Investigation of putative active-site lysine residues in hydroxymethylbilane synthase. Preparation and characterization of mutants in which (a) Lys-55, (b) Lys-59 and (c) both Lys-55 and Lys-59 have been replaced by glutamine.

Podobne knjige/članki

• Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase).
  od: Miller, A D, et al.
  Izdano: (1989)
• Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.
  od: Hart, G J, et al.
  Izdano: (1984)
• Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding.
  od: Lander, M, et al.
  Izdano: (1991)
• Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.
  od: Hart, G J, et al.
  Izdano: (1986)
• Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.
  od: Hart, G J, et al.
  Izdano: (1988)