CRYZ explained

Quinone oxidoreductase is an enzyme that in humans is encoded by the CRYZ gene.^[1]

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. The former class is also called phylogenetically-restricted crystallins. This gene encodes a taxon-specific crystallin protein which has NADPH-dependent quinone reductase activity distinct from other known quinone reductases. It lacks alcohol dehydrogenase activity although by similarity it is considered a member of the zinc-containing alcohol dehydrogenase family. Unlike other mammalian species, in humans, lens expression is low. One pseudogene is known to exist.

Further reading

• Heinzmann C, Kojis TL, Gonzalez P . Assignment of the zeta-crystallin gene (CRYZ) to human chromosome 1p22-p31 and identification of restriction fragment length polymorphisms . Genomics . 23 . 2 . 403–7 . 1995 . 7835889 . 10.1006/geno.1994.1516 . etal.
• Gonzalez P, Rao PV, Zigler JS . Organization of the human zeta-crystallin/quinone reductase gene (CRYZ) . Genomics . 21 . 2 . 317–24 . 1994 . 8088825 . 10.1006/geno.1994.1272 .
• Maruyama K, Sugano S . Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides . Gene . 138 . 1–2 . 171–4 . 1994 . 8125298 . 10.1016/0378-1119(94)90802-8 .
• Gonzalez P, Rao PV, Zigler JS . Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver . Biochem. Biophys. Res. Commun. . 191 . 3 . 902–7 . 1993 . 8466529 . 10.1006/bbrc.1993.1302 .
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K . Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library . Gene . 200 . 1–2 . 149–56 . 1997 . 9373149 . 10.1016/S0378-1119(97)00411-3 . etal.
• Wang W, Liu LQ, Higuchi CM, Chen H . Induction of NADPH:quinone reductase by dietary phytoestrogens in colonic Colo205 cells . Biochem. Pharmacol. . 56 . 2 . 189–95 . 1998 . 9698072 . 10.1016/S0006-2952(98)00141-5 .
• Goenka S, Raman B, Ramakrishna T, Rao CM . Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation . Biochem. J. . 359 . Pt 3 . 547–56 . 2001 . 11672428 . 10.1042/0264-6021:3590547 . 1222175 .
• Strausberg RL, Feingold EA, Grouse LH . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . etal. free .
• Bianco NR, Perry G, Smith MA . Functional implications of antiestrogen induction of quinone reductase: inhibition of estrogen-induced deoxyribonucleic acid damage . Mol. Endocrinol. . 17 . 7 . 1344–55 . 2004 . 12714703 . 10.1210/me.2002-0382 . etal. free .
• Ota T, Suzuki Y, Nishikawa T . Complete sequencing and characterization of 21,243 full-length human cDNAs . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . etal. free .
• Gerhard DS, Wagner L, Feingold EA . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . etal.

Notes and References

1. Web site: Entrez Gene: CRYZ crystallin, zeta (quinone reductase).