RT Journal Article SR Electronic(1) A1 Puchegger, Susanne A1 Redl, Bernhard A1 Stöffler, GeorgYR 1990 T1 Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus JF Microbiology, VO 136 IS 8 SP 1537 OP 1541 DO https://doi.org/10.1099/00221287-136-8-1537 PB Microbiology Society, SN 1465-2080, AB Fumarate hydratase (EC 4.2.1.2) from the extremely thermophilic archaeobacterium Solfolobus solfataricus has been purified to homogeneity by a rapid purification procedure using affinity chromatography and high-performance size-exclusion chromatography, and the enzyme’s physical and biochemical properties have been determined. The native enzyme has a molecular mass of 170 kDa and is composed of identical subunits with a molecular mass of 45 kDa, thus indicating a tetrameric structure similar to fumarases isolated from other organisms. The enzyme was active at temperatures ranging from 40 °C to 90 °C, with a maximum activity at 85 °C. The pH optimum for generation of fumarate was found to be pH 8·0. The enzyme showed high stability to denaturation by heat and organic solvents., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-136-8-1537