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(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
additional information
?
-
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biosynthesis of bilin pigments
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
substrate binding structure analysis, overview
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
conserved surface-charged residues on HY2 and Arabidopsis ferredoxin AtFd2 are important in the protein-protein interaction as well as biliverdin reduction activity of HY2, mutational analysis, overview. The C12 propionate group of biliverdin is important for HY2-catalyzed biliverdin reduction
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
r
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
?
additional information
?
-
two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. PPhiB synthase catalyzes the reduction of BV to produce 2(R), 3Z/E-PPhiB using reducing equivalents from ferredoxin. The 2,3,31,32-diene system of the A-ring is site-specifically reduced. The ZZZssa configurations of BV and PPhiB are displayed as observed in the present crystal structure
-
-
-
additional information
?
-
-
two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. PPhiB synthase catalyzes the reduction of BV to produce 2(R), 3Z/E-PPhiB using reducing equivalents from ferredoxin. The 2,3,31,32-diene system of the A-ring is site-specifically reduced. The ZZZssa configurations of BV and PPhiB are displayed as observed in the present crystal structure
-
-
-
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(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biosynthesis of bilin pigments
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phytochromobilin + 2 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
-
?
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Adenocarcinoma of Lung
Molecular mechanisms of Lycoris aurea agglutinin-induced apoptosis and G2 /M cell cycle arrest in human lung adenocarcinoma A549 cells, both in vitro and in vivo.
Anthrax
Antioxidant and Antimicrobial Activity of Solvent Fractions of Calpurnia aurea (Ait.) Benth. (Fabaceae).
Bacterial Infections
Antibacterial Activities of Calpurnia aurea against Selected Animal Pathogenic Bacterial Strains.
Candidiasis, Oral
The complete mitogenome of scaly thrush Zoothera aurea (Passeriformes, Turdidae).
Candidiasis, Oral
Urogonimus turdi (Digenea: Leucochloridiidae) from the White's Thrush, Zoothera aurea, in the Republic of Korea.
Carcinoma
Alkaloids from Lycoris aurea and their cytotoxicities against the head and neck squamous cell carcinoma.
Carcinoma, Squamous Cell
Alkaloids from Lycoris aurea and their cytotoxicities against the head and neck squamous cell carcinoma.
Chronic Periodontitis
Evaluation of antibacterial properties of Matricaria aurea on clinical isolates of periodontitis patients with special reference to red complex bacteria.
Dyslipidemias
Evaluation of hypoglycemic, antihyperglycemic and antihyperlipidemic activities of 80% methanolic seed extract of Calpurnia aurea (Ait.) Benth. (Fabaceae) in mice.
Elephantiasis
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Endometrial Neoplasms
Effects of Induced Exosomes from Endometrial Cancer Cells on Tumor Activity in the Presence of Aurea helianthus Extract.
Fibrosarcoma
A Comparative Study upon the Therapeutic Indices of Some Natural and Synthetic Anti-inflammatory Agents.
Hyperalgesia
Tabebuia aurea decreases hyperalgesia and neuronal injury induced by snake venom.
Hypertension
Analyzing factors that influence the folk use and phytonomy of 18 medicinal plants in Navarra.
Hypertension
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Hypertension
Antihypertensive activity of 80% methanol seed extract of Calpurnia aurea (Ait.) Benth. subsp. aurea (Fabaceae) is mediated through calcium antagonism induced vasodilation.
Infections
Antimicrobial activities of some selected traditional Ethiopian medicinal plants used in the treatment of skin disorders.
Infections
Hairy roots of Datura candida×D. aurea: effect of culture medium composition on growth and alkaloid biosynthesis.
Infections
Interaction between temperature and sublethal infection with the amphibian chytrid fungus impacts a susceptible frog species.
Infections
Low disease-causing threshold in a frog species susceptible to chytridiomycosis.
Infections
Severe sparganosis in Australian tree frogs.
Influenza, Human
Antiviral activity of Basidiomycete mycelia against influenza type A (serotype H1N1) and herpes simplex virus type 2 in cell culture.
