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Thirteen different mutations in the respective gene, which is located at chromosome 12p13 and encodes the ubiquitous housekeeping enzyme triosephosphate isomerase (TPI), have been discovered so far. [4] TPI is a crucial enzyme of glycolysis and catalyzes the interconversion of dihydroxyacetone phosphate and glyceraldehyde-3-phosphate.
Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate.
The deficiency is most commonly caused by mutations in TPI1, although mutations in other isoforms have been identified. A common marker for TPI deficiency is the increased accumulation of DHAP in erythrocyte extracts; this is because the defective enzyme no longer has the ability to catalyze the isomerization to GAP.
Triosephosphate isomerase (TPI) is a central enzyme of glycolysis, the main pathway for cells to obtain energy by metabolizing sugars. In humans, certain mutations within this enzyme, which affect the dimerisation of this protein, are causal for a rare disease, triosephosphate isomerase deficiency.
This dysfunction results from a missense mutation that effects the encoded TPI protein. [19] The most common mutation is the substitution of gene, Glu104Asp, which produces the most severe phenotype, and is responsible for approximately 80% of clinical TPI deficiency. [18] TPI deficiency is very rare with less than 50 cases reported in ...
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Additionally, the discovery of mutations in the gyrB region is hypothesized to cause quinolone-based antibiotic resistance. [10] [60] Specifically, the mutations from aspartate (D) to asparagine (N), and Lysine (K) to glutamic acid (E) are believed to disrupt interactions, leading to some loss of tertiary structure. [10] [60]
Inosine triphosphate pyrophosphatase is an enzyme that in humans is encoded by the ITPA gene, [5] [6] by the rdgB gene in bacteria E.coli [7] and the HAM1 gene in yeast S. cerevisiae; [8] the protein is also encoded by some RNA viruses of the Potyviridae family. [9]