expression of these genes in Escherichia coli proved that both gene products were essential for ACL activity. Kinetic examination of the enzyme revealed that the enzyme displayed typical Michaelis-Menten kinetics toward ATP with an apparent Km value of 0.19mM. However, strong negative cooperativity was observed with respect to citrate binding. ADP was a competitive inhibitor of ATP with a Kt value of 0.036mM. Together with the feature that the enzyme catalyzed the reaction only in the direction of citrate cleavage, these kinetic properties indicated that Cl-ACL can regulate both the direction and carbon flux of the RTCA cycle in C.limicola." @default.
- W2778594603 created "2018-01-05" @default.
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- W2778594603 date "2005-01-01" @default.
- W2778594603 modified "2023-09-28" @default.
- W2778594603 title "ATP-citrate lyase; the key enzyme of the reductive TCA cycle" @default.
- W2778594603 hasPublicationYear "2005" @default.
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