Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.96
Description:Carboxynorspermidine decarboxylase.
Alternative Name: Carboxyspermidine decarboxylase.
Cath: 3.20.20.10; 2.40.37.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.96
BRENDA Enzyme Link: BRENDA 4.1.1.96
KEGG Enzyme Link: KEGG4.1.1.96
BioCyc Enzyme Link: BioCyc 4.1.1.96
ExPASy Enzyme Link: ExPASy4.1.1.96
EC2PDB Enzyme Link: EC2PDB 4.1.1.96
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.96
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.96
IntEnz Enzyme Link: IntEnz 4.1.1.96
MEDLINE Enzyme Link: MEDLINE 4.1.1.96
MSA:

4.1.1.96;

Phylogenetic Tree:

4.1.1.96;

Uniprot:
M-CSA:
RHEA:34099 carboxynorspermidine + H(+) = CO2 + norspermidine
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6].[H+;H0:7]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]=[C;H0;+0:2]=[O;H0;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
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.Deng X, Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA2010 Aug 1320534592
Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota.Hanfrey CC, Pearson BM, Hazeldine S, Lee J, Gaskin DJ, Woster PM, Phillips MA, Michael AJ2011 Dec 1622025614
An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae.Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ2009 Apr 1019196710

RHEA:34095 carboxyspermidine + H(+) = CO2 + spermidine
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6].[H+;H0:7]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]=[C;H0;+0:2]=[O;H0;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
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.Deng X, Lee J, Michael AJ, Tomchick DR, Goldsmith EJ, Phillips MA2010 Aug 1320534592
Alternative spermidine biosynthetic route is critical for growth of Campylobacter jejuni and is the dominant polyamine pathway in human gut microbiota.Hanfrey CC, Pearson BM, Hazeldine S, Lee J, Gaskin DJ, Woster PM, Phillips MA, Michael AJ2011 Dec 1622025614
An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae.Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ2009 Apr 1019196710