Related Experiment Video
Updated: Sep 30, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
A novel Mammalian homologue of a bacterial citrate-metabolizing enzyme
Charlotte Söderberg1, Peter Lind
1Pharmacology, Biovitrum AB, SE-112 76 Stockholm, Sweden.
Abstract:
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.
More Related Videos
Related Concept Videos
The Citric Acid Cycle
The Citric Acid Cycle: Output
Regulation of Citric Acid Cycle
The citric acid cycle is regulated in several ways, including feedback inhibition, regulation of enzyme activities, and associated anaplerotic or cataplerotic pathways.
The primary substrate of the TCA cycle—acetyl CoA—is produced by the...
The Citric Acid Cycle: Overview
The citric...
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Amino Acid Catabolism
Structure of Porins

