isocitrate dehydrogenase and enoyl-coA hydratase were highly expressed in maslinic acid-treated Raji cells.
7 dehydr ogenase [NAD] subunit alpha, mitoch ondrial 8 Enoyl-coA P30084 31,361/6.
The second step is carried out by an enoyl-CoA hydratase, and the enzyme involved in the third step is an L 3-hydroxyacyl-CoA dehydrogenase using NAD as cofactor for the reaction, which is reduced to NADH transferring electrons to complex 1 of the respiratory chain.
The enzymes for the b-oxidation oflong- to mediumchain fatty acids (C-18 to C-12) are located close to the inner mitochondrial membrane, they are: very-longchain acyl-CoA dehydrogenase, long-chain enoyl-CoA hydratase, long-chain L 3-hydroxyacyl-CoA dehydrogenase and long-chain 3-ketoacyl-CoA thiolase.
In particular, the expression level of spots 26, 7, 19, 9, 6, 8 and 21, which were identified as Cathepsin H precursor, Retinal dehydrogenase 1, Enoyl-CoA hydratase, Elongation factor Tu, Ubiquinol-cytochrome-c reductase, T-complex protein 1 subunit beta and ATP synthase D chain was 9.
Structural mechanism of Enoyl-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted Fashion.
Both sequences were found to align with the enoyl-CoA
hydratase (ECH) family of enzymes which typically catalyze the hydration of double bonded intermediates during the beta-oxidation of fatty acids.
The 3 enzymes involved are long-chain enoyl-CoA
hydratase (LCEH), long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), and long-chain 3-ketoacyl-CoA thiolase (LCTH).
Two enzymes are essential: a hydratase such as D-specific enoyl-CoA
hydratase, for example, the hydratase obtained from Aeromonas caviae, and a .
The FAE reactions are (i) condensation of malonyl-CoA with a long chain acyl-CoA to give a [Beta]-ketoacyl-CoA; (ii) reduction to [Beta]-hydroxyacyl-CoA; (iii) dehydration to enoyl-CoA
, and (iv) reduction of the enoyl-CoA
, resulting in an elongated acyl-CoA (Fehling and Mukherjee, 1991).
Novel fatty acid [beta]-oxidation enzymes in rat liver mitochondria: purification and properties of enoyl-CoA
hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein.
LCHAD activity is associated with the [alpha]-subunit, as is the activity of longchain enoyl-CoA