Disease relevance of ECHS1

• The primary, alpha-secondary, beta-secondary, and beta'-secondary deuterium and primary 18O kinetic isotope effects on V/K for the dehydration of [(3S)-3-hydroxybutyryl]pantetheine by bovine liver crotonase (enoyl-CoA hydratase, EC 4.2.1.17) have been determined by the equilibrium perturbation method [1].

High impact information on ECHS1

• Since the presence of both crotonase and long chain enoyl-CoA hydratase in pig heart has been reported earlier, the presence of the same two enoyl-CoA hydratases in various tissues of several animals was investigated by sequential extraction and chromatography on hydroxylapatite of tissue homogenates [2].
• The inhibitor, upon incubation with bovine liver ECH, labels a tryptic peptide, ALGGGXEL, near the active site of the protein, where X is the amino acid that is covalently modified [3].
• Polarization of cinnamoyl-CoA substrates bound to enoyl-CoA hydratase: correlation of (13)C NMR with quantum mechanical calculations and calculation of electronic strain energy [4].
• The validity of this theory is confirmed by a model system consisting of enoyl-CoA hydratase (EC 4.2.1.17) and 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) with 2,4-decadienoyl coenzyme A (CoA) as a substrate [5].
• Disaccharide compositional analysis of both ECHS and FHS oligosaccharides showed them to contain similar amounts of 2-O-, 6-O-, and N-sulphated disaccharides [6].

Biological context of ECHS1

• The kinetics of bovine liver enoyl-CoA hydratase (EC 4.2.1.17) or crotonase with 2-trans-hexadecenoyl-CoA as a substrate were studied because different rates were obtained with two assay methods based on measurements of substrate utilization and product formation, respectively [7].

Associations of ECHS1 with chemical compounds

• 5. In the presence of the enoyl-CoA hydratase symmetrically labelled 3S-3-hydroxy[2 minus 3H2]BUTYRYL-CoA lost nearly 50% of its tritium label; 2R,3S-3hydroxy [2-3-H1]butyryl-CoA lost about 78% [8].
• Modification of enoyl-CoA hydratase using diethyl pyrocarbonate [9].
• These experiments taken together show that, in contrast to other hydratases, histidine is not involved in the catalytic mechanism of enoyl-CoA hydratase, and suggest that a single residue is important for activity [9].

Analytical, diagnostic and therapeutic context of ECHS1

• Cloning and sequence analysis of bovine liver ECH gene revealed the identity of the amino acid residue entrapped by MCPF-CoA as Cys-114 (mature sequence numbering) [3].
• To investigate the apparent discrepancy between the NMR and Raman data for HD-CoA bound to MCAD, (13)C NMR spectra have been obtained for HD-CoA bound to enoyl-CoA hydratase, an enzyme system that has also previously been studied using Raman spectroscopy [10].

References