4-hydroxy-3-methoxyphenyl-β-ketopropionyl-CoA thiolase (HMPKP-CoA thiolase)

4-hydroxy-3-methoxyphenyl-β-ketopropionyl-CoA thiolase is a bacterial enzyme involved in the catabolism of hydroxycinnamic acids, such as ferulic acid [1, 2]. It catalyzes the thiolytic cleavage of 4-hydroxy-3-methoxyphenyl-β-ketopropionyl-CoA (HMPKP-CoA) into vanilloyl-CoA and acetyl-CoA, a reaction analogous to the final step of fatty acid beta-oxidation [4, 5]. This enzyme is particularly well-characterized in the soil bacterium Agrobacterium fabrum, where it is encoded by the gene atu1421 and is essential for the microbial degradation of plant-derived aromatic compounds [2, 3]. While the enzyme is of significant interest in environmental microbiology and for the biotechnological production of vanillin from lignin, it does not have a human ortholog or a known role in human physiology [2, 4]. Consequently, there are currently no therapeutic drugs that target this enzyme, and it is not considered a target for clinical drug development.

Other names

4-hydroxy-3-methoxyphenyl-β-ketopropionic acid-CoA β-keto-thiolaseAtu14213-oxoacyl-CoA ketohydrolaseBeta-ketothiolaseHMPKP-CoA thiolase

No known therapeutic drugs target this enzyme.