| 3-hydroxypimeloyl-CoA dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.259 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 3-hydroxypimeloyl-CoA dehydrogenase ( EC 1.1.1.259) is an enzyme that catalyzes the chemical reaction
- 3-hydroxypimeloyl-CoA + NAD+ 3-oxopimeloyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxypimeloyl-CoA and NAD+, whereas its 3 products are 3-oxopimeloyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
- Harwood CS, Gibson J (1997). "Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes?". J. Bacteriol. 179 (2): 301–9. PMC 178697. PMID 8990279.
| 3-hydroxypimeloyl-CoA dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.259 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 3-hydroxypimeloyl-CoA dehydrogenase ( EC 1.1.1.259) is an enzyme that catalyzes the chemical reaction
- 3-hydroxypimeloyl-CoA + NAD+ 3-oxopimeloyl-CoA + NADH + H+
Thus, the two substrates of this enzyme are 3-hydroxypimeloyl-CoA and NAD+, whereas its 3 products are 3-oxopimeloyl-CoA, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxypimeloyl-CoA:NAD+ oxidoreductase. This enzyme participates in benzoate degradation via coa ligation.
References
- Harwood CS, Gibson J (1997). "Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes?". J. Bacteriol. 179 (2): 301–9. PMC 178697. PMID 8990279.