N-terminal domain of pepsin as a model for retroviral dimeric aspartyl protease.
Autolysis of porcine pepsin at pH 4 affords a derivative possessing intrinsic proteolytic activity. This derivative was isolated by alumina pseudo-affinity chromatography and gel-filtration and was found to result from the tight association of two identical molecules, 135 amino acids long, emerging from the N-terminal domain of pepsin. This finding emphasizes a similarity with the only aspartyl-proteases known to act as dimers, the retroviral proteases.
Bianchi
M
M
INSERM U 58, Montpellier, France.
Boigegrain
R A
RA
Castro
B
B
Coletti-Previero
M A
MA
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002846:Chromatography, Affinity; D010450:Endopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000378:metabolism*; D012190:Retroviridae / Q000201:enzymology*; D013379:Substrate Specificity; D013552:Swine
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A