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Karboksinorspermidinska dekarboksilaza
Karboksinorspermidinska dekarboksilaza
Identifikatori
EC broj	4.1.1.96
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
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PMC	članci
PubMed	članci
NCBI	proteini

Karboksinorspermidinska dekarboksilaza (EC 4.1.1.96, karboksispermidinska dekarboksilaza, CANSDC, VC1623 (gen)) je enzim sa sistematskim imenom karboksinorspermidin karboksilijaza (formira bis(3-aminopropil)amin).^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

(1) karboksinorspermidin

\rightleftharpoons

bis(3-aminopropil)amin + CO₂

(2) karboksispermidin

\rightleftharpoons

spermidin + CO₂

Ovaj enzim vezuje piridoksal 5'-fosfat.

Reference

^ Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and 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: 9899—9907. PMID 19196710.
^ Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J. and 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: 25708—25719. PMID 20534592.
^ Hanfrey, C.C., Pearson, B.M., Hazeldine, S., Lee, J., Gaskin, D.J., Woster, P.M., Phillips, M.A. and 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: 43301—43312. PMID 22025614.

Literatura

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.

Spoljašnje veze

Carboxynorspermidine+decarboxylase на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Lee, J., Sperandio, V., Frantz, D.E., Longgood, J., Camilli, A., Phillips, M.A. and 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: 9899—9907. PMID 19196710.

[2] Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J. and 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: 25708—25719. 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. (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: 43301—43312. PMID 22025614.

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