Two isozymes of clavaminate synthase central to clavulanic acid formation: cloning and sequencing of both genes from Streptomyces clavuligerus

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This article has been cited by 6 ACS Journal articles (5 most recent appear below).

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  Clavulanic Acid Dehydrogenase:  Structural and Biochemical Analysis of the Final Step in the Biosynthesis of the β-Lactamase Inhibitor Clavulanic Acid^,

  Alasdair K. MacKenzie, Nadia J. Kershaw, Helena Hernandez, Carol V. Robinson, Christopher J. Schofield, and Inger Andersson
  Biochemistry2007 46 (6), 1523-1533

  • Clavulanic Acid Dehydrogenase:  Structural and Biochemical Analysis of the Final Step in the Biosynthesis of the β-Lactamase Inhibitor Clavulanic Acid^,

    Alasdair K. MacKenzie, Nadia J. Kershaw, Helena Hernandez, Carol V. Robinson, Christopher J. Schofield, and Inger Andersson
    Biochemistry2007 46 (6), 1523-1533

    The ultimate step in the biosynthesis of the medicinally important -lactamase inhibitor clavulanic acid is catalyzed by clavulanic acid dehydrogenase (CAD). CAD is responsible for the NAPDH-dependent reduction of the unstable intermediate clavulanate-9-...

    Abstract | Full Text HTML | Hi-Res PDF
• 

  Spectroscopic Studies of Substrate Interactions with Clavaminate Synthase 2, a Multifunctional α-KG-Dependent Non-Heme Iron Enzyme:  Correlation with Mechanisms and Reactivities

  Jing Zhou, Wendy L. Kelly, Brian O. Bachmann, Michele Gunsior, Craig A. Townsend, and Edward I. Solomon
  Journal of the American Chemical Society2001 123 (30), 7388-7398

  • Spectroscopic Studies of Substrate Interactions with Clavaminate Synthase 2, a Multifunctional α-KG-Dependent Non-Heme Iron Enzyme:  Correlation with Mechanisms and Reactivities

    Jing Zhou, Wendy L. Kelly, Brian O. Bachmann, Michele Gunsior, Craig A. Townsend, and Edward I. Solomon
    Journal of the American Chemical Society2001 123 (30), 7388-7398

    Using a single ferrous active site, clavaminate synthase 2 (CS2) activates O2 and catalyzes the hydroxylation of deoxyguanidinoproclavaminic acid (DGPC), the oxidative ring closure of proclavaminic acid (PC), and the desaturation of dihydroclavaminic acid ...

    Abstract | Full Text HTML | Hi-Res PDF
• 

  Three Unusual Reactions Mediate Carbapenem and Carbapenam Biosynthesis

  Rongfeng Li, Anthony Stapon, Joanne T. Blanchfield, and Craig A. Townsend
  Journal of the American Chemical Society2000 122 (38), 9296-9297

  • Three Unusual Reactions Mediate Carbapenem and Carbapenam Biosynthesis

    Rongfeng Li, Anthony Stapon, Joanne T. Blanchfield, and Craig A. Townsend
    Journal of the American Chemical Society2000 122 (38), 9296-9297
    Abstract | Full Text HTML | Hi-Res PDF
• 

  Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes

  Edward I. Solomon, Thomas C. Brunold, Mindy I. Davis, Jyllian N. Kemsley, Sang-Kyu Lee, Nicolai Lehnert, Frank Neese, Andrew J. Skulan, Yi-Shan Yang, and Jing Zhou
  Chemical Reviews2000 100 (1), 235-350

  • Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes

    Edward I. Solomon, Thomas C. Brunold, Mindy I. Davis, Jyllian N. Kemsley, Sang-Kyu Lee, Nicolai Lehnert, Frank Neese, Andrew J. Skulan, Yi-Shan Yang, and Jing Zhou
    Chemical Reviews2000 100 (1), 235-350
    Abstract | Full Text HTML | Hi-Res PDF
• 

  Circular Dichroism and Magnetic Circular Dichroism Spectroscopic Studies of the Non-Heme Ferrous Active Site in Clavaminate Synthase and Its Interaction with α-Ketoglutarate Cosubstrate

  Elizabeth G. Pavel, Jing Zhou, Robert W. Busby, Michele Gunsior, Craig A. Townsend, and Edward I. Solomon
  Journal of the American Chemical Society1998 120 (4), 743-753

  • Circular Dichroism and Magnetic Circular Dichroism Spectroscopic Studies of the Non-Heme Ferrous Active Site in Clavaminate Synthase and Its Interaction with α-Ketoglutarate Cosubstrate

    Elizabeth G. Pavel, Jing Zhou, Robert W. Busby, Michele Gunsior, Craig A. Townsend, and Edward I. Solomon
    Journal of the American Chemical Society1998 120 (4), 743-753

    Clavaminate synthase (CS) is one member of a large class of non-heme iron enzymes that require -ketoglutarate (-KG) as a cosubstrate. While the majority of this class catalyzes the hydroxylation of unactivated CH bonds, CS is unusual in that in ...

    Abstract | Full Text HTML | Hi-Res PDF

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