Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242

This publication has 12 references indexed in Scilit:

• Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue
  Biochemical Journal, 1988
• Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase
  FEBS Letters, 1987
• Amino acid sequence of rat mast cell protease I (chymase)
  Biochemistry, 1987
• Primary structure of the activation segment of procarboxypeptidase a from porcine pancreas
  Biochemical and Biophysical Research Communications, 1986
• Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli
  Biochemical Journal, 1986
• Nucleotide sequence of thehemClocus encoding porpbobilinogen deaminase ofEscherichia coliK12
  Nucleic Acids Research, 1986
• The biosynthesis of porphyrins, chlorophylls, and vitamin B12
  Natural Product Reports, 1985
• Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5′-phosphate. Demonstration of an essential lysine residue
  Biochemical Journal, 1984
• Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides
  Biochemical Journal, 1981
• Biosynthesis of the pigments of life: formation of the macrocycle
  Nature, 1980