MetaCyc Pathway: cyanide degradation
Inferred from experiment

Pathway diagram: cyanide degradation

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.

Superclasses: Degradation/Utilization/AssimilationDegradation/Utilization/Assimilation - Other

Some taxa known to possess this pathway include : Chromobacterium violaceum

Expected Taxonomic Range: Bacteria , Viridiplantae

Chromobacterium violaceum is a cyanogenic species. Cyanide is formed as a secondary metabolite and is quickly degraded. Although the organism contains three enzymes capable of cyanide degradation, β-cyano-L-alanine synthase is the enzyme active in vivo. [Knowles86, Macadam84, Rodgers78, Rodgers82]


Knowles86: Knowles CJ, Bunch AW (1986). "Microbial cyanide metabolism." Adv Microb Physiol 1986;27;73-111. PMID: 3532718

Macadam84: Macadam AM, Knowles CJ "Purification and properties of β-cyano-L-alanine synthasefrom the cyanide-producing bacterium, Chromobacterium violaceum." Biochimica et Biophysica Acta 786:123-132 (1984).

Rodgers78: Rodgers PB, Knowles CJ "Cyanide Production and Degradation During Growth ofChromobacterium violaceum." Journal of General Microbiology 108:261-267 (1978).

Rodgers82: Rodgers PB "Cyanide Metabolism and β-Cyanoalanine Formation byWashed, Non-proliferating Cultures of Chromobacterium violaceum:Studies with Radiolabelled Cyanide." Journal of General Microbiology 128:2983-2989 (1982).

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

Han07: Han SE, Seo YS, Kim D, Sung SK, Kim WT (2007). "Expression of MdCAS1 and MdCAS2, encoding apple beta-cyanoalanine synthase homologs, is concomitantly induced during ripening and implicates MdCASs in the possible role of the cyanide detoxification in Fuji apple (Malus domestica Borkh.) fruits." Plant Cell Rep 26(8);1321-31. PMID: 17333023

Hatzfeld00: Hatzfeld Y, Maruyama A, Schmidt A, Noji M, Ishizawa K, Saito K (2000). "beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis." Plant Physiol 123(3);1163-71. PMID: 10889265

Ikegami88: Ikegami, Fumio, Takayama, Kyoko, Tajima, Chiho, Murakoshi, Isamu (1988). "Purification and properties of β-cyano-L-alanine synthase from Spinacia oleracea." Phytochemistry, 1988, 27(7):2011-2016.

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

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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
Page generated by Pathway Tools version 20.0 (software by SRI International) on Fri May 6, 2016, BIOCYC14.