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- * Pyridine nucleotide-disulphide oxidoreductases class-I active site *
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-
- 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 to 5]:
-
- - Glutathione reductase (EC 1.6.4.2) (GR).
- - Trypanothione reductase (EC 1.6.4.8).
- - Lipoamide dehydrogenase (EC 1.8.1.4), the E3 component of alpha-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.
-
- -Consensus pattern: G-G-x-C-[LIVA]-x(2)-G-C-[LIVM]-P
- [The two C's form the active site disulfide bond]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -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 [6].
-
- -Last update: October 1993 / Pattern and text revised.
-
- [ 1] Kurlyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A.,
- Williams C.H. Jr., Model P.
- Nature 352:172-174(1991).
- [ 2] Rice D.W., Schulz G.E., Guest J.R.
- J. Mol. Biol. 174:483-496(1984).
- [ 3] Brown N.L.
- Trends Biochem. Sci. 10:400-402(1985).
- [ 4] Carothers D.J., Pons G., Patel M.S.
- Arch. Biochem. Biophys. 268:409-425(1989).
- [ 5] Walsh C.T., Bradley M., Nadeau K.
- Trends Biochem. Sci. 16:305-309(1991).
- [ 6] Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.
- Plant J. 2:129-131(1991).
-