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| 090 | _aB-17992 | ||
| 245 | 1 | 0 | _aThe structure of a retinal-forming carotenoid oxigenase |
| 490 | 0 | _vScience, 308(5719), p.267-269, 2005 | |
| 520 | 3 | _aEnzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed ?-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen. | |
| 650 | 1 | 4 | _aCAROTENOID OXYGENASE |
| 700 | 1 | 2 | _aKloer, D. P. |
| 700 | 1 | 2 | _aRuch, S. |
| 700 | 1 | 2 | _aAl-Babili, S. |
| 700 | 1 | 2 | _aBeyer, P. |
| 700 | 1 | 2 | _aSchulz, G. E. |
| 856 | 4 | 0 |
_uhttps://drive.google.com/file/d/1XHMi074oCPi4cltc2APs3zZF0ll04qxt/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
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