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- *****************************************
- * Aldo/keto reductase family signatures *
- *****************************************
-
- The aldo-keto reductase family [1] groups together a number of structurally
- and functionally related NADPH-dependent oxidoreductases as well as some other
- proteins. The proteins known to belong to this family are:
-
- - Aldehyde reductase (EC 1.1.1.2).
- - Aldose reductase (EC 1.1.1.21).
- - 3-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.50) [2], which terminates
- androgen action by converting 5-alpha-dihydrotestosterone to 3-alpha-
- androstanediol.
- - Prostaglandin F synthase (EC 1.1.1.188) which catalyzes the reduction of
- prostaglandins H2 and D2 to F2-alpha.
- - D-sorbitol-6-phosphate dehydrogenase (EC 1.1.1.200) from Apple tree [3].
- - Morphine 6-dehydrogenase (EC 1.1.1.218) [4] from Pseudomonas putida plasmid
- pMDH7.2.
- - Chlordecone reductase (EC 1.1.1.225) [5] which reduces the pesticide
- chlordecone (kepone) to the corresponding alcohol.
- - 2,5-diketo-D-gluconic acid reductase (EC 1.1.1.-) which catalyzes the
- reduction of 2,5-diketogluconic acid to 2-keto-L-gulonic acid, a key
- intermediate in the production of ascorbic acid.
- - NAD(P)H-dependent xylose reductase (EC 1.1.1.-) from the yeast Pichia
- stipitis [6]. This enzyme reduces xylose into xylit.
- - Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.20).
- - 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.99.6) which catalyzes the
- reduction of delta(4)-3-oxosteroids.
- - A soybean reductase, which co-acts with chalcone synthase in the formation
- of 4,2',4'-trihydroxychalcone [6].
- - Frog eye lens rho crystallin.
- - Yeast GCY protein, whose function is not known.
- - Leishmania major P110/11E protein [7]. P110/11E is a developmentally
- regulated protein whose abundance is markedly elevated in promastigotes
- compared with amastigotes. Its exact function is not yet known.
- - Escherichia coli hypothetical protein yafB.
-
- These proteins have all about 300 amino acid residues. We derived 3 consensus
- patterns specific to this family of proteins. The first one is located in the
- N-terminal section of these proteins. The second pattern is located in the
- central section. The third pattern, located in the C-terminal, is centered on
- a lysine residue whose chemical modification, in aldose and aldehyde
- reductases, affect the catalytic efficiency.
-
- -Consensus pattern: G-[FY]-R-[HAL]-[LIVMF]-D-[STAGC]-A-x(5)-E-x(2)-[LIVM]-G
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [LIVMFY]-x(9)-[KREQ]-x-[LIVM]-G-[LIVM]-[SC]-N-[FY]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: Escherichia coli protein glgX and a
- retrovirus-related pol polyprotein from Sciara coprophila.
-
- -Consensus pattern: [LIVMFYS]-[EQ]-x(5)-[LIVM]-x-[KR]-S-x(4)-R-x(6)-[LIVM]-
- [LFN]
- [K is a putative active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for morphine 6-dehydrogenase and Escherichia coli yafB.
- -Other sequence(s) detected in SWISS-PROT: mouse 5-HT-3 receptor.
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.
- J. Biol. Chem. 264:9547-9551(1989).
- [ 2] Pawlowski J.E., Huizinga M., Penning T.M.
- J. Biol. Chem. 266:8820-8825(1991).
- [ 3] Kanayama Y., Mori H., Imaseki H., Yamaki S.
- EMBL/GenBank: D11080.
- [ 4] Willey D.L., Caswell D.A., Lowe C.R., Bruce N.C.
- Biochem. J. 290:539-544(1993).
- [ 5] Winters C.J., Molowa D.T., Guzelian P.S.
- Biochemistry 29:1080-1087(1990).
- [ 6] Amore R., Koetter P., Kuester C., Ciriacy M., Hollenberg C.P.
- Gene 109:89-97(1991).
- [ 7] Welle R., Schroeder G., Schiltz E., Grisebach H., Schroeder J.
- Eur. J. Biochem. 196:423-430(1991).
- [ 8] Samaras N., Spithill T.W.
- J. Biol. Chem. 264:4251-4254(1989).
-