The Substrate Specificity of Fumarase

The substrate specificity of fumarase.

The substrate specificity of fumarase has been studied by measuring the ability of the enzyme to hydrate or dehydrate derivatives of fumarate and L-malate. Fumarase was observed to hydrate fumarate and its derivatives in the order, fluorofumarate > fumarate > chlorofumarate > bromofumarate > acetylenedicarboxylate > iodofumarate > mesaconate. With the exception of fluorofumarate, water was adde...

The number of substrate- and inhibitor-binding sites of fumarase.

The reversible binding to fumarase of the competitive inhibitors, tram+aconitate and citrate, and of the natural substrates, fumarate and L-malate, was studied by the method of equilibrium dialysis. The binding of the enol tautomer of oxalacetate, a secondary substrate of fumarase, was measured spectrophotometrically. The results of these studies indicate that there are four substrateor inhibit...

The Role of Highly Conserved Tryptophan in the Sixth Conserved Region at Substrate Specificity of α- amylase

Early in this study, an α-Amylase from Bacillus megaterium WHO (BMW) was isolated from hot springs of Ramsar (North of Iran), and its gene was cloned in E.coli. Based on its conserved sequence regions and substrate specificity, it was classified as intermediary group enzymes with the specificity of oligo-1,6-glucosidase and neopullulanase subfamilies. In the sixth conserved re...

Substrate Specificity of MMPs

Glutamyl Endopeptidases: The Puzzle of Substrate Specificity

Glutamyl endopeptidases (GEPases) are chymotrypsin-like enzymes that preferentially cleave the peptide bonds of the α-carboxyl groups of glutamic acid. Despite the many years of research, the structural determinants underlying the strong substrate specificity of GEPases still remain unclear. In this review, data concerning the molecular mechanisms that determine the substrate preference of GEPa...