Trans-feruloyl-CoA synthase
From Wikipedia, the free encyclopedia
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 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.
[edit] References
- IUBMB entry for 6.2.1.34
- BRENDA references for 6.2.1.34 (Recommended.)
- PubMed references for 6.2.1.34
- PubMed Central references for 6.2.1.34
- Google Scholar references for 6.2.1.34
- Narbad A, Gasson MJ (Pt 5). "Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens". Microbiology. 144: 1397–405. PMID 9611814.
- Pometto AL 3rd Crawford DL (1983). "Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus". Appl. Environ. Microbiol. 45: 1582–5. PMID 6870241.