Carboxynorspermidine decarboxylase

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Carboxynorspermidine decarboxylase
Identifiers
EC no.4.1.1.96
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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[edit]

  1. ^ Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ (April 2009). "An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae". The Journal of Biological Chemistry. 284 (15): 9899–907. doi:10.1074/jbc.M900110200. PMC 2665113. PMID 19196710.
  2. ^ Deng X, Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA (August 2010). "Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine". The Journal of Biological Chemistry. 285 (33): 25708–19. doi:10.1074/jbc.M110.121137. PMC 2919134. PMID 20534592.
  3. ^ Hanfrey CC, Pearson BM, Hazeldine S, Lee J, Gaskin DJ, Woster PM, Phillips MA, Michael AJ (December 2011). "Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota". The Journal of Biological Chemistry. 286 (50): 43301–12. doi:10.1074/jbc.M111.307835. PMC 3234850. PMID 22025614.

External links[edit]