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090			_aB-19297
245	1	0	_aStructural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs)
490	0		_vBiochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1865(11), p.158590, 2020
520	3		_aCarotenoid cleavage dioxygenases (CCDs)comprise a superfamily of mononuclear non-heme iron proteins that catalyze the oxygenolytic fission of alkene bonds in carotenoids to generate apocarotenoid products. Some of these enzymes exhibit additional activities such as carbon skeleton rearrangement and trans-cis isomerization. The group also includes a subfamily of enzymes that split the interphenyl alkene bond in molecules such as resveratrol and lignostilbene. CCDs are involved in numerous biological processes ranging from production of light-sensing chromophores to degradation of lignin derivatives in pulping waste sludge. These enzymes exhibit unique features that distinguish them from other families of non-heme iron enzymes. The distinctive properties and biological importance of CCDs have stimulated interest in their modes of catalysis. Recent structural, spectroscopic, and computational studies have helped clarify mechanistic aspects of CCD catalysis. Here, we review these findings emphasizing common and unique properties of CCDs that enable their variable substrate specificity and regioselectivity.
650	1	4	_aNON-HEME IRON
650	1	4	_aBETA-PROPELLER
650	1	4	_aNITRIC OXIDE
650	1	4	_aRESVERATROL
650	1	4	_aDIOXETANE
650	1	4	_aMONOTOPIC MEMBRANE PROTEIN
700	1	2	_aDaruwalla, A.
700	1	2	_aKiser, P. D.
856	4	0	_uhttps://drive.google.com/file/d/1v9oymx1zU5X7_IOXRlj5HRVb3G4S9HxU/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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