Identification of the Active-site Arginine in Rat Neutral Endopeptidase 24.11 (Enkephalinase) as Arginine 102 and Analysis of a Glutamine 102 Mutant

This publication has 30 references indexed in Scilit:

• Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)
  FEBS Letters, 1988
• Primary structure homologies between two zinc metallopeptidases, the neutral endopeptidase 24.11 ("enkephalinase") and thermolysin, through clustering analysis
  Biochemistry, 1988
• Molecular cloning and amino acid sequence of rat enkephalinase
  Biochemical and Biophysical Research Communications, 1987
• Presence of a histidine at the active site of the neutral endopeptidase — 24.11
  Biochemical and Biophysical Research Communications, 1986
• Nomenclature for enkephalin degrading peptidases
  Life Sciences, 1986
• Pharmacology of enkephalinase inhibitors
  Trends in Pharmacological Sciences, 1985
• Properties of “enkephalinase” from rat kidney: Comparison of dipeptidyl-carboxypeptidase and endopeptidase activities
  Biochemical and Biophysical Research Communications, 1982
• Identification of an arginine important for enzymic activity within the covalent structure of yeast inorganic pyrophosphatase
  Biochemistry, 1980
• Functional residues at the active site of angiotensin converting enzyme
  Biochemical and Biophysical Research Communications, 1978
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976