Catalyses the two-electron reduction of biliverdin IXalpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phytochromobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of 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
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
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
one of the six Arabidopsis ferredoxins, AtFd2, is the preferred electron donor for HY2. Activity with ferredoxin AtFd2 mutants D78N, E81Q, E82Q, Y89F, R92Q, and D112N, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Evaluation of antibacterial properties of Matricaria aurea on clinical isolates of periodontitis patients with special reference to red complex bacteria.
Evaluation of hypoglycemic, antihyperglycemic and antihyperlipidemic activities of 80% methanolic seed extract of Calpurnia aurea (Ait.) Benth. (Fabaceae) in mice.
Disseminated neoplasia in clams Venerupis aurea from Galicia (NW Spain): histopathology, ultrastructure and ploidy of the neoplastic cells, and comparison of diagnostic procedures.
Evaluation of antibacterial properties of Matricaria aurea on clinical isolates of periodontitis patients with special reference to red complex bacteria.
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
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
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
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
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
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
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
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
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
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and selenomethionine-labeled phytochromobilin synthase in complex with substrate biliverdin IXalpha, sitting drop vapor diffusion method, mixing of protein in 150 mM KCl, and 20 mM Tris-HCl, pH 7.4, with reservoir solution, at 4°C. Tiny needle-shaped crystals of the BV-PPhiB synthase complex are obtained with a reservoir solution containing 20% w/v PEG 8000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M MgCl2. Isomorphous crystals are also obtained with a reservoir solution containing 30% w/v PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M MgCl2, X-ray diffraction structure determination and analysis at 1.95-2.2 A resolution
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
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
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
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
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
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration. The PPhiB synthase monomer is contained in the major peak of anion-exchange chromatography, and the PPhiB synthase homodimer in the minor peak, for purification, the monomeric major peak fraction is used
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