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A Novel Mammalian Homologue of a Bacterial Citrate‐Metabolizing Enzyme
Author(s) -
SÖDERBERG CHARLOTTE,
LIND PETER
Publication year - 2002
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2002.tb04305.x
Subject(s) - atp citrate lyase , citrate synthase , enzyme , biochemistry , gene , metabolite , lyase , homology (biology) , biology , bacteria , gene product , cleavage (geology) , amino acid , cleave , chemistry , gene expression , genetics , paleontology , fracture (geology)
A bstract : 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.