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Protein Domain : Pyridine nucleotide-disulphide oxidoreductase, class I

Primary Identifier  IPR001100 Type  Family
Short Name  Pyr_nuc-diS_OxRdtase
description  The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazinering of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residuethat is usually a part of a redox-active disulphide bridge. In a secondstep, the reduced disulphide reduces the substrate. On the basis of sequence and structural similarities [], PNDR can be categorised into 2groups.Class I includes glutathione reductase, trypanothione reductase,lipoamide dehydrogenase and mercuric reductase. They cover a wide range ofcatalytic functions: glutathione reductase ensures that the cell has enough reduced glutathione to maintain protein thiol groups in the reducedstate []; trypanothione reductase carries out the analogous reaction in trypanosomal cells (trypanothione is an analogue of glutathione) []; lipoamide dehydrogenase, the E3 component of alpha-ketoacid dehydrogenasemultienzyme complex, oxidises the dihydrolypoyl groups of lipoate acyltransferase, and so couples glycolysis to the tricarboxylic acid cycle []; and mercuric reductase enables bacteria to detoxify the mercuric ionby reducing it to elemental mercury, which evaporates from the cell [].

7 Child Features

0 Parent Features

16 Protein Domain Regions