Leishmaniasis
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Malaria
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Mycoses
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Neoplasms
Chemical profiling, antiviral and antiproliferative activities of the essential oil of Phlomis aurea Decne grown in Egypt.
Neoplasms
Disseminated neoplasia in clams Venerupis aurea from Galicia (NW Spain): histopathology, ultrastructure and ploidy of the neoplastic cells, and comparison of diagnostic procedures.
Neoplasms
Effects of Induced Exosomes from Endometrial Cancer Cells on Tumor Activity in the Presence of Aurea helianthus Extract.
Neoplasms
Methanolic Extract Isolated from Root of Lycoris aurea Inhibits Cancer Cell Growth and Endothelial Cell Tube Formation In Vitro.
Neoplasms
Phytochemical Screening and In-Vitro Antibacterial and Anticancer Activity of Crude Extract of Matricaria aurea.
Paronychia
Ethnobotanical survey in the Palestinian area: a classification of the healing potential of medicinal plants.
Paronychia
Plants used for the treatment of diabetes in Israel.
Periodontitis
Evaluation of antibacterial properties of Matricaria aurea on clinical isolates of periodontitis patients with special reference to red complex bacteria.
Rabies
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Sarcoma
Extracts of Lycoris aurea induce apoptosis in murine sarcoma S180 cells.
Sarcoma 180
Extracts of Lycoris aurea induce apoptosis in murine sarcoma S180 cells.
Skin Diseases
Analyzing factors that influence the folk use and phytonomy of 18 medicinal plants in Navarra.
Squamous Cell Carcinoma of Head and Neck
Alkaloids from Lycoris aurea and their cytotoxicities against the head and neck squamous cell carcinoma.
Syphilis
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Trachoma
Antidiarrhoeal and antimicrobial activity of Calpurnia aurea leaf extract.
Tuberculosis
In vitro anti-mycobacterial activity of selected medicinal plants against Mycobacterium tuberculosis and Mycobacterium bovis strains.
Virus Diseases
Incidence and pathology of common viruses of nerine in Tasmania.
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metabolism
enzyme phytochromobilin synthase function in the heme pathway in tetrapyrrole metabolism, overview
evolution
-
synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, overview
evolution
enzyme structure analysis and comparison, overview. PPhiB synthase is a member of the ferredoxin-dependent bilin reductase (FDBR) family. The FDBR family comprises several different but closely related proteins including phycocyanobilin: ferredoxin oxidoreductase (PcyA, EC 1.3.7.5), 15,16-dihydrobiliverdin:ferredoxin oxidoreductase (PebA, EC 1.3.7.2), phycoerythrobilin:ferredoxin oxidoreductase (PebB, EC 1.3.7.3), phycoerythrobilin synthase (PebS, EC 1.3.7.6), and PPhiB synthase (EC 1.3.7.4). These enzymes are widely distributed in oxygenic phototrophs
evolution
phylogenetic analysis of CsHY2 homologues from different plants
malfunction
a recessive mutant, exhibiting highly enhanced submergence resistance, is identified. Phenotypical analyses show that this resistant to flooding (rf) mutant displays slightly chlorotic leaves and spontaneous initiation of adventitious roots (ARs) on stems. The mutation is mapped to the phytochromobilin synthase gene AUREA (AU), in which a single amino acid substitution from asparagine to tyrosine is found. Temporal coincidence of the two phenotypes is evidenced in the rf mutant: chlorosis and spontaneous AR formation, revealing that AU functions by maintaining heme homeostasis. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The rf mutant is highly resistant to waterlogging in contrast to the wild-type, phenotypes, overview. Active HO-1 is necessary for the scion of rf to stimulate ARs in the stock of wild-type, but there is insufficient HO-1 in the wild-type hypocotyls to initiate AR primordium
malfunction
the long hypocotyl mutant C1238 is identified from an EMS-induced mutagenesis population of the cucumber inbred line CCMC with normal hypocotyl and green leaves. The mutant C1238 exhibits apparently elongated hypocotyl and yellow-green leaves at the seedling stage
physiological function
HY2 synthesizes the open chain tetrapyrrole chromophore for light-sensing phytochromes. It catalyzes the double bond reduction of a heme-derived tetrapyrrole intermediate biliverdin IXalpha at the A-ring diene system
physiological function
-
plants utilize 3Z-phytochromobilin:ferredoxin oxidoreductase to reduce the diene system of the A ring of biliverdin IXalpha to form PthetaB
physiological function
-
