fumarase

Similar orientation has been discovered in other fumarase C crystal structures.

Despite its biological significance, the reaction mechanism of fumarase is not completely understood.

This sibling also turned out to have fumarase deficiency.

Germinal mutations in fumarase are associated with two distinct conditions.

Fumarase is prevalent in both fetal and adult tissues.

Molecular genetic testing for fumarase deficiency is currently available.

Fumarate is then converted by the enzyme fumarase to malate.

Fumarase comes in two forms: mitochondrial and cytosolic.

Figure 2 depicts the fumarase reaction mechanism.

Inactivity of both cytosolic and mitochondrial forms of fumarase are potential causes.

The fumarate released in the cytosol is converted to malate by cytosolic fumarase.

Mutations in the production and development of fumarase have led to the discovery of several fumarase-related diseases in humans.

The Colorado City/Hildale area has the world's highest incidence of fumarase deficiency, an extremely rare genetic condition.

Isolated, increased concentration of fumaric acid on urine organic acid analysis is highly suggestive of fumarase deficiency.

Autosomal recessive mutations cause a serious neurological disease known as fumarase deficiency, which is associated with a variety of congenital lesions in the brain.

Crystal structures of fumarase C from Escherichia coli have been observed to have two occupied dicarboxylate binding sites.

This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans-elimination reaction.

The function of fumarase in the citric acid cycle is to facilitate a transition step in the production of energy in the form of NADH.

Theodore Tarby, a pediatric neurologist who has treated some of the community's fumarase deficient residents, has been quoted as estimating the IQ of his patients as around 25.

Fumarase deficiency causes encephalopathy, severe mental retardation, unusual facial features, brain malformation, and epileptic seizures due to an abnormally low amount of fumarase in cells.

The primary binding site on fumarase is known as catalytic site A. Studies have revealed that catalytic site A is composed of amino acid residues from three of the four subunits within the tetrameric enzyme.

Bayley JP, Launonen V, Tomlinson IP: The FH mutation database: an online database of fumarate hydratase mutations involved in the MCUL (HLRCC) tumor syndrome and congenital fumarase deficiency.