Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store

Caulobacter crescentus CB15 Pathway: glyoxylate cycle
Inferred by computational analysis

Pathway diagram: glyoxylate cycle

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Synonyms: glyoxylate bypass, glyoxylate shunt

Superclasses: Generation of Precursor Metabolites and Energy

Pathway Summary from MetaCyc:
The glyoxylate cycle is a sequence of anaplerotic reactions (reactions that form metabolic intermediates for biosynthesis) that enables an organism to use substrates that enter central carbon metabolism at the level of acetyl-CoA as the sole carbon source. Such substrates include fatty acids, alcohols, and esters (often the products of fermentation), as well as waxes, alkenes, and methylated compounds. The pathway does not occur in vertebrates, but it is found in plants and certain bacteria, fungi, and invertebrates.

The pathway is essentially a modified version of the TCA cycle I (prokaryotic) that bypasses those steps in the cycle that lead to a loss of CO2. Acetyl-CoA enters the cycle at two steps, but no carbon escapes it in the form of CO2.

The glyoxylate cycle uses a two-step bypass. One key enzyme, isocitrate lyase (EC, converts D-threo-isocitrate to form succinate and glyoxylate. A second key enzyme, malate synthase (EC, condenses glyoxylate and a second molecule of acetyl-CoA to form (S)-malate. The subsequent oxidation of malate regenerates the initial acetyl-CoA acceptor molecule of the TCA cycle, oxaloacetate. Thus, the succinate that was formed by isocitrate lyase (EC can be withdrawn from the cycle and used for cell carbon biosynthesis.

The pathway was originally discovered in bacteria [Kornberg57], but later was found to operate in some eukaryotic organisms as well. In plants the cycle is invovled in the metabolism of storage oils during germination of seeds [Brownleader97a]. The cycle also operates in developing eggs of nematodes, where it converts triacylglycerols to carbohydrates [Patel78].

In Escherichia coli the pathway is active when growth on 2 carbon compounds requires conservation of 4 carbon TCA intermediates. Two acetyl-CoA are taken up per turn. The glyoxylate cycle is repressed during growth on glucose and induced by growth on acetate [Cortay89, Walsh84, LaPorte84, Nimmo84].

It should be notes that some organisms possess alternative pathways that convert acetyl-CoA to 4 carbon biosynthetic intermediates, such as the ethylmalonyl-CoA pathway and the methylaspartate cycle.

Superpathways: superpathway of glyoxylate bypass and TCA

Pathway Evidence Glyph:

Pathway evidence glyph

This organism is in the expected taxonomic range for this pathway.

Key to pathway glyph edge colors:

  An enzyme catalyzing this reaction is present in this organism
  The reaction is unique to this pathway in MetaCyc

Revised 04-Dec-2007 by SRI International


Brownleader97a: Brownleader, M.D., Harborne, J.B., Dey, P.M. (1997). "Carbohydrate metabolism: primary metabolism of monosaccharides." Plant Biochemistry, Eds Dey & Harborne, Academic Press, Harcourt Brace & Co, Publishers, London.

Cortay89: Cortay JC, Bleicher F, Duclos B, Cenatiempo Y, Gautier C, Prato JL, Cozzone AJ (1989). "Utilization of acetate in Escherichia coli: structural organization and differential expression of the ace operon." Biochimie 71(9-10):1043-1049. PMID: 2512996

Kornberg57: Kornberg, HL, Krebs, HA (1957). "Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle." Nature 179(4568);988-91. PMID: 13430766

LaPorte84: LaPorte DC, Walsh K, Koshland DE (1984). "The branch point effect. Ultrasensitivity and subsensitivity to metabolic control." J Biol Chem 1984;259(22);14068-75. PMID: 6389540

Nimmo84: Nimmo GA, Nimmo HG (1984). "The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase." Eur J Biochem 1984;141(2);409-14. PMID: 6329757

Patel78: Patel TR, McFadden BA (1978). "Caenorhabditis elegans and Ascaris suum: fragmentation of isocitrate lyase in crude extracts." Exp Parasitol 44(1);72-81. PMID: 627278

Walsh84: Walsh K, Koshland DE (1984). "Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt." J Biol Chem 1984;259(15);9646-54. PMID: 6378912

Report Errors or Provide Feedback
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue May 3, 2016, biocyc14.