carD function substantiated by its targeted disruption in a Fusarium fujikuroi carotenoid-overproducing strain, which resulted in the loss of neurosporaxanthin and the accumulation of beta-apo-4'-carotenal
C20-retinal i.e. beta-apo-15'-carotenal is not converted by carD enzymatic activity, indicating the requirement for a minimal length of the substrate chain
carD function substantiated by its targeted disruption in a Fusarium fujikuroi carotenoid-overproducing strain, which resulted in the loss of neurosporaxanthin and the accumulation of beta-apo-4'-carotenal
dominating carotenoids in the Ylo mutant are 4'-apolycopene-4'-myristate and 4'-apo-gamma-carotene-4'-myristate. In vivo, the aldehyde intermediates 4'-apo-gamma-carotene-4'-al and 4'-apo-lycopene-4'-al do not accumulate substantially but are reduced instead to the corresponding alcohols, 4'-apolycopene-4'-ol and 4'-apo-gamma-carotene-4'-ol, and both further esterified with mainly myristic acid yielding 4'-apolycopene-4'-myristate and 4'-apo-gamma-carotene-4'-myristate
enzyme is involved in the biosynthetic pathway to neurosporaxanthin. First step is the cleavage of 3,4-didehydrolycopene into apo-4'-lycopenal by Cao2, which is then oxidized by YLO-1 to yield apo-4'-lycopenoic acid, the last intermediate in the pathway. The final step is then catalyzed by the cyclase activity of AL-2. An Ylo-1 mutant accumulates three major pigments, i.e. lycopene, apo-4'-lycopenal and apo-4'-lycopenol. The pigments accumulating in the Ylo-1 mutant are non-cyclic and represent lycopene and apolycopenoids, indicating that the in vivo substrate of Ylo-1 is apo-4'-lycopenal rather than its cyclic isomer beta-apo-4'-carotenal
targeted disruption of CarD in a Gibberella fujikuroi carotenoid-overproducing strain results in the loss of neurosporaxanthin and the accumulation of beta-apo-4'-carotenal, its derivative beta-apo-4'-carotenol, and minor amounts of other carotenoids. Strains harboring the CarD mutation acquire a yellowish pigmentation
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1.2.1.82 beta-apo-4'-carotenal oxygenase
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