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: cyanate catabolism
|Superclasses:||Degradation/Utilization/Assimilation → Inorganic Nutrients Metabolism → Nitrogen Compounds Metabolism|
In Escherichia coli cyanate can occur inside the cell as a result of nonenzymatic decomposition of carbamoyl phosphate, and in the environment due to dissociation of urea and photooxidation of hydrogen cyanide. Although cyanate at high concentrations is toxic to Escherichia coli, it can serve as a sole source of nitrogen due to the production of ammonia by cyanase [Sung87]. The cyanate degradation pathway therefore serves the dual purpose of detoxification and nitrogen utilization [Kozliak95].
Cyanase catalyzes the first step of the pathway, producing CO2 and the unstable compound carbamate, which spontaneously decomposes to CO2 and ammonia, thus producing a source of nitrogen for growth. The second enzyme of this pathway, carbonic anhydrase, is an essential component of the pathway. In the absence of carbonic anhydrase at atmospheric concentrations of CO2, non-enzymatic hydration of CO2 is not sufficient to prevent depletion of the intracellular hydrogen carbonate pool due to rapid diffusion of CO2 [Guilloton93].
Pseudomonas fluorescens NCIB 11764 is also capable of utilizing cyanate as a sole source of nitrogen for growth [Kunz89]. The induced enzymatic activity of extracts of cyanate grown Pseudomonas fluorescens NCIB 11764 cells was shown to be bicarbonate dependent and specific for cyanate, resembling the enzymatic activity of cyanase as described in Escherichia coli [Kunz89].
Guilloton93: Guilloton MB, Lamblin AF, Kozliak EI, Gerami-Nejad M, Tu C, Silverman D, Anderson PM, Fuchs JA (1993). "A physiological role for cyanate-induced carbonic anhydrase in Escherichia coli." J Bacteriol 1993;175(5);1443-51. PMID: 8444806
Rowlett02: Rowlett RS, Tu C, McKay MM, Preiss JR, Loomis RJ, Hicks KA, Marchione RJ, Strong JA, Donovan GS, Chamberlin JE (2002). "Kinetic characterization of wild-type and proton transfer-impaired variants of beta-carbonic anhydrase from Arabidopsis thaliana." Arch Biochem Biophys 404(2);197-209. PMID: 12147257
Anderson87: Anderson PM, Johnson WV, Endrizzi JA, Little RM, Korte JJ (1987). "Interaction of mono- and dianions with cyanase: evidence for apparent half-site binding." Biochemistry 26(13);3938-43. PMID: 3651424
Anderson88a: Anderson PM, Johnson WV, Korte JJ, Xiong XF, Sung YC, Fuchs JA (1988). "Reversible dissociation of active octamer of cyanase to inactive dimer promoted by alteration of the sulfhydryl group." J Biol Chem 263(12);5674-80. PMID: 3128546
Anderson94: Anderson PM, Korte JJ, Holcomb TA, Cho YG, Son CM, Sung YC (1994). "Formation of intersubunit disulfide bonds and properties of the single histidine and cysteine residues in each subunit relative to the decameric structure of cyanase." J Biol Chem 269(21);15036-45. PMID: 8195141
Burnell90: Burnell JN (1990). "Immunological Study of Carbonic Anhydrase in C3 and C4 Plants Using Antibodies to Maize Cytosolic and Spinach Chloroplastic Carbonic Anhydrase." Plant Cell Physiol. 31(4):423-427.
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Hashimoto03: Hashimoto M, Kato J (2003). "Indispensability of the Escherichia coli carbonic anhydrases YadF and CynT in cell proliferation at a low CO2 partial pressure." Biosci Biotechnol Biochem 67(4);919-22. PMID: 12784642
Ito11: Ito J, Batth TS, Petzold CJ, Redding-Johanson AM, Mukhopadhyay A, Verboom R, Meyer EH, Millar AH, Heazlewood JL (2011). "Analysis of the Arabidopsis cytosolic proteome highlights subcellular partitioning of central plant metabolism." J Proteome Res 10(4);1571-82. PMID: 21166475
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