Fumarase from porcine heart has been used:
- as a positive control in isocitrate dehydrogenase and α-ketoglutarate dehydrogenase assay
- for immobilized enzyme based stability assay
- in fumarate hydratase assays in human lung carcinoma cells (A549)
An enzyme that catalyzes the interconversion of
fumaric acid and malic acid. It is an important reactant in the tricarboxylic acid cycle.
Fumarase (FH in human) is a well-known tricarboxylic-acid-cycle enzyme found in both the cytoplasm and mitochondria of all eukaryotes.
Fumarase catalyzes the reversible hydration of fumarate to malate. In its mitochondrial form, fumarate is involved in the Krebs Cycle, while the cytosolic form is involved in amino acid metabolism.
Fumarase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 467 amino acids (44-510) and having a molecular mass of 50.2 kDa.
Fumarate Hydratase is purified by proprietary chromatographic techniques.
Fumarase is an enzymatic factor of Krebs cycle, which catalyzes the formation of L-malate from fumarate. Fumarase exists in both a cytosolic form and an N-terminal extended form, differing only in the translation start site used. The N-terminal extended form is aimed to the mitochondrion, where the removal of the extension results in the same form as in the cytoplasm. Fumarase is similar to a number of thermostable Class-2 fumarases and functions as a homotetramer. Mutations in the Fumarase gene causes fumarase deficiency and leads to progressive encephalopathy, cerebral atrophy and developmental delay. Fumarase enzyme is also thought to act as a tumor suppressor. Leydig cell tumors are caused by Fumarase mutations and represents one of the first reports of germline mutations in any type of adult testicular tumor.
