Aerobic respiration is the process of converting energy in the form of glucose into ATP, the primary currency of energy used by cells to fuel biochemical processes and support growth. The first phase of respiration is glycolysis, a series of ten biochemical reactions in the cytoplasm that convert glucose into<unk> .<unk>  is then transported into mitochondria, where it is converted by the<unk>  dehydrogenase complex into acetyl-CoA, the starting substrate of the Krebs cycle. When PDC activity is reduced or abolished by mutation,<unk>  levels rise. Excess<unk>  is then converted into lactic acid by lactate dehydrogenase. Lactic acid enters the blood stream, causing acidification in a condition known as lactic acidosis. Glycolysis Citric acid cycle with aconitate 2 The most commonly seen form of PDCD is caused by mutations in the X-linked E1 alpha gene,<unk> A1, and is approximately equally prevalent in both males and females. However, males are more severely affected than heterozygous females. This can be explained by x-inactivation, as females carry one normal and one mutant gene. Cells with a normal allele active can metabolize the lactic acid that is released by the<unk>  deficient cells. They cannot, however, supply ATP to these cells and, therefore, phenotype depends largely on the nature/severity of the mutation. More rarely, mutations occur in the E2 (dihydrolipoyl transacetylase) or the E3 (dihydrolipoyl dehydrogenase) subunits of the PDC enzymatic complex, DLAT and DLD genes respectively. In these cases, PDCD displays autosomal recessive inheritance, affecting males and females equally. In cases where PDCD is a result of a mutation in a gene other than<unk> A1, it is most commonly known to be due to mutations in the following four genes,<unk> B, DLAT,<unk> X and PDP1. All of these genes, like the<unk> A1 gene are responsible for coding for a specific subunit of the<unk>  dehydrogenase complex. The<unk> B gene is responsible for the coding of the E1 beta subunit of the<unk>  dehydrogenase complex. The DLAT gene is responsible for the coding of the E2 subunit, and the PDP1 is responsible for producing the<unk>  phosphatase catalytic subunit that catalyzes<unk>  dephosphorylation. This dephosphorylation activates the complex. The final gene that could be responsible for this disease is the<unk> X gene, which codes for the E3 binding protein which is responsible for binding E3 dimers to the E2 subunit of the complex.
Pyruvate dehydrogenase deficiency
Glutaminase deficiency
Pyruvate carboxylase deficiency
Pyruvate kinase deficiency
3-Methylcrotonyl-CoA carboxylase deficiency
Malonyl-CoA decarboxylase deficiency
2-Methylbutyryl-CoA dehydrogenase deficiency
D-glycerate dehydrogenase deficiency