Enzyme

Download
EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.68
Description:5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase.
Alternative Name: 5-oxopent-3-ene-1,2,5-tricarboxylate carboxy-lyase.
Cath: 3.90.850.10;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.68
BRENDA Enzyme Link: BRENDA 4.1.1.68
KEGG Enzyme Link: KEGG4.1.1.68
BioCyc Enzyme Link: BioCyc 4.1.1.68
ExPASy Enzyme Link: ExPASy4.1.1.68
EC2PDB Enzyme Link: EC2PDB 4.1.1.68
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.68
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.68
IntEnz Enzyme Link: IntEnz 4.1.1.68
MEDLINE Enzyme Link: MEDLINE 4.1.1.68
MSA:

4.1.1.68;

Phylogenetic Tree:

4.1.1.68;

Uniprot:
M-CSA:
RHEA:14397 (3E,5R)-5-carboxy-2-oxohept-3-enedioate + H(+) = (4Z)-2-oxohept-4-enedioate + CO2
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[*:8].[H+;H0:9]>>[*:5]-[CH;+0:4]=[CH;+0:6]-[CH2;+0:7]-[*:8].[*: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
Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C.Roper DI, Cooper RA1993 Oct 158223600
Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.Garrido-Peritierra A, Cooper RA1981 Jul7026235