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Insulysin

From Wikipedia, the free encyclopedia
Insulysin
Identifiers
EC no.3.4.24.56
CAS no.9013-83-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
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Insulysin (EC3.4.24.56) (Also calledinsulinase,insulin-degrading enzyme,insulin protease,insulin proteinase,insulin-degrading neutral proteinase,insulin-specific protease,insulin-glucagon protease,metalloinsulinase,IDE) is anenzyme.[1][2][3][4][5] This enzymecatalyses the degradationreaction ofinsulin,glucagon and otherpolypeptides.

This cytosolic enzyme is present inmammals and in manyarthropods such as the flyDrosophila melanogaster.

See also

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References

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  1. ^Duckworth WC (August 1988). "Insulin degradation: mechanisms, products, and significance".Endocrine Reviews.9 (3):319–45.doi:10.1210/edrv-9-3-319.PMID 3061785.
  2. ^Affholter JA, Hsieh CL, Francke U, Roth RA (August 1990)."Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes".Molecular Endocrinology.4 (8):1125–35.doi:10.1210/mend-4-8-1125.PMID 2293021.
  3. ^Duckworth WC, Hamel FG, Bennett R, Ryan MP, Roth RA (February 1990). "Human red blood cell insulin-degrading enzyme and rat skeletal muscle insulin protease share antigenic sites and generate identical products from insulin".The Journal of Biological Chemistry.265 (5):2984–7.PMID 1689296.
  4. ^Kuo WL, Gehm BD, Rosner MR (October 1990)."Cloning and expression of the cDNA for a Drosophila insulin-degrading enzyme".Molecular Endocrinology.4 (10):1580–91.doi:10.1210/mend-4-10-1580.PMID 2126597.
  5. ^Ding L, Becker AB, Suzuki A, Roth RA (February 1992). "Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III".The Journal of Biological Chemistry.267 (4):2414–20.PMID 1733942.

http://www.jneurosci.org/content/20/23/8745.full

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