Sulfurtransferases

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  Subject Areas on Research

  • A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. 
  • Biosynthesis and processing of the molybdenum cofactors. 
  • Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. 
  • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. 
  • Escherichia coli MoeA and MogA. Function in metal incorporation step of molybdenum cofactor biosynthesis. 
  • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. 
  • In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene. 
  • Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis. 
  • Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. 
  • Molybdopterin biosynthesis in man. Properties of the converting factor in liver tissue from a molybdenum cofactor deficient patient. 
  • Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency. 
  • Structural studies of molybdopterin synthase provide insights into its catalytic mechanism. 
  • The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor. 
  • The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. 
  • Thermodynamic analysis of subunit interactions in Escherichia coli molybdopterin synthase.