Hy2 mutants display a long hypocotyl in white light. Mutant seedlings grown under continuous far-red light display a typical blind phenotype showing very long hypocotyls and closed cotyledons. When grown in short-day regime, wild-type bolts after having produced about 44 leaves whereas the null mutants flower after 18 to 20 leaves
physiological function
in addition to the classic function of the enzyme phytochromobilin synthase (gene AUREA, AU), in phytochrome and chlorophyll biogenesis in leaves, a role in mediating adventitious roots (AR) formation on stems is uncovered. Genetic evidence for the involvement of the AU-heme oxygenase-1-heme pathway in AR initiation is found in tomato. Dual roles of phytochromobilin synthase in chlorophyll synthesis and AR primordia initiation, overview. Communication between leaves and hypocotyls is responsible for AR initiation
physiological function
PPhiB synthase is a ferredoxin-dependent bilin reductase (FDBR) that catalyzes the site-specific reduction of bilins, which are sensory and photosynthesis pigments, and produces phytochromobilin (PPhiB) from biliverdin, a heme-derived linear tetrapyrrole pigment. Phytochromobilin is a red/far-red light sensory pigment in plant phytochrome
physiological function
the CsHY2 protein plays a role in the chloroplast, which is consistent with the plastid localization of PPhiB synthesis and the RNA-seq data, suggesting that tetrapyrrole chromophore biosynthesis and chlorophyll metabolism are mainly in the chloroplast in Cucumis sativus
additional information
the overall structure of tomato PPhiB synthase is similar to those of other ferredoxin-dependent bilin reductases (FDBRs), except for the addition of a long C-terminal loop and short helices. The C-terminal loop is part of the biliverdin-binding pocket and that two basic residues in the C-terminal loop form salt bridges with the propionate groups of biliverdin. The C-terminal loop is involved in the interaction with ferredoxin and biliverdin. The configuration of biliverdin bound to tomato PPhiB synthase differed from that of biliverdin ound to other FDBRs, and its orientation in PPhiB synthase is inverted relative to its orientation in the other FDBRs. Enzyme structure analysis and comparison, overview. Two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. Product release mechanism: PPhiB synthase-catalyzed stereospecific reduction produces 2(R)-PPhiB, which when bound to PPhiB synthase collides with the side chain of Val-121, releasing 2(R)-PPhiB from the synthase
additional information
-
the overall structure of tomato PPhiB synthase is similar to those of other ferredoxin-dependent bilin reductases (FDBRs), except for the addition of a long C-terminal loop and short helices. The C-terminal loop is part of the biliverdin-binding pocket and that two basic residues in the C-terminal loop form salt bridges with the propionate groups of biliverdin. The C-terminal loop is involved in the interaction with ferredoxin and biliverdin. The configuration of biliverdin bound to tomato PPhiB synthase differed from that of biliverdin ound to other FDBRs, and its orientation in PPhiB synthase is inverted relative to its orientation in the other FDBRs. Enzyme structure analysis and comparison, overview. Two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. Product release mechanism: PPhiB synthase-catalyzed stereospecific reduction produces 2(R)-PPhiB, which when bound to PPhiB synthase collides with the side chain of Val-121, releasing 2(R)-PPhiB from the synthase
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D116N
-
mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein
D146N
-
mutant completely loses catalytic activity and also the ability of biliverdin binding
D256E
-
mutant retains only partial activity
E110Q
site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
E187Q
site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
H259Q
site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
K183Q
site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
K255Q
site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
K263Q
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
N133
-
mutant produces only partial activity
R200Q
site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
R200Q/R264Q
site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
R252Q
-
mutant loses catalytic activity and the ability of substrate binding
R264Q
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity
D123N
site-directed mutagenesis, the mutated enzyme retains biliverdin IXalpha binding activity and radical formation activity, whereas the PPhiB formation activity is negligible
D263N
