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Title:
A novel carotenoid biosynthesis gene coding for ζ-carotene desaturase: functional expression, sequence and phylogenetic origin | Plant Molecular Biology
Description:
A DNA fragment which has been isolated previously from an Anabaena DNA expression library was subcloned. The corresponding protein was overexpressed in Escherichia coli. The recombinant enzyme was fully active in converting ζ-carotene into lycopene in vitro with neurosporene as an intermediate. A smaller fragment which still contained the active enzyme was sequenced. An open reading frame of 1497 bp was found coding for a protein consisting of 499 amino acids with the calculated molecular weight of 56 740. In a computer search of nucleotide sequences contained in the EMBL nucleotide sequence library, all the best-fitting comparisons were carotenoid desaturases. The highest similarity was found with the crtI phytoene desaturase genes of bacteria and the al-1 gene from Neurospora crassa. A much lower similarity was found with the pds genes coding for phytoene desaturase from cyanobacteria and higher plants. It is shown in protein similarity plots that the amino acid similarity of ζ-carotene desaturase to the latter is mainly limited to the N terminus of the polypeptides. In contrast, the protein similarity plots and a comparison of a conserved region clearly demonstrate that there is a strong relationship between ζ-carotene desaturase and the phytoene desaturases from various bacteria and fungi. Therefore we propose that the ζ-carotene desaturase gene is homologous to the crt I phytoene desaturase genes of bacteria and fungi.
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Keywords {🔍}
google, scholar, desaturase, carotenoid, gene, phytoene, article, biosynthesis, molecular, ζcarotene, sequence, plant, sandmann, linden, misawa, genes, biology, coding, expression, dna, protein, coli, usa, biol, biochem, privacy, cookies, content, search, escherichia, similarity, access, nature, mol, proc, natl, acad, sci, carotenoids, analysis, publish, research, functional, anabaena, nucleotide, bacteria, products, pecker, chamovitz, hirschberg,
Topics {✒️}
month download article/chapter ζ-carotene desaturase gene phytoene desaturase genes pds genes coding single-stranded plasmid dna anabaena pcc 7120 norihiko misawa carotenoid biosynthesis pathway ζ-carotene desaturase open reading frame cold spring harbor carotenoid biosynthetic gene key technology converting ζ-carotene privacy choices/manage cookies full article pdf gene products expressed phytoene desaturase gene carotene patterns derives phytoene desaturase diversification check access instant access phytoene desaturase reaction calculated molecular weight carotenoid biosynthesis european economic area xanthophyllomyces dendrorhous leading related subjects mathews-roth mm nadp-binding sites single polypeptide catalyzing tomato fruit ripening chain-terminating inhibitors ribosome binding sites soybean cdna coding conditions privacy policy kluwer academic publishers ζ-carotene cyanobacterium anabaena 7120 accepting optional cookies amino acid similarity protein similarity plots nucleotide sequences contained main content log flavoprotein disulfide oxidoreductases article linden carotenoid pathway conserved enzymes mediate journal finder publish phylogenetic origin
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headline:A novel carotenoid biosynthesis gene coding for ζ-carotene desaturase: functional expression, sequence and phylogenetic origin
description:A DNA fragment which has been isolated previously from an Anabaena DNA expression library was subcloned. The corresponding protein was overexpressed in Escherichia coli. The recombinant enzyme was fully active in converting ζ-carotene into lycopene in vitro with neurosporene as an intermediate. A smaller fragment which still contained the active enzyme was sequenced. An open reading frame of 1497 bp was found coding for a protein consisting of 499 amino acids with the calculated molecular weight of 56 740. In a computer search of nucleotide sequences contained in the EMBL nucleotide sequence library, all the best-fitting comparisons were carotenoid desaturases. The highest similarity was found with the crtI phytoene desaturase genes of bacteria and the al-1 gene from Neurospora crassa. A much lower similarity was found with the pds genes coding for phytoene desaturase from cyanobacteria and higher plants. It is shown in protein similarity plots that the amino acid similarity of ζ-carotene desaturase to the latter is mainly limited to the N terminus of the polypeptides. In contrast, the protein similarity plots and a comparison of a conserved region clearly demonstrate that there is a strong relationship between ζ-carotene desaturase and the phytoene desaturases from various bacteria and fungi. Therefore we propose that the ζ-carotene desaturase gene is homologous to the crt I phytoene desaturase genes of bacteria and fungi.
datePublished:
dateModified:
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carotenoid biosynthesis
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Plant Sciences
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headline:A novel carotenoid biosynthesis gene coding for ζ-carotene desaturase: functional expression, sequence and phylogenetic origin
description:A DNA fragment which has been isolated previously from an Anabaena DNA expression library was subcloned. The corresponding protein was overexpressed in Escherichia coli. The recombinant enzyme was fully active in converting ζ-carotene into lycopene in vitro with neurosporene as an intermediate. A smaller fragment which still contained the active enzyme was sequenced. An open reading frame of 1497 bp was found coding for a protein consisting of 499 amino acids with the calculated molecular weight of 56 740. In a computer search of nucleotide sequences contained in the EMBL nucleotide sequence library, all the best-fitting comparisons were carotenoid desaturases. The highest similarity was found with the crtI phytoene desaturase genes of bacteria and the al-1 gene from Neurospora crassa. A much lower similarity was found with the pds genes coding for phytoene desaturase from cyanobacteria and higher plants. It is shown in protein similarity plots that the amino acid similarity of ζ-carotene desaturase to the latter is mainly limited to the N terminus of the polypeptides. In contrast, the protein similarity plots and a comparison of a conserved region clearly demonstrate that there is a strong relationship between ζ-carotene desaturase and the phytoene desaturases from various bacteria and fungi. Therefore we propose that the ζ-carotene desaturase gene is homologous to the crt I phytoene desaturase genes of bacteria and fungi.
datePublished:
dateModified:
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pageEnd:379
sameAs:https://doi.org/10.1007/BF00020174
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carotenoid biosynthesis
ζ-carotene desaturase
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