Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate Identifier CHEBI:57471 (Beilstein: 1124055) help_outline Charge -3 Formula C7H3O7 InChIKeyhelp_outline ODTDYYZJDQGKQT-NSCUHMNNSA-K SMILEShelp_outline [O-]C(=O)\C=C(/CC(=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (3Z)-2-oxo-4-carboxy-3-hexenedioate Identifier CHEBI:142690 Charge -3 Formula C7H3O7 InChIKeyhelp_outline POTZSFVTPSBXLW-IWQZZHSRSA-K SMILEShelp_outline C(/C(=C/C(C(=O)[O-])=O)/C(=O)[O-])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58504 | RHEA:58505 | RHEA:58506 | RHEA:58507 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Functional annotation of LigU as a 1,3-allylic isomerase during the degradation of lignin in the protocatechuate 4,5-cleavage pathway from the soil bacterium Sphingobium sp. SYK-6.
Hogancamp T.N., Raushel F.M.
Sphingobium sp. SYK-6 is a Gram-negative soil bacterium that contributes to the degradation of lignin. Lignin provides structural support and protection to plants as a complex aromatic heteropolymer. The lignin degradation pathway of guaiacyl moieties leads to the intermediate, protocatechuate (PC ... >> More
Sphingobium sp. SYK-6 is a Gram-negative soil bacterium that contributes to the degradation of lignin. Lignin provides structural support and protection to plants as a complex aromatic heteropolymer. The lignin degradation pathway of guaiacyl moieties leads to the intermediate, protocatechuate (PCA), which is further degraded via the 4,5-cleavage pathway in which PCA is ultimately metabolized to pyruvate and oxaloacetate. In this pathway, LigI has been shown to catalyze the hydrolysis of 2-pyrone-4,6-dicarboxylate to (4 E)-oxalomesaconate (OMA). Here we have demonstrated, using <sup>1</sup>H and <sup>13</sup>C nuclear magnetic resonance spectroscopy, that LigU catalyzes the isomerization of the double bond between C4 and C5 in (4 E)-OMA to (3 Z)-2-keto-4-carboxy-3-hexenedioate (KCH), where the double bond has migrated to be between C3 and C4 via a 1,3-allylic isomerization. LigU is most closely related in amino acid sequence to methylaconitate isomerase (PrpF) from Shewanella oneidensis and methylitaconate-Δ-isomerase (Mii) from Eubacterium barkeri. The kinetic constants for the isomerization of OMA to KCH by LigU at pH 8.0 were determined to be 1300 ± 120 s<sup>-1</sup> and (7.7 ± 1.5) × 10<sup>6</sup> M<sup>-1</sup> s<sup>-1</sup> for k<sub>cat</sub> and k<sub>cat</sub>/ K<sub>m</sub>, respectively. We have also shown that the product of the LigU-catalyzed reaction is the preferred substrate for the LigJ hydratase. In this reaction, LigJ catalyzes the hydration of KCH to 4-carboxy-4-hydroxy-2-oxoadipate. << Less
Biochemistry 57:2837-2845(2018) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.