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Tsuyoshi Inoue - One of the best experts on this subject based on the ideXlab platform.

  • Structural insight into the stereoselective production of PGF2α by Old Yellow Enzyme from Trypanosoma cruzi
    Journal of Biochemistry, 2011
    Co-Authors: Naoki Okamoto, Keishi Yamaguchi, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Eiichi Mizohata, Tsuyoshi Inoue
    Abstract:

    : Old yellow enzyme (OYE) is an NADPH Oxidoreductase capable of reducing a variety of compounds. It contains flavin mononucleotide (FMN) as a prosthetic group. A ternary complex structure of OYE from Trypanosoma cruzi (TcOYE) with FMN and one of the substrates, p-hydroxybenzaldehyde, shows a striking movement around the active site upon binding of the substrate. From a structural comparison of other OYE complexed with 12-oxophytodienoate, we have constructed a complex structure with another substrate, prostaglandin H(2) (PGH(2)), to provide a proposed stereoselective reaction mechanism for the reduction of PGH(2) to prostaglandin F(2α) by TcOYE.

  • structure of the inhibitor complex of old yellow enzyme from trypanosoma cruzi
    Journal of Synchrotron Radiation, 2011
    Co-Authors: Keishi Yamaguchi, Naoki Okamoto, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase which contains flavin mononucleotide as prosthetic group. The X-ray structures of OYE from Trypanosoma cruzi (TcOYE) which produces prostaglandin (PG) F2α from PGH2 have been determined in the presence or absence of menadione. The binding motif of menadione, known as one of the inhibitors for TcOYE, should accelerate the structure-based development of novel anti-chagasic drugs that inhibit PGF2α production specifically.

  • Preparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruzi.
    Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2007
    Co-Authors: Shigeru Sugiyama, Naoki Okamoto, Keiji Tokuoka, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Yousuke Okano, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase that contains a flavin mononucleotide as a prosthetic group. The OYE from Trypanosoma cruzi, which produces prostaglandin F2α, a potent mediator of various physiological and pathological processes, from prostaglandin H2. The protein was recombinantly expressed and purified from Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 56.3, b = 78.8, c = 78.8 A, β = 93.4° and two molecules per asymmetric unit. The crystals were suitable for X-ray crystallographic studies and diffracted to 1.70 A resolution. A Patterson search method is in progress using the structure of OYE from Pseudomonas putida as a starting model.

  • Preparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruzi.
    Acta crystallographica. Section F Structural biology and crystallization communications, 2007
    Co-Authors: Shigeru Sugiyama, Naoki Okamoto, Keiji Tokuoka, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Yousuke Okano, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase that contains a flavin mononucleotide as a prosthetic group. The OYE from Trypanosoma cruzi, which produces prostaglandin F(2alpha), a potent mediator of various physiological and pathological processes, from prostaglandin H2. The protein was recombinantly expressed and purified from Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 56.3, b = 78.8, c = 78.8 A, beta = 93.4 degrees and two molecules per asymmetric unit. The crystals were suitable for X-ray crystallographic studies and diffracted to 1.70 A resolution. A Patterson search method is in progress using the structure of OYE from Pseudomonas putida as a starting model.

Youichi Niimura - One of the best experts on this subject based on the ideXlab platform.

  • Synechocystis ferredoxin-NADP^+ Oxidoreductase is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin
    BioMetals, 2011
    Co-Authors: Junichi Sato, Kouji Takeda, Rika Nishiyama, Toshihiro Watanabe, Etsuro Yoshimura, Junichi Nakagawa, Shinji Kawasaki, Youichi Niimura
    Abstract:

    We purified free flavin-independent NADPH Oxidoreductase from Synechocystis sp. PCC6803 based on NADPH oxidation activity elicited during reduction of t -butyl hydroperoxide in the presence of Fe(III)-EDTA. The N-terminal sequencing of the purified enzyme revealed it to be ferredoxin-NADP^+ Oxidoreductase (FNR_ S ). The purified enzyme reacted with cytochrome c , ferricyanide and 2,6-dichloroindophenol (DCIP). The substrate specificity of the enzyme was similar to the known FNR. DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide was potently enhanced by the purified enzyme, indicating that Synechocystis FNR_ S may drive the Fenton reaction. The Fenton reaction by Synechocystis FNR_ S in the presence of natural chelate iron compounds tended to be considerably lower than that in the presence of synthetic chelate iron compounds. The Synechocystis FNR_ S is considered to reduce ferric iron to ferrous iron when it evokes the Fenton reaction. Although Synechocystis FNR_ S was able to reduce iron compounds in the absence of free flavin, the ferric reduction by the enzyme was enhanced by the addition of free flavin. The enhancement was detected not only in the presence of natural chelate iron compounds but also synthetic chelate iron compounds.

