Pyridine nucleotide-disulphide oxidoreductase domain 1

Pyridine nucleotide-disulphide oxidoreductase domain 1 (Pyr_redox_1) is a protein domain that is part of the pyridine nucleotide-disulphide oxidoreductase family. This domain is found in a variety of enzymes, including glutathione reductase, trypanothione reductase, and mercaptopyruvate sulfurtransferase.

Structure

The Pyr_redox_1 domain is approximately 100 amino acids in length and forms a Rossmann fold, a common protein structure motif that binds nucleotides such as FAD or NAD(P)H. The domain contains a conserved sequence motif, GXGXXG, which is involved in binding the adenine portion of FAD or NAD(P)H.

Function

Enzymes containing the Pyr_redox_1 domain are involved in various redox reactions, particularly those involving the reduction of disulphide bonds. These enzymes play crucial roles in maintaining the redox state of the cell and protecting against oxidative stress.

Clinical significance

Mutations in the Pyr_redox_1 domain can lead to dysfunction of the enzymes in which it is found, potentially leading to various diseases. For example, mutations in glutathione reductase can lead to hemolytic anemia, while mutations in trypanothione reductase can lead to increased susceptibility to trypanosomiasis.

See also

• Pyridine nucleotide-disulphide oxidoreductase
• Glutathione reductase
• Trypanothione reductase
• Mercaptopyruvate sulfurtransferase