Identification of a New Type of Mammalian Peroxiredoxin That Forms an Intramolecular Disulfide as a Reaction Intermediate

• Published in: The Journal of biological chemistry Vol. 275; no. 27; pp. 20346 - 20354
• Main Authors: Seo, Min Seok, Kang, Sang Won, Kim, Kanghwa, Baines, Ivan C., Lee, Tae Hoon, Rhee, Sue Goo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07.07.2000; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; Cell Line; Cloning, Molecular; Conserved Sequence; Cysteine - genetics; Disulfides - chemistry; Enzyme Activation; Glutaredoxins; Humans; Hydrogen Peroxide - metabolism; JNK Mitogen-Activated Protein Kinases; Mitogen-Activated Protein Kinases - metabolism; Molecular Sequence Data; Mutation; Oxidoreductases; Peroxidases - chemistry; Peroxidases - genetics; Peroxiredoxins; Protein Isoforms - metabolism; Proteins - metabolism; Recombinant Proteins - metabolism; Sequence Alignment; Thioredoxins - metabolism

Peroxidases of the peroxiredoxin (Prx) family contain a Cys residue that is preceded by a conserved sequence in the NH2-terminal region. A new type of mammalian Prx, designated PrxV, has now been identified as the result of a data base search with this conserved Cys-containing sequence. The 162-amin...