MetaCyc Pathway: acetaldehyde biosynthesis II
Inferred from experiment

Pathway diagram: acetaldehyde biosynthesis II

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Synonyms: PDH-bypass, ligt-dark transition acetaldehyde biosynthesis

Superclasses: BiosynthesisCarbohydrates BiosynthesisAcetaldehyde Biosynthesis
BiosynthesisSecondary Metabolites Biosynthesis

Some taxa known to possess this pathway include : Populus deltoides

Expected Taxonomic Range: Viridiplantae

Acetaldehyde is released by plants into the atmosphere after a wide variety of stresses. Acetaldehyde is a potent antibiotic and its emission from damaged tissue may help prevent infections [Utama02] and activate the expression of plant defense genes [Tadege98]. Enhanced acetaldehyde emissions have been observed following mechanical wounding, desiccation, freeze-thaw events, herbivore attack, ozone fumigation, high light, high temperature, and many other biotic and abiotic stresses.

Since acetaldehyde is reactive in the atmosphere, its emisions is of interest to atmospheric chemists, who are not able to account for large amounts of biogenic acetaldehyde [Jardine09].

Two models that explain the biosynthesis of acetaldehyde have been proposed. According to the model depicted here, which is related to light-dark transition, acetaldehyde is produced as a correction for imbalance in the cytosolic and mitochondrial pyruvate concentrations. This pathway premises on the hypothesis that the acetaldehyde is synthesized in the leaf itself by the action of tissue localized pyruvate decarboxylase, which is usually present in the leaf veins and petioles [Nguyen09].

Variants: acetaldehyde biosynthesis I

Created 16-Sep-2009 by Pujar A, Boyce Thompson Institute


Jardine09: Jardine K, Karl T, Lerdau M, Harley P, Guenther A, Mak JE (2009). "Carbon isotope analysis of acetaldehyde emitted from leaves following mechanical stress and anoxia." Plant Biol (Stuttg) 11(4);591-7. PMID: 19538397

Kimmerer87: Kimmerer TW (1987). "Alcohol Dehydrogenase and Pyruvate Decarboxylase Activity in Leaves and Roots of Eastern Cottonwood (Populus deltoides Bartr.) and Soybean (Glycine max L.)." Plant Physiol 84(4);1210-1213. PMID: 16665586

Kimmerer88: Kimmerer TW, Stringer MA (1988). "Alcohol Dehydrogenase and Ethanol in the Stems of Trees : Evidence for Anaerobic Metabolism in the Vascular Cambium." Plant Physiol 87(3);693-697. PMID: 16666209

Nguyen09: Nguyen T, Drotar AM, Monson RK, Fall R (2009). "A high affinity pyruvate decarboxylase is present in cottonwood leaf veins and petioles: a second source of leaf acetaldehyde emission?." Phytochemistry 70(10);1217-21. PMID: 19698964

Tadege98: Tadege M, Bucher M, Stahli W, Suter M, Dupuis I, Kuhlemeier C (1998). "Activation of plant defense responses and sugar efflux by expression of pyruvate decarboxylase in potato leaves." The Plant Journal 16(6);661-671.

Utama02: Utama IM, Wills RB, Ben-Yehoshua S, Kuek C (2002). "In vitro efficacy of plant volatiles for inhibiting the growth of fruit and vegetable decay microorganisms." J Agric Food Chem 50(22);6371-7. PMID: 12381119

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Catalanotti12: Catalanotti C, Dubini A, Subramanian V, Yang W, Magneschi L, Mus F, Seibert M, Posewitz MC, Grossman AR (2012). "Altered fermentative metabolism in Chlamydomonas reinhardtii mutants lacking pyruvate formate lyase and both pyruvate formate lyase and alcohol dehydrogenase." Plant Cell 24(2);692-707. PMID: 22353371

Chae11: Chae, Lee (2011). "The functional annotation of protein sequences was performed by the in-house Ensemble Enzyme Prediction Pipeline (E2P2, version 1.0). E2P2 systematically integrates results from three molecular function annotation algorithms using an ensemble classification scheme. For a given genome, all protein sequences are submitted as individual queries against the base-level annotation methods. The individual methods rely on homology transfer to annotate protein sequences, using single sequence (BLAST, E-value cutoff <= 1e-30, subset of SwissProt 15.3) and multiple sequence (Priam, November 2010; CatFam, version 2.0, 1% FDR profile library) models of enzymatic functions. The base-level predictions are then integrated into a final set of annotations using an average weighted integration algorithm, where the weight of each prediction from each individual method was determined via a 0.632 bootstrap process over 1000 rounds of testing. The training and testing data for E2P2 and the BLAST reference database were drawn from protein sequences with experimental support of existence, compiled from SwissProt release 15.3."

Dickinson00: Dickinson JR, Harrison SJ, Dickinson JA, Hewlins MJ (2000). "An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." J Biol Chem 275(15);10937-42. PMID: 10753893

Dickinson03: Dickinson JR, Salgado LE, Hewlins MJ (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278(10);8028-34. PMID: 12499363

Flikweert99: Flikweert MT, de Swaaf M, van Dijken JP, Pronk JT (1999). "Growth requirements of pyruvate-decarboxylase-negative Saccharomyces cerevisiae." FEMS Microbiol Lett 174(1);73-9. PMID: 10234824

Hemschemeier08: Hemschemeier A, Jacobs J, Happe T (2008). "Biochemical and physiological characterization of the pyruvate formate-lyase Pfl1 of Chlamydomonas reinhardtii, a typically bacterial enzyme in a eukaryotic alga." Eukaryot Cell 7(3);518-26. PMID: 18245276

Hohmann91: Hohmann S (1991). "Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae." J Bacteriol 173(24);7963-9. PMID: 1744053

KillenbergJabs96: Killenberg-Jabs M, Konig S, Hohmann S, Hubner G (1996). "Purification and characterisation of the pyruvate decarboxylase from a haploid strain of Saccharomyces cerevisiae." Biol Chem Hoppe Seyler 377(5);313-7. PMID: 8828822

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lee85: Lee T.C., Langston-Unkefer P.J. "Pyruvate decarboxylase from Zea mays L. I. Purification and partial characterization from mature kernels and anaerobically treated roots." Plant Physiol. (1985) 79:242-247.

Mucke96: Mucke U, Wohlfarth T, Fiedler U, Baumlein H, Rucknagel KP, Konig S (1996). "Pyruvate decarboxylase from Pisum sativum. Properties, nucleotide and amino acid sequences." Eur J Biochem 237(2);373-82. PMID: 8647075

Neale87: Neale AD, Scopes RK, Wettenhall RE, Hoogenraad NJ (1987). "Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli." J Bacteriol 169(3);1024-8. PMID: 3546263

Sirikantaramas09: Sirikantaramas S, Yamazaki M, Saito K (2009). "A survival strategy: The coevolution of the camptothecin biosynthetic pathway and self-resistance mechanism." Phytochemistry. PMID: 19709698

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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