TY - JOUR
T1 - Proteases
AU - Phillips, Margaret A.
AU - Fletterick, Robert J.
PY - 1992/10
Y1 - 1992/10
N2 - Proteases control many physiological responses, thus the identification and characterization of specific proteases offers the prospect of new medical adbances. Study of the structure-function relationships in protease-catalyzed hydrolysis of the peptide bond has adbanced our understanding of enzyme catalysis and specificity. Three-dimensional structures have been solved for each mechanistic class of protease, and these studies have been extended using site-directed mutagenesis to characterize the amino acid residues required for enzyme function.
AB - Proteases control many physiological responses, thus the identification and characterization of specific proteases offers the prospect of new medical adbances. Study of the structure-function relationships in protease-catalyzed hydrolysis of the peptide bond has adbanced our understanding of enzyme catalysis and specificity. Three-dimensional structures have been solved for each mechanistic class of protease, and these studies have been extended using site-directed mutagenesis to characterize the amino acid residues required for enzyme function.
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U2 - 10.1016/0959-440X(92)90206-M
DO - 10.1016/0959-440X(92)90206-M
M3 - Article
AN - SCOPUS:0001126884
SN - 0959-440X
VL - 2
SP - 713
EP - 720
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 5
ER -