Trans-feruloyl-CoA synthase
| trans-feruloyl-CoA synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.34 | ||||||||
| 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 trans-feruloyl-CoA synthase (EC 6.2.1.34) is an enzyme that catalyzes the chemical reaction
- ferulic acid + CoASH + ATP trans-feruloyl-CoA + products of ATP breakdown
The 3 substrates of this enzyme are ferulic acid, CoASH, and ATP, whereas its two products are and .
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is trans-ferulate:CoASH ligase (ATP-hydrolysing). This enzyme is also called trans-feruloyl-CoA synthetase.
References[]
- Narbad A, Gasson MJ. "Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens". Microbiology. 144 (5): 1397–405. doi:10.1099/00221287-144-5-1397. PMID 9611814.
- Pometto AL III, Crawford DL (1983). "Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus". Appl. Environ. Microbiol. 45 (5): 1582–5. PMC 242504. PMID 6870241.
Categories:
- EC 6.2.1
- Enzymes of unknown structure
- Ligase stubs