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/Assimilation → Degradation/Utilization/Assimilation - Other|
Some taxa known to possess this pathway include : Chromobacterium violaceum
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]
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).
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).
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.
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493