Isolation and Characterization of Phytoene Desaturase cDNA Involved in the β-Carotene Biosynthetic Pathway inDunaliella salina

2005 ◽  
Vol 53 (14) ◽  
pp. 5593-5597 ◽  
Author(s):  
Yue-Hui Zhu ◽  
Jian-Guo Jiang ◽  
Yuan Yan ◽  
Xing-Wen Chen
Keyword(s):  
Biosynthetic Pathway ◽  
Phytoene Desaturase ◽  
Isolation And Characterization ◽  
Β Carotene

Isolation and characterization of cDNAs encoding β-carotene hydroxylase in Citrus

Plant Science ◽  
2001 ◽  
Vol 161 (5) ◽  
pp. 1005-1010 ◽  
Author(s):  
In-Jung Kim ◽  
Kyong-Cheol Ko ◽  
Chan-Shick Kim ◽  
Won-Il Chung
Keyword(s):  
Isolation And Characterization ◽  
Β Carotene

scholarly journals Biflavonoids from the Unripe Fruits of Clusia Paralicola and their Antioxidant Activity

2012 ◽  
Vol 7 (12) ◽  
pp. 1934578X1200701 ◽  
Author(s):  
Rafaela Ferreira Oliveira ◽  
Celso Amorim Camara ◽  
Maria de Fátima Agra ◽  
Tania Maria Sarmento Silva
Keyword(s):  
Antioxidant Activity ◽  
Linoleic Acid ◽  
Spectral Data ◽  
2D Nmr ◽  
Cd Spectra ◽  
Total Extract ◽  
Isolation And Characterization ◽  
Β Carotene ◽  
Unripe Fruits

Investigation of the green fruits of Clusia paralicola (Clusiaceae) led to the isolation and characterization of two 3,8″-biflavonoids, 2R, 3S, 2″R, 3″R-GB1-7″- O-β-glucoside (1) and 2R, 3S, 2″R, 3,8″-binaringenin-7″-O-β-glucoside (2), together with four known compounds: β-sitosterol, stigmasterol, β-amyrin, and epicatechin. The structures were established from the IR, LC-ESI-MS and NMR spectral data, including 2D-NMR experiments. The absolute configurations of 1 and 2 were determined by CD spectra. The total extract and the biflavonoids demonstrated significant antioxidant activity in DPPH, ABTS, and β-carotene/linoleic acid tests.

Cloning and characterization of a maize cDNA encoding phytoene desaturase, an enzyme of the carotenoid biosynthetic pathway

1996 ◽  
Vol 30 (2) ◽  
pp. 269-279 ◽  
Author(s):  
Zhou-Hui Li ◽  
Paul D. Matthews ◽  
Benjamin Burr ◽  
Eleanore T. Wurtzel
Keyword(s):  
Biosynthetic Pathway ◽  
Phytoene Desaturase ◽  
Carotenoid Biosynthetic Pathway

scholarly journals The Mycobacterium tuberculosis purine biosynthetic pathway: isolation and characterization of the purC and purL genes

Microbiology ◽  
1996 ◽  
Vol 142 (9) ◽  
pp. 2439-2447 ◽  
Author(s):  
M. Jackson ◽  
F.-X. Berthet ◽  
I. Otal ◽  
J. Rauzier ◽  
C. Martin ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biosynthetic Pathway ◽  
Isolation And Characterization

Characterization of three genes encoding enzymes of the folate biosynthetic pathway in Plasmodium falciparum

Parasitology ◽  
2001 ◽  
Vol 122 (1) ◽  
pp. 1-13 ◽  
Author(s):  
C.-S. LEE ◽  
E. SALCEDO ◽  
Q. WANG ◽  
P. WANG ◽  
P.F.G. SIMS ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Serine Hydroxymethyltransferase ◽  
Gtp Cyclohydrolase I ◽  
Gene Encoding ◽  
New Genes ◽  
Isolation And Characterization ◽  
Genes Encoding ◽  
Antifolate Drugs ◽  
Dihydroneopterin Aldolase

