Pepstatin-insensitive carboxyl proteinases from prokaryotes. Catalytic residues and substrate specificities.
Oda
K
K
Department of Applied Biology, Kyoto Institute of Technology, Japan.
Takahashi
S
S
Ito
M
M
Dunn
B M
BM
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins; D002384:Catalysis; D008969:Molecular Sequence Data; D010436:Pepstatins / Q000494:pharmacology*; D011387:Prokaryotic Cells; D011480:Protease Inhibitors / Q000494:pharmacology*; D011549:Pseudomonas / Q000201:enzymology*; D012697:Serine Endopeptidases; D013379:Substrate Specificity
D001426:Bacterial Proteins; D010436:Pepstatins; D011480:Protease Inhibitors; C014195:Streptomyces pepsin inhibitor; D012697:Serine Endopeptidases; C104058:xanthomonapepsin; D016282:Aspartic Acid Endopeptidases; C031375:pepstatin