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Science 9 December 1988:
Vol. 242. no. 4884, pp. 1415 - 1418
DOI: 10.1126/science.3059494
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Articles
Science, Vol 242, Issue 4884, 1415-1418
Copyright © 1988 by American Association for the Advancement of Science
Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III
JA Affholter,
VA Fried,
and
RA Roth
Department of Pharmacology, Stanford University School of Medicine, CA 94305.
A proteinase with high affinity for insulin has been proposed to play a role in the cellular processing of this hormone. A complementary DNA (cDNA) coding for this enzyme has been isolated and sequenced. The deduced amino acid sequence of the enzyme contained the sequences of 13 peptides derived from the isolated protein. The cDNA could be transcribed in vitro to yield a synthetic RNA that in cell-free translations produced a protein that coelectrophoresed with the native proteinase and could be immunoprecipitated with monoclonal antibodies to this enzyme. The deduced sequence of this proteinase did not contain the consensus sequences for any of the known classes of proteinases (that is, metallo, cysteine, aspartic, or serine), but it did show homology to an Escherichia coli proteinase (called protease III), which also cleaves insulin and is present in the periplasmic space. Thus, these two proteins may be members of a family of proteases that are involved in intercellular peptide signaling.
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