The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including beta-carotene, alpha-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including beta-carotene, alpha-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
11-cis-3-hydroxyretinal and 11-cis-retinal exist in a molar ratio of 8:1, indicating that the enzyme preferentially isomerizes the half site of cryptoxanthin with the hydroxylated beta-ionone ring
enzyme catalyzes the production of 11-cis-retinal and all-trans-retinal, i.e. cleavage at the 15,15' double bond. The 11-cis-retinal product maybe thermally converted either into the all-trans or the 13-cis stereoisomer in the aqueous test solution
enzyme cleaves the central C15-C15' and an excentric double bond at the C13-C14 position, leading to retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone (C18) from beta-carotene, as well as the corresponding hydroxylated products from zeaxanthin and lutein. Enzyme also cleaves 3,3'-dihydroxy-isorenieratene representing aromatic carotenoids synthesized by other mycobacteria. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring. Incubation of apocarotenoids shorter than beta-apo-10'-carotenal reveals only weak activity, substrates with a shorter chain length are not converted
enzyme cleaves the central C15-C15' and an excentric double bond at the C13-C14 position, leading to retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone (C18) from beta-carotene, as well as the corresponding hydroxylated products from zeaxanthin and lutein. Enzyme also cleaves 3,3'-dihydroxy-isorenieratene representing aromatic carotenoids synthesized by other mycobacteria. The preference for each of the cleavage positions is determined by the hydroxylation and the nature of the ionone ring. Incubation of apocarotenoids shorter than beta-apo-10'-carotenal reveals only weak activity, substrates with a shorter chain length are not converted
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Tuberculosis
The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase mediating central and excentric cleavage of conventional and aromatic carotenoids.
mutants show no photophobic behavior indicating that NinaB is essential for larval light perception. Enzyme expression and chromophore production is governed by eyeless and so, major control genes for eye development
the catalytic efficiency of the mutant is 1.6fold that of the wild type enzyme. The mutant exhibits better thermostability than that of wild type. Under temperatures lower than 30°C, mutant A49P retains almost all the activities within the shorter incubation time (less than 5 h). The mutant also shows better performance even at 35°C
the catalytic efficiency of the mutant is 1.6fold that of the wild type enzyme. The mutant exhibits better thermostability than that of wild type. Under temperatures lower than 30°C, mutant A49P retains almost all the activities within the shorter incubation time (less than 5 h). The mutant also shows better performance even at 35°C
the enzyme retains about 70-90% activity after approximately 3 h at 15-23°C. At 30°C, the enzyme maintains about 50% activity after 3 h incubation. The enzyme is inactivated after about 3 h at 35°C
Scherzinger, D.; Scheffer, E.; Bar, C.; Ernst, H.; Al-Babili, S.
The Mycobacterium tuberculosis ORF Rv0654 encodes a carotenoid oxygenase mediating central and excentric cleavage of conventional and aromatic carotenoids
Hoffmann, J.; Bona-Lovasz, J.; Beuttler, H.; Altenbuchner, J.
In vivo and in vitro studies on the carotenoid cleavage oxygenases from Sphingopyxis alaskensis RB2256 and Plesiocystis pacifica SIR-1 revealed their substrate specificities and non-retinal-forming cleavage activities