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An Enzyme Assay Using pM
Author(s) -
Klein Gérard,
Reymond JeanLouis
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010504)40:9<1771::aid-anie17710>3.0.co;2-m
Subject(s) - chelation , enzyme , metal ions in aqueous solution , chemistry , metal , aminopeptidase , amidase , fluorescence , ligand (biochemistry) , nuclear chemistry , amino acid , biochemistry , inorganic chemistry , organic chemistry , leucine , receptor , physics , quantum mechanics
A high‐throughput fluorescence assay for amidases is demonstrated. It illustrates a new principle in enzyme assays, whereby changes in the pM value during the reaction are recorded (pM=−lg[M], M=free metal ions). An orange fluorescent quinacridone‐based ligand 1 is the pM sensor (shown chelated to a reporter metal ion, M 2+ =Cu 2+ or Ni 2+ ) that is used to monitor the release of metal‐chelating amino acids by the enzymes acylase I and aminopeptidase.