Trans-feruloyl-CoA synthase

In enzymology, a trans-feruloyl—CoA synthase (EC 6.2.1.34) is an enzyme that catalyzes the chemical reaction

trans-Feruloyl—CoA synthase
Identifiers
EC no.6.2.1.34
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
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 trans-feruloyl-CoA and products of ATP breakdown.

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

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  • 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.