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Plant carotene cis-trans isomerase CRTISO : a new member of the FAD<sub>RED</sub>-dependent flavoproteins catalyzing non-redox reactions

Plant carotene cis-trans isomerase CRTISO : a new member of the FADRED-dependent flavoproteins catalyzing non-redox reactions

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YU, Qiuju, Sandro GHISLA, Joseph HIRSCHBERG, Varda MANN, Peter BEYER, 2011. Plant carotene cis-trans isomerase CRTISO : a new member of the FADRED-dependent flavoproteins catalyzing non-redox reactions. In: The Journal of Biological Chemistry (JBC). American Society for Biochemistry and Molecular Biology. 286(10), pp. 8666-8676. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M110.208017

@article{Yu2011-03-11Plant-51076, title={Plant carotene cis-trans isomerase CRTISO : a new member of the FADRED-dependent flavoproteins catalyzing non-redox reactions}, year={2011}, doi={10.1074/jbc.M110.208017}, number={10}, volume={286}, issn={0021-9258}, journal={The Journal of Biological Chemistry (JBC)}, pages={8666--8676}, author={Yu, Qiuju and Ghisla, Sandro and Hirschberg, Joseph and Mann, Varda and Beyer, Peter} }

Mann, Varda Hirschberg, Joseph 2020-09-29T07:23:01Z Beyer, Peter Plant carotene cis-trans isomerase CRTISO : a new member of the FAD<sub>RED</sub>-dependent flavoproteins catalyzing non-redox reactions Yu, Qiuju 2020-09-29T07:23:01Z Ghisla, Sandro Beyer, Peter Mann, Varda Hirschberg, Joseph The carotene cis-trans isomerase CRTISO is a constituent of the carotene desaturation pathway as evolved in cyanobacteria and prevailing in plants,in which a tetra-cis-lycopene species, termed prolycopene, is formed. CRTISO, an evolutionary descendant of the bacterial carotene desaturaseCRTI, catalyzes the cis-to-trans isomerization reactions leading to all-trans-lycopene, the substrate for the subsequent lycopene cyclization to form all-trans-α/β-carotene. CRTISO and CRTI share a dinucleotide binding motif at the N terminus. Here we report that this site is occupiedby FAD in CRTISO. The reduced form of this cofactor catalyzes a reaction not involving net redox changes. Results obtainedwith C(1)- and C(5)-deaza-FAD suggest mechanistic similarities with type II isopentenyl diphosphate: dimethylallyl diphosphateisomerase (IDI-2). CRTISO, together with lycopene cyclase CRTY and IDI-2, thus represents the third enzyme in isoprenoid metabolismbelonging to the class of non-redox enzymes depending on reduced flavin for activity. The regional specificity and the kineticsof the isomerization reaction were investigated in vitro using purified enzyme and biphasic liposome-based systems carrying specific cis-configured lycopene species as substrates. The reaction proceeded from cis to trans, recognizing half-sides of the symmetrical prolycopene and was accompanied by one trans-to-cis isomerization step specific for the C(5)-C(6) double bond. Rice lycopene β-cyclase (OsLCY-b), when additionally introducedinto the biphasic in vitro system used, was found to be stereospecific for all-trans-lycopene and allowed the CRTISO reaction to proceed toward completion by modifying the thermodynamics of the overall reaction. eng Yu, Qiuju Ghisla, Sandro 2011-03-11

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