|Alternate Names:||MFE1, PBFE, PBE, Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase, 3-hydroxyacyl-CoA dehydrogenase, 3-Hydroxyacyl ACP dehydrase, EHHADH|
|Structure and Function:||
ECHD or peroxisomal bifunctional enzyme (gene name EHHADH), also called L-PBE, is one of two multifunctional proteins involved in peroxisomal fatty acid oxidation; the other is MFE2. ECHD shows 2-enoyl CoA hydratase 1 (crotonase), 3S-hydroxyacyl-CoA dehydrogenase as well as enoyl-CoA isomerase activities. MFE 2 shows similar activities.
Both ECHD and MFE2 are 79 kDa; they are around 20% identical in sequence and have involved independently, one, ECHD to catalyze L and MFE2 to catalyze the D isomers of fatty acids. ECHD accepts short and long chain enoyl CoA esters, CoA esters of hydroxylated C27 bile synthesis intermediates and dicarboxylic acids.
A recent x-ray structure of rat ECHD has been reported. (Kasaragod P, et al., May 2010. The crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites.)