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PROSITE documentation PDOC00073Pyridine nucleotide-disulphide oxidoreductases class-I active site
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00073
The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contains a pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate. On the basis of sequence and structural similarities [1] these enzymes can be classified into two categories. The first category groups together the following enzymes [2,3,4,5,6]:
- Glutathione reductase (EC 1.8.1.7) (GR).
- Higher eukaryotes thioredoxin reductase (EC 1.8.1.9).
- Trypanothione reductase (EC 1.8.1.12).
- Lipoamide dehydrogenase (EC 1.8.1.4), the E3 component of α-ketoacid dehydrogenase complexes.
- Mercuric reductase (EC 1.16.1.1).
The sequence around the two cysteines involved in the redox-active disulfide bond is conserved and can be used as a signature pattern.
Note:In positions 6 and 7 of the pattern all known sequences have Asn-(Val/ Ile) with the exception of GR from plant chloroplasts and from cyanobacteria which have Ile-Arg [7].
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Kurlyan J. Krishna T.S.R. Wong L. Guenther B. Pahler A. Williams C.H. Jr. Model P. |
| Source | Nature 352:172-174(1991). |
| 2 | Authors | Rice D.W. Schulz G.E. Guest J.R. |
| Title | Structural relationship between glutathione reductase and lipoamide dehydrogenase. | |
| Source | J. Mol. Biol. 174:483-496(1984). | |
| PubMed ID | 6546954 |
| 3 | Authors | Brown N.L. |
| Source | Trends Biochem. Sci. 10:400-402(1985). |
| 4 | Authors | Carothers D.J. Pons G. Patel M.S. |
| Title | Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. | |
| Source | Arch. Biochem. Biophys. 268:409-425(1989). | |
| PubMed ID | 2643922 |
| 5 | Authors | Walsh C.T. Bradley M. Nadeau K. |
| Title | Molecular studies on trypanothione reductase, a target for antiparasitic drugs. | |
| Source | Trends Biochem. Sci. 16:305-309(1991). | |
| PubMed ID | 1957352 |
| 6 | Authors | Gasdaska P.Y. Gasdaska J.R. Cochran S. Powis G. |
| Title | Cloning and sequencing of a human thioredoxin reductase. | |
| Source | FEBS Lett. 373:5-9(1995). | |
| PubMed ID | 7589432 |
| 7 | Authors | Creissen G. Edwards E.A. Enard C. Wellburn A. Mullineaux P. |
| Title | Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.). | |
| Source | Plant J. 2:129-131(1992). | |
| PubMed ID | 1303792 |
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