From Wikipedia, the free encyclopedia
Carboxynorspermidine decarboxylase
Identifiers
EC no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ 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.
  2. ^ 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.
  3. ^ 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

From Wikipedia, the free encyclopedia
Carboxynorspermidine decarboxylase
Identifiers
EC no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. ^ 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.
  2. ^ 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.
  3. ^ 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


Videos

Youtube | Vimeo | Bing

Websites

Google | Yahoo | Bing

Encyclopedia

Google | Yahoo | Bing

Facebook