Carboxynorspermidine decarboxylase
Carboxynorspermidine decarboxylase (EC 4.1.1.96, carboxyspermidine decarboxylase, CANSDC, VC1623 (gene)) is an enzyme with systematic name carboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- (1) carboxynorspermidine bis(3-aminopropyl)amine + CO2
- (2) carboxyspermidine spermidine + CO2
This enzyme contains pyridoxal 5'-phosphate.
References
- ↑ Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. (2009). "An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae". J. Biol. Chem. 284 (15): 9899–9907. doi:10.1074/jbc.M900110200. PMC 2665113. PMID 19196710.
- ↑ Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J. and Phillips, M.A. (2010). "Evolution of substrate specificity within a diverse family of β/α-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine". J. Biol. Chem. 285 (33): 25708–25719. doi:10.1074/jbc.M110.121137. PMID 20534592.
- ↑ Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and Michael, A.J. (2011). "Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota". J. Biol. Chem. 286 (50): 43301–43312. doi:10.1074/jbc.M111.307835. PMC 3234850. PMID 22025614.
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