2-Hydroxymuconate-6-semialdehyde dehydrogenase
2-Hydroxymuconate-6-semialdehyde dehydrogenase (EC 1.2.1.85, xylG [gene], praB [gene] ) is an enzyme with systematic name (2E,4Z)-2-hydroxy-6-oxohexa-2,4-dienoate:NAD+ oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
| 2-Hydroxymuconate-6-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.85 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This substrate for this enzyme is formed by meta ring cleavage of catechol (EC 1.13.11.2, catechol 2,3-dioxygenase), and is an intermediate in the bacterial degradation of several aromatic compounds.
References
- Inoue J, Shaw JP, Rekik M, Harayama S (March 1995). "Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida". Journal of Bacteriology. 177 (5): 1196–201. PMC 176723. PMID 7868591.
- Orii C, Takenaka S, Murakami S, Aoki K (November 2006). "Metabolism of 4-amino-3-hydroxybenzoic acid by Bordetella sp. strain 10d: A different modified meta-cleavage pathway for 2-aminophenols". Bioscience, Biotechnology, and Biochemistry. 70 (11): 2653–61. doi:10.1271/bbb.60264. PMID 17090920.
- Kasai D, Fujinami T, Abe T, Mase K, Katayama Y, Fukuda M, Masai E (November 2009). "Uncovering the protocatechuate 2,3-cleavage pathway genes". Journal of Bacteriology. 191 (21): 6758–68. doi:10.1128/JB.00840-09. PMC 2795304. PMID 19717587.
External links
- 2-hydroxymuconate-6-semialdehyde+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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