Carboxynorspermidine decarboxylase (EC 4.1.1.96, carboxyspermidine decarboxylase, CANSDC, VC1623 (gene)) is an enzyme with systematic namecarboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming).[1][2][3] This enzyme catalyses the following chemical reaction
^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. PMC2665113. PMID 19196710.
^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. PMC2919134. PMID 20534592.
^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. PMC3234850. PMID 22025614.
External linksedit
Carboxynorspermidine+decarboxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
carboxynorspermidine, decarboxylase, carboxyspermidine, decarboxylase, cansdc, vc1623, gene, enzyme, with, systematic, name, carboxynorspermidine, carboxy, lyase, aminopropyl, amine, forming, this, enzyme, catalyses, following, chemical, reactionidentifiersec,. 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 reactionCarboxynorspermidine decarboxylaseIdentifiersEC no 4 1 1 96DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins 1 carboxynorspermidine displaystyle rightleftharpoons bis 3 aminopropyl amine CO2 2 carboxyspermidine displaystyle rightleftharpoons spermidine CO2 This enzyme contains pyridoxal 5 phosphate References edit 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 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 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 editCarboxynorspermidine decarboxylase at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Carboxynorspermidine decarboxylase amp oldid 1172341723, wikipedia, wiki, book, books, library,
