Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.95
Description:L-glutamyl-[BtrI acyl-carrier protein] decarboxylase.
Cath: 3.20.20.10; 2.40.37.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.95
BRENDA Enzyme Link: BRENDA 4.1.1.95
KEGG Enzyme Link: KEGG4.1.1.95
BioCyc Enzyme Link: BioCyc 4.1.1.95
ExPASy Enzyme Link: ExPASy4.1.1.95
EC2PDB Enzyme Link: EC2PDB 4.1.1.95
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.95
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.95
IntEnz Enzyme Link: IntEnz 4.1.1.95
MEDLINE Enzyme Link: MEDLINE 4.1.1.95
MSA:

4.1.1.95;

Phylogenetic Tree:

4.1.1.95;

Uniprot:
M-CSA:
RHEA:53956 H(+) + L-glutamyl-[BtrI ACP] = 4-aminobutanoyl-[BtrI ACP] + CO2
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](=[*:5])-[OH;+0:6].[H+;H0:7]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]=[C;H0;+0:4]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Biosynthesis of the unique amino acid side chain of butirosin: possible protective-group chemistry in an acyl carrier protein-mediated pathway.Li Y, Llewellyn NM, Giri R, Huang F, Spencer JB2005 Jun15975512
Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain.Llewellyn NM, Li Y, Spencer JB2007 Apr17462573