Carboxynorspermidine decarboxylase

Carboxynorspermidine decarboxylase
Identifiers
EC number 4.1.1.96
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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 \rightleftharpoons bis(3-aminopropyl)amine + CO2
(2) carboxyspermidine \rightleftharpoons spermidine + CO2

This enzyme contains pyridoxal 5'-phosphate.

References

  1. 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.
  2. 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.
  3. 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.

External links

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