  • Synechocystis ferredoxin-NADP(+) Oxidoreductase is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin.
    Biometals, 2011
    Co-Authors: Junichi Sato, Kouji Takeda, Rika Nishiyama, Toshihiro Watanabe, Etsuro Yoshimura, Junichi Nakagawa, Shinji Kawasaki, Youichi Niimura
    Abstract:

    We purified free flavin-independent NADPH Oxidoreductase from Synechocystis sp. PCC6803 based on NADPH oxidation activity elicited during reduction of t-butyl hydroperoxide in the presence of Fe(III)-EDTA. The N-terminal sequencing of the purified enzyme revealed it to be ferredoxin-NADP+ Oxidoreductase (FNR S ). The purified enzyme reacted with cytochrome c, ferricyanide and 2,6-dichloroindophenol (DCIP). The substrate specificity of the enzyme was similar to the known FNR. DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide was potently enhanced by the purified enzyme, indicating that Synechocystis FNR S may drive the Fenton reaction. The Fenton reaction by Synechocystis FNR S in the presence of natural chelate iron compounds tended to be considerably lower than that in the presence of synthetic chelate iron compounds. The Synechocystis FNR S is considered to reduce ferric iron to ferrous iron when it evokes the Fenton reaction. Although Synechocystis FNR S was able to reduce iron compounds in the absence of free flavin, the ferric reduction by the enzyme was enhanced by the addition of free flavin. The enhancement was detected not only in the presence of natural chelate iron compounds but also synthetic chelate iron compounds.

Naoki Okamoto - One of the best experts on this subject based on the ideXlab platform.

  • Structural insight into the stereoselective production of PGF2α by Old Yellow Enzyme from Trypanosoma cruzi
    Journal of Biochemistry, 2011
    Co-Authors: Naoki Okamoto, Keishi Yamaguchi, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Eiichi Mizohata, Tsuyoshi Inoue
    Abstract:

    : Old yellow enzyme (OYE) is an NADPH Oxidoreductase capable of reducing a variety of compounds. It contains flavin mononucleotide (FMN) as a prosthetic group. A ternary complex structure of OYE from Trypanosoma cruzi (TcOYE) with FMN and one of the substrates, p-hydroxybenzaldehyde, shows a striking movement around the active site upon binding of the substrate. From a structural comparison of other OYE complexed with 12-oxophytodienoate, we have constructed a complex structure with another substrate, prostaglandin H(2) (PGH(2)), to provide a proposed stereoselective reaction mechanism for the reduction of PGH(2) to prostaglandin F(2α) by TcOYE.

  • structure of the inhibitor complex of old yellow enzyme from trypanosoma cruzi
    Journal of Synchrotron Radiation, 2011
    Co-Authors: Keishi Yamaguchi, Naoki Okamoto, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase which contains flavin mononucleotide as prosthetic group. The X-ray structures of OYE from Trypanosoma cruzi (TcOYE) which produces prostaglandin (PG) F2α from PGH2 have been determined in the presence or absence of menadione. The binding motif of menadione, known as one of the inhibitors for TcOYE, should accelerate the structure-based development of novel anti-chagasic drugs that inhibit PGF2α production specifically.

  • Preparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruzi.
    Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2007
    Co-Authors: Shigeru Sugiyama, Naoki Okamoto, Keiji Tokuoka, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Yousuke Okano, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase that contains a flavin mononucleotide as a prosthetic group. The OYE from Trypanosoma cruzi, which produces prostaglandin F2α, a potent mediator of various physiological and pathological processes, from prostaglandin H2. The protein was recombinantly expressed and purified from Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 56.3, b = 78.8, c = 78.8 A, β = 93.4° and two molecules per asymmetric unit. The crystals were suitable for X-ray crystallographic studies and diffracted to 1.70 A resolution. A Patterson search method is in progress using the structure of OYE from Pseudomonas putida as a starting model.

  • Preparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruzi.
    Acta crystallographica. Section F Structural biology and crystallization communications, 2007
    Co-Authors: Shigeru Sugiyama, Naoki Okamoto, Keiji Tokuoka, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Yousuke Okano, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase that contains a flavin mononucleotide as a prosthetic group. The OYE from Trypanosoma cruzi, which produces prostaglandin F(2alpha), a potent mediator of various physiological and pathological processes, from prostaglandin H2. The protein was recombinantly expressed and purified from Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 56.3, b = 78.8, c = 78.8 A, beta = 93.4 degrees and two molecules per asymmetric unit. The crystals were suitable for X-ray crystallographic studies and diffracted to 1.70 A resolution. A Patterson search method is in progress using the structure of OYE from Pseudomonas putida as a starting model.

Keishi Yamaguchi - One of the best experts on this subject based on the ideXlab platform.

