Charge polarity reversal inverses the specificity of neutral endopeptidase-24.11.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. Identification of the Active-site Arginine in Rat Neutral Endopeptidase 24.11 (Enkephalinase) as Arginine 102 and Analysis of a Glutamine 102 Mutant
2. N-bromoacetyl-D-leucylglycine. An affinity label for neutral endopeptidase 24.11.
3. Evidence that both arginine 102 and arginine 747 are involved in substrate binding to neutral endopeptidase (EC 3.4.24.11).
4. Primary structure homologies between two zinc metallopeptidases, the neutral endopeptidase 24.11 ("enkephalinase") and thermolysin, through clustering analysis
5. Enzyme-resistant CCK analogs with high affinities for central receptors
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