Although the folate metabolic pathway in malaria parasites is a major chemotherapeutic target, resistance to currently available antifolate drugs is an increasing problem. This pathway, however, includes a number of enzymes that, to date, have not been characterized despite their potential for clinical exploitation. As a step towards evaluation of additional targets in this pathway, we report the isolation and characterization of 3 new genes that encode homologues of GTP cyclohydrolase I (GTP-CH), dihydrofolate synthase/folylpolyglutamate synthase (DHFS/FPGS) and serine hydroxymethyltransferase (SHMT). The genes encoding GTP-CH and SHMT are unambiguously assigned to chromosome 12, while that for DHFS/FPGS is tentatively assigned to chromosome 13. All 3 genes are expressed in blood-stage parasites, yielding transcripts of which only ca 60–70% is accounted for by coding sequence. All 3 of the proteins predicted to be encoded by these genes display sequence differences compared to the human host homologues that may be of functional significance. These data bring the complement of cloned genes that encode activities in the pathway to seven, leaving only the gene encoding dihydroneopterin aldolase (DHNA) to be identified in the route from GTP to folate synthesis and folate turnover in the thymidylate cycle.

Isolation and characterization of pigmentation mutants of Micrococcus roseus

1974 ◽  
Vol 20 (7) ◽  
pp. 1007-1013 ◽  
Author(s):  
E. H. Schwartzel ◽  
J. J. Cooney
Keyword(s):  
Carotenoid Pigment ◽  
Pigment Composition ◽  
Wild Type ◽  
Total Carotenoids ◽  
Isolation And Characterization ◽  
Micrococcus Roseus ◽  
Β Carotene

A number of UV-induced pigmentation mutants of Micrococcus roseus were isolated. The carotenoid pigment composition of a yellow mutant and a pink mutant were determined and compared with the composition of the wild type. The yellow mutant appeared to have the ability to insert oxygen functions on only one end of β-carotene. The pink mutant formed less total carotenoids than the wild type; it formed diketo-carotenoids but no dihydroxy compounds. The results are discussed in relation to xanthophyll synthesis in M. roseus.

scholarly journals The Biosynthetic Pathway for Myxol-2′ Fucoside (Myxoxanthophyll) in the Cyanobacterium Synechococcus sp. Strain PCC 7002

2009 ◽  
Vol 191 (10) ◽  
pp. 3292-3300 ◽  
Author(s):  
Joel E. Graham ◽  
Donald A. Bryant
Keyword(s):  
Biosynthetic Pathway ◽  
Chemical Characterization ◽  
Open Reading Frame ◽  
Biotechnological Applications ◽  
Reading Frame ◽  
Genes Encoding ◽  
Synechococcus Sp ◽  
Related Compounds ◽  
Β Carotene

ABSTRACT Synechococcus sp. strain PCC 7002 produces a variety of carotenoids, which comprise predominantly dicylic β-carotene and two dicyclic xanthophylls, zeaxanthin and synechoxanthin. However, this cyanobacterium also produces a monocyclic myxoxanthophyll, which was identified as myxol-2′ fucoside. Compared to the carotenoid glycosides produced by diverse microorganisms, cyanobacterial myxoxanthophyll and closely related compounds are unusual because they are glycosylated on the 2′-OH rather than on the 1′-OH position of the ψ end of the molecule. In this study, the genes encoding two enzymes that modify the ψ end of myxoxanthophyll in Synechococcus sp. strain PCC 7002 were identified. Mutational and biochemical studies showed that open reading frame SynPCC7002_A2032, renamed cruF, encodes a 1′-hydroxylase and that open reading frame SynPCC7002_A2031, renamed cruG, encodes a 2′-O-glycosyltransferase. The enzymatic activity of CruF was verified by chemical characterization of the carotenoid products synthesized when cruF was expressed in a lycopene-producing strain of Escherichia coli. Database searches showed that homologs of cruF and cruG occur in the genomes of all sequenced cyanobacterial strains that are known to produce myxol or the acylic xanthophyll oscillaxanthin. The genomes of many other bacteria that produce hydroxylated carotenoids but do not contain crtC homologs also contain cruF orthologs. Based upon observable intermediates, a complete biosynthetic pathway for myxoxanthophyll is proposed. This study expands the suite of enzymes available for metabolic engineering of carotenoid biosynthetic pathways for biotechnological applications.

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