site-directed mutagenesis, the mutated enzyme retains biliverdin IXalpha binding activity and radical formation activity, whereas the PPhiB formation activity is negligible
V121A
site-directed mutagenesis, single-turnover analysis demonstrates that the V121A mutated protein is slightly slower, although it produces 3Z/E-PPhiB on wild-type level, whereas no activity is detected in the V121A mutated protein in the steady-state analysis
additional information
identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1
additional information
-
identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1
additional information
the flooding (rf) mutation is analysed in the tomato gene AUREA (AU), it not only led to leaf chlorosis but also causes the spontaneous formation of adventitious roots (ARs) on stems. Under flooding stress, au mutants extensively form ARs along the stem, while wild-type plants produce ARs only at the root-shoot junction. After submergence for 7 days, the resistant to flooding (rf) mutants show higher sensitivity to flooding regarding AR initiation compared to wild-type. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The flooding resistance of rf mutants mainly results from the accumulation of heme and enhanced HO-1 activity, both of which function in the phytochrome synthesis pathway. In addition, the exchange of substances, including heme, between leaves and stems accounts for AR formation on stems
additional information
-
the flooding (rf) mutation is analysed in the tomato gene AUREA (AU), it not only led to leaf chlorosis but also causes the spontaneous formation of adventitious roots (ARs) on stems. Under flooding stress, au mutants extensively form ARs along the stem, while wild-type plants produce ARs only at the root-shoot junction. After submergence for 7 days, the resistant to flooding (rf) mutants show higher sensitivity to flooding regarding AR initiation compared to wild-type. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The flooding resistance of rf mutants mainly results from the accumulation of heme and enhanced HO-1 activity, both of which function in the phytochrome synthesis pathway. In addition, the exchange of substances, including heme, between leaves and stems accounts for AR formation on stems
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development of a system to produce phytochromobilin in Escherichia coli by coexpression of heme oxygenase and phytochromobilin:ferredoxin oxidoreductase in a single operon in conjunction with apophytochrome using two compatible plasmids
-
expressed in Escherichia coli strain BL21
-
expression in Nicotiana plumbaginifolia and Escherichia coli
-
expression in Pichia pastoris
gene AUREA (AU), quantitative real-time RT-PCR enzyme expression analysis in wild-type and mutant seedlings
gene CsHY2, genotyping, several segregating populations qre employed by crossing C1238 with the original parental line CCMC, the American pickling cucumber line Gy14 and the North China fresh marker type cucumber line 9930, respectively. For linkage mapping and cloning of the elh1 gene, F2 populations are derived from the C1238×9930 F1 and C1238×Gy14 F1 plants, respectively. Quantitative real-time PCR enzyme expression analysis. Phylogenetic analysis of CsHY2 homologues from different plants. Linkage mapping of the elh1 locus
overexpression in Synechococcus sp. strain PCC 7002, from endogenous plasmid pAQ1 under the control of the Synechocystis sp. strain PCC 6803 cpcBA promoter, leads to overproduction of phytochromobilin, the cells show a phenotype only slightly less pigmented and blue-green than the wild-type, the strain producing phycobiliproteins carrying phytochromobilin grow much more slowly at low light intensity. Transformant colonies in which pcyA is inactivated in the HY2 overexpression background does not develop a chlorotic appearance, and segregation of the mutant and wild-type alleles is rapidly achieved
-
recombinant functional expression of HT-HY2 in Escherichia coli with production of phytochromobilin, functional co-expression with cyanobacterial heme oxygenase, and the phycocyanin alpha-subunit, CpcA, from Synechocystis sp. PCC 6803 or Synechococcus sp. PCC 7002, and with the phycocyanin alpha-subunit phycocyanobilin lyase, CpcE/CpcF, or the phycoerythrocyanin alpha-subunit phycocyanobilin isomerizing lyase, PecE/PecF, from Noctoc sp. PCC 7120. Production levels of fluorescent pigments and chromophore analysis, overview
-
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
wild type and mutant allels
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Frankenberg, N.; Mukougawa, K.; Kohchi, T.; Lagarias, J.C.
Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
Plant Cell
13
965-978
2001
Arabidopsis thaliana (Q9SR43)
brenda
Kohchi, T.; Mukougawa, K.; Frankenberg, N.; Masuda, M.; Yokota, A.; Lagarias, J.C.
The Arabidopsis hy2 gene encodes phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase
Plant Cell
13
425-436
2001
Arabidopsis thaliana (Q9SR43)
brenda
McDowell, M.T.; Lagarias, J.C.
Purification and biochemical properties of phytochromobilin synthase from etiolated oat seedlings
Plant Physiol.
126
1546-1554
2001
Avena sativa
brenda
Terry, M.J.; Lagarias, J.C.
Holophytochrome assembly. Coupled assay for phytochromobilin synthase in organello
J. Biol. Chem.
266
22215-22221
1991
Cucumis sativus
brenda
Sawers, R.J.; Linley, P.J.; Gutierrez-Marcos, J.F.; Delli-Bovi, T.; Farmer, P.R.; Kohchi, T.; Terry, M.J.; Brutnell, T.P.
The Elm1 (ZmHy2) gene of maize encodes a phytochromobilin synthase
Plant Physiol.
136
2771-2781
2004
Zea mays
brenda
Mukougawa, K.; Kanamoto, H.; Kobayashi, T.; Yokota, A.; Kohchi, T.
Metabolic engineering to produce phytochromes with phytochromobilin, phycocyanobilin, or phycoerythrobilin chromophore in Escherichia coli
FEBS Lett.
580
1333-1338
2006
Escherichia coli
brenda
Muramoto, T.; Kami, C.; Kataoka, H.; Iwata, N.; Linley, P.J.; Mukougawa, K.; Yokota, A.; Kohchi, T.
The tomato photomorphogenetic mutant, aurea, is deficient in phytochromobilin synthase for phytochrome chromophore biosynthesis
Plant Cell Physiol.
46
661-665
2005
Solanum lycopersicum (Q588D6), Solanum lycopersicum
brenda
Tu, S.L.; Rockwell, N.C.; Lagarias, J.C.; Fisher, A.J.
Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements
Biochemistry
46
1484-1494
2007
Arabidopsis thaliana
brenda
Tu, S.L.; Chen, H.C.; Ku, L.W.
Mechanistic studies of the phytochromobilin synthase HY2 from Arabidopsis
J. Biol. Chem.
283
27555-27564
2008
Arabidopsis thaliana
brenda
Chiu, F.Y.; Chen, Y.R.; Tu, S.L.
Electrostatic interaction of phytochromobilin synthase and ferredoxin for biosynthesis of phytochrome chromophore
J. Biol. Chem.
285
5056-5065
2010
Arabidopsis thaliana (Q9SR43), Arabidopsis thaliana
brenda
Alvey, R.M.; Biswas, A.; Schluchter, W.M.; Bryant, D.A.
Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli
Biochemistry
50
4890-4902
2011
Arabidopsis thaliana
brenda
Alvey, R.M.; Biswas, A.; Schluchter, W.M.; Bryant, D.A.
Effects of modified phycobilin biosynthesis in the cyanobacterium Synechococcus sp. strain PCC 7002
J. Bacteriol.
193
1663-1671
2011
Arabidopsis thaliana
brenda
Shin, A.Y.; Han, Y.J.; Song, P.S.; Kim, J.I.
Expression of recombinant full-length plant phytochromes assembled with phytochromobilin in Pichia pastoris
FEBS Lett.
588
2964-2970
2014
Arabidopsis thaliana (Q9SR43)
brenda
Creff, A.; Lonard, B.; Desnos, T.
Targeted Ds-tagging strategy generates high allelic diversity at the Arabidopsis HY2 locus
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