  • Structural insight into the stereoselective production of PGF2α by Old Yellow Enzyme from Trypanosoma cruzi
    Journal of Biochemistry, 2011
    Co-Authors: Naoki Okamoto, Keishi Yamaguchi, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Eiichi Mizohata, Tsuyoshi Inoue
    Abstract:

    : Old yellow enzyme (OYE) is an NADPH Oxidoreductase capable of reducing a variety of compounds. It contains flavin mononucleotide (FMN) as a prosthetic group. A ternary complex structure of OYE from Trypanosoma cruzi (TcOYE) with FMN and one of the substrates, p-hydroxybenzaldehyde, shows a striking movement around the active site upon binding of the substrate. From a structural comparison of other OYE complexed with 12-oxophytodienoate, we have constructed a complex structure with another substrate, prostaglandin H(2) (PGH(2)), to provide a proposed stereoselective reaction mechanism for the reduction of PGH(2) to prostaglandin F(2α) by TcOYE.

  • structure of the inhibitor complex of old yellow enzyme from trypanosoma cruzi
    Journal of Synchrotron Radiation, 2011
    Co-Authors: Keishi Yamaguchi, Naoki Okamoto, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase which contains flavin mononucleotide as prosthetic group. The X-ray structures of OYE from Trypanosoma cruzi (TcOYE) which produces prostaglandin (PG) F2α from PGH2 have been determined in the presence or absence of menadione. The binding motif of menadione, known as one of the inhibitors for TcOYE, should accelerate the structure-based development of novel anti-chagasic drugs that inhibit PGF2α production specifically.

Shigeru Sugiyama - One of the best experts on this subject based on the ideXlab platform.

  • Structural insight into the stereoselective production of PGF2α by Old Yellow Enzyme from Trypanosoma cruzi
    Journal of Biochemistry, 2011
    Co-Authors: Naoki Okamoto, Keishi Yamaguchi, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Eiichi Mizohata, Tsuyoshi Inoue
    Abstract:

    : Old yellow enzyme (OYE) is an NADPH Oxidoreductase capable of reducing a variety of compounds. It contains flavin mononucleotide (FMN) as a prosthetic group. A ternary complex structure of OYE from Trypanosoma cruzi (TcOYE) with FMN and one of the substrates, p-hydroxybenzaldehyde, shows a striking movement around the active site upon binding of the substrate. From a structural comparison of other OYE complexed with 12-oxophytodienoate, we have constructed a complex structure with another substrate, prostaglandin H(2) (PGH(2)), to provide a proposed stereoselective reaction mechanism for the reduction of PGH(2) to prostaglandin F(2α) by TcOYE.

  • structure of the inhibitor complex of old yellow enzyme from trypanosoma cruzi
    Journal of Synchrotron Radiation, 2011
    Co-Authors: Keishi Yamaguchi, Naoki Okamoto, Keiji Tokuoka, Shigeru Sugiyama, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase which contains flavin mononucleotide as prosthetic group. The X-ray structures of OYE from Trypanosoma cruzi (TcOYE) which produces prostaglandin (PG) F2α from PGH2 have been determined in the presence or absence of menadione. The binding motif of menadione, known as one of the inhibitors for TcOYE, should accelerate the structure-based development of novel anti-chagasic drugs that inhibit PGF2α production specifically.

  • Preparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruzi.
    Acta Crystallographica Section F-structural Biology and Crystallization Communications, 2007
    Co-Authors: Shigeru Sugiyama, Naoki Okamoto, Keiji Tokuoka, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Yousuke Okano, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase that contains a flavin mononucleotide as a prosthetic group. The OYE from Trypanosoma cruzi, which produces prostaglandin F2α, a potent mediator of various physiological and pathological processes, from prostaglandin H2. The protein was recombinantly expressed and purified from Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 56.3, b = 78.8, c = 78.8 A, β = 93.4° and two molecules per asymmetric unit. The crystals were suitable for X-ray crystallographic studies and diffracted to 1.70 A resolution. A Patterson search method is in progress using the structure of OYE from Pseudomonas putida as a starting model.

  • Preparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruzi.
    Acta crystallographica. Section F Structural biology and crystallization communications, 2007
    Co-Authors: Shigeru Sugiyama, Naoki Okamoto, Keiji Tokuoka, Nahoko Uchiyama, Hiroyoshi Matsumura, Koji Inaka, Yoshihiro Urade, Yousuke Okano, Tsuyoshi Inoue
    Abstract:

    Old yellow enzyme (OYE) is an NADPH Oxidoreductase that contains a flavin mononucleotide as a prosthetic group. The OYE from Trypanosoma cruzi, which produces prostaglandin F(2alpha), a potent mediator of various physiological and pathological processes, from prostaglandin H2. The protein was recombinantly expressed and purified from Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 56.3, b = 78.8, c = 78.8 A, beta = 93.4 degrees and two molecules per asymmetric unit. The crystals were suitable for X-ray crystallographic studies and diffracted to 1.70 A resolution. A Patterson search method is in progress using the structure of OYE from Pseudomonas putida as a starting model.