Thioredoxin reductases (TR, TrxR) (EC 1.8.1.9) are enzymes that reduce thioredoxin (Trx).[1] Two classes of thioredoxin reductase have been identified: one class in bacteria and some eukaryotes and one in animals. In bacteria TrxR also catalyzes the reduction of glutaredoxin like proteins known as NrdH.[2][3][4] Both classes are flavoproteins which function as homodimers. Each monomer contains a FAD prosthetic group, a NADPH binding domain, and an active site containing a redox-active disulfide bond.[5]
^Jordan A, Aslund F, Pontis E, Reichard P, Holmgren A (July 1997). "Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile". The Journal of Biological Chemistry. 272 (29): 18044–50. doi:10.1074/jbc.272.29.18044. PMID 9218434.
^Phulera S, Mande SC (June 2013). "The crystal structure of Mycobacterium tuberculosis NrdH at 0.87 Å suggests a possible mode of its activity". Biochemistry. 52 (23): 4056–65. doi:10.1021/bi400191z. PMID 23675692.
^Phulera S, Akif M, Sardesai AA, Mande SC (2014-01-01). "Redox Proteins of Mycobacterium tuberculosis". Journal of the Indian Institute of Science. 94 (1): 127–138. ISSN 0970-4140.
^Hirt RP, Müller S, Embley TM, Coombs GH (July 2002). "The diversity and evolution of thioredoxin reductase: new perspectives". Trends in Parasitology. 18 (7): 302–8. doi:10.1016/S1471-4922(02)02293-6. PMID 12379950.
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