Peroxidase and Phosphatase Activity of Active-site Mutants of Vanadium Chloroperoxidase from the Fungus Curvularia inaequalis

This publication has 26 references indexed in Scilit:

• X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 Å resolution 1 1Edited by R. Huber
  Journal of Molecular Biology, 1999
• Vanadate-Containing Haloperoxidases and Acid Phosphatases: The Conserved Active Site
  Published by American Chemical Society (ACS) ,1998
• An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
  Protein Science, 1997
• Identification of a novel phosphatase sequence motif
  Protein Science, 1997
• Implications for the Catalytic Mechanism of the Vanadium-Containing Enzyme Chloroperoxidase from the Fungus Curvularia inaequalis by X-Ray Structures of the Native and Peroxide Form
  Biological Chemistry, 1997
• Inactivation of Vanadium Bromoperoxidase: Formation of 2-Oxohistidine
  Biochemistry, 1996
• Aqueous Chemistry of Labile Oxovanadates: Relevance to Biological Studies
  Comments on Inorganic Chemistry, 1994
• The vanadium chloroperoxidase from the fungus, Curvularia inaequalis
  FEBS Letters, 1993
• Vanadate: A potent inhibitor of multifunctional glucose-6-phosphatase
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1981
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976