Insulysin

Insulysin
Identifiers
EC number 3.4.24.56
CAS number 9013-83-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Insulysin (EC 3.4.24.56, 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 following chemical reaction

Degradation of insulin, glucagon and other polypeptides. No action on proteins

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

References

  1. Duckworth, W.C. (1988). "Insulin degradation: mechanisms, products, and significance". Endocrine Rev. 9: 319–345. doi:10.1210/edrv-9-3-319. PMID 3061785.
  2. Affholter, J.A.; Hsieh, C.-L.; Francke, U.; Roth, R.A. (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". Mol. Endocrinol. 4: 1125–1135. doi:10.1210/mend-4-8-1125. PMID 2293021.
  3. Duckworth, W.C.; Hamel, F.G.; Bennett, R.; Ryan, M.P.; Roth, R.A. (1990). "Human red blood cell insulin-degrading enzyme and rat skeletal muscle insulin protease share antigenic sites and generate identical products from insulin". J. Biol. Chem. 265: 2984–2987. PMID 1689296.
  4. Kuo, W.-L.; Gehm, B.D.; Rosner, M.R. (1990). "Cloning and expression of the cDNA for a Drosophila insulin-degrading enzyme". Mol. Endocrinol. 4: 1580–1591. doi:10.1210/mend-4-10-1580. PMID 2126597.
  5. Ding, L.; Becker, A.B.; Suzuki, A.; Roth, R.A. (1992). "Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III". J. Biol. Chem. 267: 2414–2420. PMID 1733942.

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

See also

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