ExplorEnz: EC 4.1.1.96

Your query returned 1 entry. Printable version

4.1.1.96

Accepted name:

carboxynorspermidine decarboxylase

Reaction:

(1) carboxynorspermidine = bis(3-aminopropyl)amine + CO₂
(2) carboxyspermidine = spermidine + CO₂

Glossary:

bis(3-aminopropyl)amine = norspermidine

Other name(s):

carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name)

Systematic name:

carboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming)

Comments:

A pyridoxal 5′-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae [1]. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro [3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and Michael, A.J. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284 (2009) 9899–9907. [DOI] [PMID: 19196710]
2.	Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J. and Phillips, M.A. 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 (2010) 25708–25719. [DOI] [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. 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 (2011) 43301–43312. [DOI] [PMID: 22025614]

[EC 4.1.1.96 created 2012]