Carboxynorspermidine decarboxylase
Carboxynorspermidine decarboxylase | |||||||||
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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 | ||||||||
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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.; 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.; 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.; 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
- Carboxynorspermidine decarboxylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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