Insulysin
Identifiers
EC no.3.4.24.56
CAS no.9013-83-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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NCBIproteins

Insulysin (EC 3.4.24.56) (Also called insulinase, insulin-degrading enzyme, insulin protease, insulin proteinase, insulin-degrading neutral proteinase, insulin-specific protease, insulin-glucagon protease, metalloinsulinase, IDE) is an enzyme.[1][2][3][4][5] This enzyme catalyses the degradation reaction of insulin, glucagon and other polypeptides.

This cytosolic enzyme is present in mammals and in many arthropods such as the fly Drosophila melanogaster.

See also

References

  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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