S'-subsite mapping of endoproteinase Glu/Asp-C from Actinomyces sp.
The S'-subsite specificity of the endoproteinase Glu/Asp-C from Actinomyces sp. was studied by acyl transfer reactions using amino-acid- and peptide-derived nucleophilic amino components. The following results were obtained: 1. The enzyme prefers amino acid amides with hydrophobic side chains in P'i position. In addition, positively charged functions in this position favour S'-P' interactions significantly. 2. Stereospecific binding is a prerequisite for nucleophilic efficiency. 3. Dipeptide amides are more efficient amino components in comparison to free dipeptides whereas oligoglycines show a poor nucleophilic behaviour independent of chain length.
Schuster
M
M
Department of Biochemistry, University of Leipzig, FRG.
Aaviksaar
A
A
Stepanov
V M
VM
Rudenskaya
G N
GN
Jakubke
H D
HD
D000190:Actinomyces / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D010450:Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D010455:Peptides / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D010455:Peptides; D010450:Endopeptidases; C070421:endoproteinase Glu-Asp-C