Biology:Carboxynorspermidine decarboxylase
From HandWiki
| Carboxynorspermidine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] bis(3-aminopropyl)amine + CO2
- (2) carboxyspermidine [math]\displaystyle{ \rightleftharpoons }[/math] spermidine + CO2
This enzyme contains pyridoxal 5'-phosphate.
References
- ↑ "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. April 2009. doi:10.1074/jbc.M900110200. PMID 19196710.
- ↑ "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. August 2010. doi:10.1074/jbc.M110.121137. PMID 20534592.
- ↑ "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. December 2011. doi:10.1074/jbc.M111.307835. PMID 22025614.
External links
- Carboxynorspermidine+decarboxylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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