pairidaza

Pairidaza is an enzyme that belongs to the family of amidohydrolases. It is involved in the degradation of certain amino acids, particularly the branched-chain amino acids leucine, isoleucine, and valine. The enzyme catalyzes the hydrolysis of these amino acids to their corresponding α-keto acids and ammonia. Pairidaza is found in various organisms, including bacteria, fungi, and plants. In plants, it plays a crucial role in the regulation of amino acid levels, which is essential for growth and development. The enzyme is also involved in the metabolism of certain drugs, such as the antibiotic rifampicin, which is degraded by pairidaza in bacteria. Pairidaza is a dimeric enzyme, consisting of two identical subunits. Each subunit contains a catalytic triad consisting of serine, histidine, and aspartic acid residues. The active site of the enzyme is located at the interface between the two subunits. Pairidaza is inhibited by certain compounds, such as isoleucine and valine, which are competitive inhibitors. The inhibition of pairidaza can lead to the accumulation of branched-chain amino acids and has been studied as a potential target for the development of new drugs. The gene encoding pairidaza is conserved across different organisms, indicating its importance in amino acid metabolism. Pairidaza is a key enzyme in the degradation of branched-chain amino acids and plays a significant role in the regulation of amino acid levels in various organisms.