Evidence of interallelic complementation at clinically relevant loci is limited to biochemical and cell - based studies of a handful of metabolic disorders with defects in enzymes including propinyl - CoA carboxylase [2], argininosuccinate lyase [3], galactose -1-phosphate uridylyltransferase [4], and methylmalonyl
CoA mutase [5].
Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus
chorismate mutase fold and suggest a role in amino - acid metabolism.
Researchers from the Chinese Academy of Sciences have discovered that the metabolic enzyme
phosphoglycerate mutase 1 (PGAM1) helps cancer cells repair their DNA and found that inhibiting PGAM1 sensitizes tumors to the cancer drug Olaparib (Lynparza).
Their findings in the study «
Phosphoglycerate mutase 1 regulates dNTP pool and promotes homologous recombination repair in cancer cells,» which has been published in The Journal of Cell Biology, suggest that this FDA - approved ovarian cancer medicine has the potential to treat a wider range of cancer types than currently indicated.
The enzyme, known as methylmalonyl -
CoA mutase (MUT), is made primarily in the liver, and it helps break down proteins and fats in food.
The researchers» target was
chorismate mutase (CM), an enzyme that helps bacteria and higher plants make certain amino acids.
The enzyme, called methylmalonyl - CoA
mutase (MUT), is an important component of the chemical process that metabolizes organic acids, specifically methylmalonic acid.