The Experts below are selected from a list of 12 Experts worldwide ranked by ideXlab platform

Catherine L Drennan - One of the best experts on this subject based on the ideXlab platform.

  • A B_12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwell-rabb, Aoshu Zhong, Catherine L Drennan
    Abstract:

    Oxetanocin-A (OXT-A) and its oxetane-ring-containing derivatives have been shown to be potent inhibitors of DNA viruses, as well as having antitumour and antibacterial activity. Oxetanes can be prepared synthetically, but how these four-membered, oxygen-containing rings are naturally formed is unknown. This work outlines the biosynthesis of OXT-A, which involves OxsB, a B12-dependent S-adenosylmethionine (SAM) radical enzyme. OxsB catalyses an unusual ring contraction from AMP. The crystal structure of OxsB represents the first of a B12-dependent SAM enzyme, of which there are around 7,000 members, and reveals how it can accommodate the B12 and iron–sulfur cluster at the active site. Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA , oxsB , oxrA and oxrB . Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S -adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2′-Deoxyadenosine Phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2′. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes. The biosynthesis of oxetanocin A involves OxsB, a B_12-dependent S -adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate.

  • a b12 dependent radical sam enzyme involved in oxetanocin a biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwellrabb, Aoshu Zhong, He G Sun, Catherine L Drennan, Hungwen Liu
    Abstract:

    The biosynthesis of oxetanocin A involves OxsB, a B12-dependent S-adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate.

  • a b12 dependent radical sam enzyme involved in oxetanocin a biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwellrabb, Aoshu Zhong, Catherine L Drennan
    Abstract:

    Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S-adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2′-Deoxyadenosine Phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2′. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes. The biosynthesis of oxetanocin A involves OxsB, a B12-dependent S-adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate. Oxetanocin-A (OXT-A) and its oxetane-ring-containing derivatives have been shown to be potent inhibitors of DNA viruses, as well as having antitumour and antibacterial activity. Oxetanes can be prepared synthetically, but how these four-membered, oxygen-containing rings are naturally formed is unknown. This work outlines the biosynthesis of OXT-A, which involves OxsB, a B12-dependent S-adenosylmethionine (SAM) radical enzyme. OxsB catalyses an unusual ring contraction from AMP. The crystal structure of OxsB represents the first of a B12-dependent SAM enzyme, of which there are around 7,000 members, and reveals how it can accommodate the B12 and iron–sulfur cluster at the active site.

Aoshu Zhong - One of the best experts on this subject based on the ideXlab platform.

  • A B_12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwell-rabb, Aoshu Zhong, Catherine L Drennan
    Abstract:

    Oxetanocin-A (OXT-A) and its oxetane-ring-containing derivatives have been shown to be potent inhibitors of DNA viruses, as well as having antitumour and antibacterial activity. Oxetanes can be prepared synthetically, but how these four-membered, oxygen-containing rings are naturally formed is unknown. This work outlines the biosynthesis of OXT-A, which involves OxsB, a B12-dependent S-adenosylmethionine (SAM) radical enzyme. OxsB catalyses an unusual ring contraction from AMP. The crystal structure of OxsB represents the first of a B12-dependent SAM enzyme, of which there are around 7,000 members, and reveals how it can accommodate the B12 and iron–sulfur cluster at the active site. Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA , oxsB , oxrA and oxrB . Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S -adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2′-Deoxyadenosine Phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2′. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes. The biosynthesis of oxetanocin A involves OxsB, a B_12-dependent S -adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate.

  • a b12 dependent radical sam enzyme involved in oxetanocin a biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwellrabb, Aoshu Zhong, He G Sun, Catherine L Drennan, Hungwen Liu
    Abstract:

    The biosynthesis of oxetanocin A involves OxsB, a B12-dependent S-adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate.

  • a b12 dependent radical sam enzyme involved in oxetanocin a biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwellrabb, Aoshu Zhong, Catherine L Drennan
    Abstract:

    Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S-adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2′-Deoxyadenosine Phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2′. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes. The biosynthesis of oxetanocin A involves OxsB, a B12-dependent S-adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate. Oxetanocin-A (OXT-A) and its oxetane-ring-containing derivatives have been shown to be potent inhibitors of DNA viruses, as well as having antitumour and antibacterial activity. Oxetanes can be prepared synthetically, but how these four-membered, oxygen-containing rings are naturally formed is unknown. This work outlines the biosynthesis of OXT-A, which involves OxsB, a B12-dependent S-adenosylmethionine (SAM) radical enzyme. OxsB catalyses an unusual ring contraction from AMP. The crystal structure of OxsB represents the first of a B12-dependent SAM enzyme, of which there are around 7,000 members, and reveals how it can accommodate the B12 and iron–sulfur cluster at the active site.

Jennifer Bridwellrabb - One of the best experts on this subject based on the ideXlab platform.

  • a b12 dependent radical sam enzyme involved in oxetanocin a biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwellrabb, Aoshu Zhong, He G Sun, Catherine L Drennan, Hungwen Liu
    Abstract:

    The biosynthesis of oxetanocin A involves OxsB, a B12-dependent S-adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate.

  • a b12 dependent radical sam enzyme involved in oxetanocin a biosynthesis
    Nature, 2017
    Co-Authors: Jennifer Bridwellrabb, Aoshu Zhong, Catherine L Drennan
    Abstract:

    Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S-adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2′-Deoxyadenosine Phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2′. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes. The biosynthesis of oxetanocin A involves OxsB, a B12-dependent S-adenosylmethionine radical enzyme, which catalyses an unusual ring contraction of a 2′-Deoxyadenosine Phosphate. Oxetanocin-A (OXT-A) and its oxetane-ring-containing derivatives have been shown to be potent inhibitors of DNA viruses, as well as having antitumour and antibacterial activity. Oxetanes can be prepared synthetically, but how these four-membered, oxygen-containing rings are naturally formed is unknown. This work outlines the biosynthesis of OXT-A, which involves OxsB, a B12-dependent S-adenosylmethionine (SAM) radical enzyme. OxsB catalyses an unusual ring contraction from AMP. The crystal structure of OxsB represents the first of a B12-dependent SAM enzyme, of which there are around 7,000 members, and reveals how it can accommodate the B12 and iron–sulfur cluster at the active site.

Hungwen Liu - One of the best experts on this subject based on the ideXlab platform.

He G Sun - One of the best experts on this subject based on the ideXlab platform.