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EcoSal Plus

Domain 3:

Metabolism

Tricarboxylic Acid Cycle and Glyoxylate Bypass

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  • Authors: John E. Cronan, Jr.1, and David Laporte2
  • Editor: Valley Stewart3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Departments of Microbiology and Biochemistry, University of Illinois, Urbana, IL 61801; 2: Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN 55455; 3: University of California, Davis, Davis, CA
  • Received 19 April 2006 Accepted 28 June 2006 Published 11 September 2006
  • Address correspondence to John E. Cronan, Jr. j-cronan@life.uiuc.edu
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  • Abstract:

    The tricarboxylic acid (TCA) cycle plays two essential roles in metabolism. First, under aerobic conditions the cycle is responsible for the total oxidation of acetyl-CoA that is derived mainly from the pyruvate produced by glycolysis. Second, TCA cycle intermediates are required in the biosynthesis of several amino acids. Although the TCA cycle has long been considered a “housekeeping” pathway in and , the pathway is highly regulated at the transcriptional level. Much of this control is exerted in response to respiratory conditions. The TCA cycle gene-protein relationship and mutant phenotypes have been well studied, although a few loose ends remain. The realization that a “shadow” TCA cycle exists that proceeds through methylcitrate has cleared up prior ambiguities. The glyoxylate bypass has long been known to be essential for growth on carbon sources such as acetate or fatty acids because this pathway allowsnet conversion of acetyl-CoA to metabolic intermediates. Strains lacking this pathway fail to grow on these carbon sources, since acetate carbon entering the TCA cycle is quantitatively lost as CO resulting in the lack of a means to replenish the dicarboxylic acids consumed in amino acid biosynthesis. The TCA cycle gene-protein relationship and mutant phenotypes have been well studied, although the identity of the small molecule ligand that modulates transcriptional control of the glyoxylate cycle genes by binding to the IclR repressor remains unknown. The activity of the cycle is also exerted at the enzyme level by the reversible phosphorylation of the TCA cycle enzyme isocitrate dehydrogenase catalyzed by a specific kinase/phosphatase to allow isocitratelyase to compete for isocitrate and cleave this intermediate to glyoxylate and succinate.

  • Citation: Cronan, Jr. J, Laporte D. 2006. Tricarboxylic Acid Cycle and Glyoxylate Bypass, EcoSal Plus 2006; doi:10.1128/ecosalplus.3.5.2

Key Concept Ranking

Gene Expression and Regulation
0.49983478
Lipoic Acid Synthesis
0.47443378
Amino Acid Addition
0.45074612
Fatty Acid Degradation
0.44565102
0.49983478

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ecosalplus.3.5.2.citations
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content/journal/ecosalplus/10.1128/ecosalplus.3.5.2
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/content/journal/ecosalplus/10.1128/ecosalplus.3.5.2
2006-09-11
2017-03-30

Abstract:

The tricarboxylic acid (TCA) cycle plays two essential roles in metabolism. First, under aerobic conditions the cycle is responsible for the total oxidation of acetyl-CoA that is derived mainly from the pyruvate produced by glycolysis. Second, TCA cycle intermediates are required in the biosynthesis of several amino acids. Although the TCA cycle has long been considered a “housekeeping” pathway in and , the pathway is highly regulated at the transcriptional level. Much of this control is exerted in response to respiratory conditions. The TCA cycle gene-protein relationship and mutant phenotypes have been well studied, although a few loose ends remain. The realization that a “shadow” TCA cycle exists that proceeds through methylcitrate has cleared up prior ambiguities. The glyoxylate bypass has long been known to be essential for growth on carbon sources such as acetate or fatty acids because this pathway allowsnet conversion of acetyl-CoA to metabolic intermediates. Strains lacking this pathway fail to grow on these carbon sources, since acetate carbon entering the TCA cycle is quantitatively lost as CO resulting in the lack of a means to replenish the dicarboxylic acids consumed in amino acid biosynthesis. The TCA cycle gene-protein relationship and mutant phenotypes have been well studied, although the identity of the small molecule ligand that modulates transcriptional control of the glyoxylate cycle genes by binding to the IclR repressor remains unknown. The activity of the cycle is also exerted at the enzyme level by the reversible phosphorylation of the TCA cycle enzyme isocitrate dehydrogenase catalyzed by a specific kinase/phosphatase to allow isocitratelyase to compete for isocitrate and cleave this intermediate to glyoxylate and succinate.

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Figures

Image of Figure 1
Figure 1

The glyoxylate bypass is composed of isocitrate lyase and malate synthase. IDH and IDH-P indicate the dephosphorylated and phosphorylated forms of isocitrate dehydrogenase, respectively.

Citation: Cronan, Jr. J, Laporte D. 2006. Tricarboxylic Acid Cycle and Glyoxylate Bypass, EcoSal Plus 2006; doi:10.1128/ecosalplus.3.5.2
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Figure 2

The oxidative branch is to the right, and the reductive branch is to the left.

Citation: Cronan, Jr. J, Laporte D. 2006. Tricarboxylic Acid Cycle and Glyoxylate Bypass, EcoSal Plus 2006; doi:10.1128/ecosalplus.3.5.2
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Figure 3

Citation: Cronan, Jr. J, Laporte D. 2006. Tricarboxylic Acid Cycle and Glyoxylate Bypass, EcoSal Plus 2006; doi:10.1128/ecosalplus.3.5.2
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Image of Figure 4
Figure 4

Malate synthase, isocitrate lyase, and IDH kinase/phosphatase are encoded by , , and . These genes are transcribed from a single promoter upstream of .

Citation: Cronan, Jr. J, Laporte D. 2006. Tricarboxylic Acid Cycle and Glyoxylate Bypass, EcoSal Plus 2006; doi:10.1128/ecosalplus.3.5.2
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Tables

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Table 1

Genes and enzymes

Citation: Cronan, Jr. J, Laporte D. 2006. Tricarboxylic Acid Cycle and Glyoxylate Bypass, EcoSal Plus 2006; doi:10.1128/ecosalplus.3.5.2

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