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Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: Evidence for a metabolon

Paper ID Volume ID Publish Year Pages File Format Full-Text
31831 44842 2011 10 PDF Available
Title
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: Evidence for a metabolon
Abstract

The majority of all proteins of a living cell is active in complexes rather than in an isolated way. These protein–protein interactions are of high relevance for many biological functions. In addition to many well established protein complexes an increasing number of protein–protein interactions, which form rather transient complexes has recently been discovered. The formation of such complexes seems to be a common feature especially for metabolic pathways. In the Gram-positive model organism Bacillus subtilis, we identified a protein complex of three citric acid cycle enzymes. This complex consists of the citrate synthase, the isocitrate dehydrogenase, and the malate dehydrogenase. Moreover, fumarase and aconitase interact with malate dehydrogenase and with each other. These five enzymes catalyze sequential reaction of the TCA cycle. Thus, this interaction might be important for a direct transfer of intermediates of the TCA cycle and thus for elevated metabolic fluxes via substrate channeling. In addition, we discovered a link between the TCA cycle and gluconeogenesis through a flexible interaction of two proteins: the association between the malate dehydrogenase and phosphoenolpyruvate carboxykinase is directly controlled by the metabolic flux. The phosphoenolpyruvate carboxykinase links the TCA cycle with gluconeogenesis and is essential for B. subtilis growing on gluconeogenic carbon sources. Only under gluconeogenic growth conditions an interaction of these two proteins is detectable and disappears under glycolytic growth conditions.

Keywords
Protein–protein interaction; Metabolon; Substrate channeling; Krebs cycle; Gluconeogenesis
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Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: Evidence for a metabolon
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Publisher
Database: Elsevier - ScienceDirect
Journal: Metabolic Engineering - Volume 13, Issue 1, January 2011, Pages 18–27
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us