Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
|
| GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline (3E,5R)-5-carboxy-2-oxohept-3-enedioate Identifier CHEBI:87491 Charge -3 Formula C8H5O7 InChIKeyhelp_outline WHGVLEMQINVDLH-QPHDTYRISA-K SMILEShelp_outline [O-]C(=O)C[C@H](\C=C\C(=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (4Z)-2-oxohept-4-enedioate Identifier CHEBI:87507 Charge -2 Formula C7H6O5 InChIKeyhelp_outline ICGKEQXHPZUYSF-UPHRSURJSA-L SMILEShelp_outline C(=C\CC(C([O-])=O)=O)\CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 980 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:14397 | RHEA:14398 | RHEA:14399 | RHEA:14400 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C.
Roper D.I., Cooper R.A.
A 1.8-kbp region of DNA that appeared from deletion subcloning to code for 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase and 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase was investigated further. By nucleotide sequencing, a single open reading frame was found encoding a polypeptide of M(r)44 ... >> More
A 1.8-kbp region of DNA that appeared from deletion subcloning to code for 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase and 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase was investigated further. By nucleotide sequencing, a single open reading frame was found encoding a polypeptide of M(r)44514. One of the deletion subclones expressed the decarboxylase and isomerase activities at elevated levels and was used to facilitate purification of the enzyme(s). Both activities copurified, indicating that they were distinct activities of the same protein. Some kinetic properties of the purified isomerase/decarboxylase protein were investigated and it was shown that there is a 49,000-fold preference for 2-hydroxyhepta-2,4-diene-1,7-dioate over the structurally related compound 5-carboxymethyl-2-hydroxymuconate, the substrate of a second isomerase in the same catabolic pathway. Comparison of the amino acid sequences of the two isomerases showed only a low level of similarity, suggesting that these two enzymes are not evolutionarily related. However, comparison of the N-terminal half of the isomerase/decarboxylase sequence (residues 1-202) with the second half (residues 203-406) showed significant similarity, suggesting that a duplication may have occurred to produce the bifunctional gene. << Less
Eur. J. Biochem. 217:575-580(1993) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli.
Garrido-Peritierra A., Cooper R.A.
The possible involvement of an isomerase in the 4-hydroxyphenylacetate meta-cleavage pathway has been studied. 5-Carboxymethyl-2-hydroxymuconate has been shown to undergo both spontaneous and enzyme-catalysed isomerisation to give 5-carboxymethyl-2-oxo-hex-3-ene-1,5-dioate, a compound with an abso ... >> More
The possible involvement of an isomerase in the 4-hydroxyphenylacetate meta-cleavage pathway has been studied. 5-Carboxymethyl-2-hydroxymuconate has been shown to undergo both spontaneous and enzyme-catalysed isomerisation to give 5-carboxymethyl-2-oxo-hex-3-ene-1,5-dioate, a compound with an absorbance maximum at 246 nm. The latter compound rather than the former is the substrate for a decarboxylase that produces 2-hydroxyhepta-2,4-diene,1,7-dioate. The isomerase and decarboxylase enzymes have been purified to over 90% homogeneity. Mg2+ is required for the decarboxylase reaction but not for the isomerase. << Less
Eur J Biochem 117:581-584(1981) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
Comments
Multi-step reaction: RHEA:38031 and RHEA:38035. Johnson, W.H.; Hajipour, G.; Whitman, C.P. Stereochemical studies of 5-(carboxymethyl)-2-hydroxymuconate isomerase and 5-(carboxymethyl)-2-oxo-3-hexene-1,6-dioate decarboxylase from Escherichia coli C: mechanistic and evolutionary implications. J. Am. Chem. Soc. 117, 8719-8726 (1995)