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4.1.1.96 |
| Description |
Carboxynorspermidine decarboxylase |
| Alternative names |
nspC;
CANS DC;
Carboxyspermidine decarboxylase. |
| Catalyzed reaction |
Carboxynorspermidine <=> bis(3-aminopropyl)amine + CO(2)
Carboxyspermidine <=> spermidine + CO(2) |
| Cofactor |
Pyridoxal-phosphate |
| Comments |
Part of a bacterial polyamine biosynthesis pathway.
The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae.
The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro. |
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This is the last enzyme in the biosynthesis of norspermidine, a polyamine similar to the more common spermidine.
Norspermidine has been found to occur naturally in some species of bacteria as well as in plants. |
| PDB |
3N29; |
| Organisms |
-Eubacteria |
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Family |
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| Links |
Enzyme (activities) 4.1.1.96
BRENDA (activities) 4.1.1.96
KEGG (pathways) 4.1.1.96
PLPMDB (PLP mutants) 4.1.1.96
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| References |
Deng X, Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA. (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. J Biol Chem. 285 25708-19. Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ. (2009) An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae J Biol Chem 284 9899-907. Yamamoto S, Sugahara T, Tougou K, Shinoda S. (1994) Cloning and nucleotide sequence of the carboxynorspermidine decarboxylase gene from Vibrio alginolyticus Microbiology 140 3117-24. |
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| last changed |
2014/03/20 13:20 |
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