A novel Mammalian homologue of a bacterial citrate-metabolizing enzyme.
Mammals metabolize citrate to acetyl-CoA and oxaloacetate via the enzyme, ATP:citrate lyase. Bacteria lack this enzyme, but have the ability to cleave citrate in the form of citryl-CoA in an analogous manner using a structurally distinct enzyme. 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. We propose that this gene encodes an enzyme that catalyzes cleavage of substrates related to CoA esters of citrate or an analogous intermediary metabolite. The product of this novel gene may represent a component of an unknown metabolic pathway in mammals.
Söderberg
Charlotte
C
Pharmacology, Biovitrum AB, SE-112 76 Stockholm, Sweden.
Lind
Peter
P
D000595:Amino Acid Sequence; D000818:Animals; D019343:Citric Acid / Q000378:metabolism*; D006801:Humans; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D007652:Oxo-Acid-Lyases / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D019343:Citric Acid; D007652:Oxo-Acid-Lyases; C021536:malyl-CoA lyase; C110489:citryl-CoA lyase