- Source: Trans-feruloyl-CoA hydratase
In enzymology, a trans-feruloyl-CoA hydratase (EC 4.2.1.101) is an enzyme that catalyzes the chemical reaction
4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA
⇌
{\displaystyle \rightleftharpoons }
trans-feruloyl-CoA + H2O
Hence, this enzyme has one substrate, 4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA, and two products, trans-feruloyl-CoA and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA hydro-lyase (trans-feruloyl-CoA-forming). This enzyme is also called trans-feruloyl-CoA hydro-lyase (incorrect).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2J5I.
References
Narbad A, Gasson MJ (1998). "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. Bibcode:1983ApEnM..45.1582P. doi:10.1128/AEM.45.5.1582-1585.1983. PMC 242504. PMID 6870241.
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