2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
| 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.312 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase (EC 1.1.1.312, 2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase, 4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+ oxidoreductase, alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase, 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase, LigC, ProD) is an enzyme with systematic name 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
- 4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
Unsubstituted aliphatic or aromatic aldehydes or glucose cannot serve as substrate of this enzyme.
References[edit]
- ^ Maruyama K, Ariga N, Tsuda M, Deguchi K (April 1978). "Purification and properties of alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase". Journal of Biochemistry. 83 (4): 1125–34. PMID 26671.
- ^ Maruyama K (December 1979). "Isolation and identification of the reaction product of alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase". Journal of Biochemistry. 86 (6): 1671–7. PMID 528534.
- ^ Maruyama K (February 1983). "Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase". Journal of Biochemistry. 93 (2): 557–65. PMID 6841353.
- ^ Masai E, Momose K, Hara H, Nishikawa S, Katayama Y, Fukuda M (December 2000). "Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6". Journal of Bacteriology. 182 (23): 6651–8. doi:10.1128/jb.182.23.6651-6658.2000. PMC 111406. PMID 11073908.
External links[edit]
- 2-hydroxy-4-carboxymuconate+semialdehyde+hemiacetal+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
