Structural and functional analysis of the gene cluster encoding carotenoid biosynthesis in<i>Mycobacterium aurum</i>A+

Viveiros, Miguel; Krubasik, Philipp; Sandmann, Gerhard; Houssaini-Iraqui, Mohamed

doi:10.1111/j.1574-6968.2000.tb09143.x

Cited by 47 publications

(8 citation statements)

References 26 publications

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“…18 and 19), Streptomyces spp. (17), and the Chloroflexi; the CrtL family, which includes the ␤-and -cyclases in some cyanobacteria and plants (20,21); and the heterodimeric cyclases of some Gram-positive bacteria (22,23), which are related to the lycopene cyclases of archaea (24,25) and halophilic bacteria (26). These classes are distantly related to each other and share only a few conserved motifs, including an N-terminal flavin-binding domain that is found in the first two groups but appears to be missing in the third (27).…”

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confidence: 99%

Identification of a fourth family of lycopene cyclases in photosynthetic bacteria

Maresca

Graham

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

133

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A fourth and large family of lycopene cyclases was identified in photosynthetic prokaryotes. The first member of this family, encoded by the cruA gene of the green sulfur bacterium Chlorobium tepidum, was identified in a complementation assay with a lycopene-producing strain of Escherichia coli. Orthologs of cruA are found in all available green sulfur bacterial genomes and in all cyanobacterial genomes that lack genes encoding CrtL-or CrtY-type lycopene cyclases. The cyanobacterium Synechococcus sp. PCC 7002 has two homologs of CruA, denoted CruA and CruP, and both were shown to have lycopene cyclase activity. Although all characterized lycopene cyclases in plants are CrtL-type proteins, genes orthologous to cruP also occur in plant genomes. The CruA-and CruP-type carotenoid cyclases are members of the FixC dehydrogenase superfamily and are distantly related to CrtL-and CrtY-type lycopene cyclases. Identification of these cyclases fills a major gap in the carotenoid biosynthetic pathways of green sulfur bacteria and cyanobacteria.carotenogenesis ͉ carotenoids ͉ cyanobacteria ͉ green sulfur bacteria ͉ photosynthesis C olored carotenoids are found in nearly all photosynthetic species and in a variety of nonphotosynthetic organisms and play roles in light-harvesting, photoprotection, structural maintenance of pigment-protein complexes (1), and membrane structure and fluidity (2). The cyclization of the linear compound lycopene to produce ␣-, ␤-, ␥-, or -carotene is a branch point in carotenoid biosynthetic pathways in many species of bacteria, plants, and fungi (3, 4). The monocyclic ␥-carotene is a precursor to myxoxanthophylls in cyanobacteria (5, 6), is both an intermediate and an end product of carotenogenesis in orange and yellow flowers and fruits (7-10), and is an intermediate in chlorobactene biosynthesis in green sulfur bacteria (GSB) (11-13). Dicyclic ␤-carotene is a major component of photosystems (PS) I and II in cyanobacteria and plants (14,15) and is modified to isorenieratene in brown-colored GSB and some actinomycetes (16,17).Three classes of lycopene cyclases have previously been identified in bacteria: the CrtY-type ␤-cyclases that are found in many carotenogenic proteobacteria (e.g., refs. 18 and 19), Streptomyces spp. (17), and the Chloroflexi; the CrtL family, which includes the ␤-and -cyclases in some cyanobacteria and plants (20,21); and the heterodimeric cyclases of some Gram-positive bacteria (22, 23), which are related to the lycopene cyclases of archaea (24, 25) and halophilic bacteria (26). These classes are distantly related to each other and share only a few conserved motifs, including an N-terminal flavin-binding domain that is found in the first two groups but appears to be missing in the third (27). Carotenoid monocyclases are found in both the CrtY and CrtL families (28-30), and there are no obvious sequence differences between mono-and dicyclases (28).The cyclization of lycopene to ␥-or ␤-carotene is an isomerization reaction, which produces no net change in mass or redox state o...

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confidence: 99%

Identification of a fourth family of lycopene cyclases in photosynthetic bacteria

Maresca

Graham

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

133

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“…CrtYc and CrtYd are the two-peptide types of lycopene β-cyclases. CrtYc and CrtYd are usually found in the bacteria Brevibacterium linens and Mycobacterium aurum . − The two individual proteins are encoded by crtYc and crtYd , respectively, and they then combine to form a heterodimeric cyclase with β-monocyclic activity to produce γ-carotene. By fusing both proteins with an extra transmembrane domain, the chimeric protein performs two cyclization reactions to produce β-carotene …”

Section: Definition and Classification Of Lycopene β-Cyclasesmentioning

confidence: 99%

Biotechnological Advances in Lycopene β-Cyclases

Zhao

Liu

Mao

2020

J. Agric. Food Chem.

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Lycopene β-cyclase is one of the key enzymes in the biosynthesis of carotenoids, which catalyzes the β-cyclization of both ends of lycopene to produce β-carotene. Lycopene β-cyclases are found in a wide range of sources, mainly plants and microorganisms. Lycopene β-cyclases have been extensively studied for their important catalytic activity, including for use in genetic engineering to modify plants and microorganisms, as a blocking target for lycopene industrial production strains, and for their genetic and physiological effects related to microorganic and plant biological traits. This review of lycopene β-cyclases summarizes the major studies on their basic classification, functional activity, metabolic engineering, and plant science.

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“…These components are isopentenyl pyrophosphate (IPP)-derived compounds, such as polyprenol carrier lipids, menaquinone, isotuberculosinol and carotenoids, and are involved in the transport of saccharides and mycolic acids for the cell wall, electron transport chain, arrest of phagosomal maturation as well as free radical scavenging [30,31,32,33]. A reduction or even lack of these compounds has been reported to lead to defects of the lipoglycan biosynthesis and a reduction of virulence [34,35,36,37]. In mycobacteria, IPP is produced via a different pathway to that found in human cells, which presents a valuable exploitable drug target [38].…”

Section: Metabolite Profiling a “New” Approach For Drug Discoverymentioning

confidence: 99%

Metabolite Profiling: A Tool for the Biochemical Characterisation of Mycobacterium sp.

Drapal

Fraser

2019

Microorganisms

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Over the last decades, the prevalence of drug-resistance in Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, has increased. These findings have rekindled interest in elucidating the unique adaptive molecular and biochemistry physiology of Mycobacterium. The use of metabolite profiling independently or in combination with other levels of “-omic” analyses has proven an effective approach to elucidate key physiological/biochemical mechanisms associated with Mtb throughout infection. The following review discusses the use of metabolite profiling in the study of tuberculosis, future approaches, and the technical and logistical limitations of the methodology.

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Structural and functional analysis of the gene cluster encoding carotenoid biosynthesis inMycobacterium aurumA+

Cited by 47 publications

References 26 publications

Identification of a fourth family of lycopene cyclases in photosynthetic bacteria

Identification of a fourth family of lycopene cyclases in photosynthetic bacteria

Biotechnological Advances in Lycopene β-Cyclases

Metabolite Profiling: A Tool for the Biochemical Characterisation of Mycobacterium sp.

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