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; |
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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.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 |
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 |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C. | Roper DI, Cooper RA | 1993 Oct 15 | 8223600 |
Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli. | Garrido-Peritierra A, Cooper RA | 1981 Jul | 7026235 |