IUBMB Enzyme Nomenclature


Accepted name: insulysin

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

Other names: insulinase; insulin-degrading enzyme; insulin protease; insulin proteinase; insulin-degrading neutral proteinase; insulin-specific protease; insulin-glucagon protease; metalloinsulinase; IDE

Comments: A 110 kDa cytosolic enzyme, known from mammals and the fruit fly, Drosophila melanogaster. Inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon. In peptidase family M16 (pitrilysin family). Formerly EC, EC and EC

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 9013-83-6


1. Duckworth, W.C. Insulin degradation: mechanisms, products, and significance. Endocrine Rev. 9 (1988) 319-345. [PMID: 3061785]

2. Affholter, J.A., Hsieh, C.-L., Francke, U. and Roth, R.A. 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 (1990) 1125-1135. [PMID: 2293021]

3. Duckworth, W.C., Hamel, F.G., Bennett, R., Ryan, M.P. and Roth, R.A. 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 (1990) 2984-2987. [PMID: 1689296]

4. Kuo, W.-L., Gehm, B.D. and Rosner, M.R. Cloning and expression of the cDNA for a Drosophila insulin-degrading enzyme. Mol.Endocrinol. 4 (1990) 1580-1591. [PMID: 2126597]

5. Ding, L., Becker, A.B., Suzuki, A. and Roth, R.A. Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III. J. Biol. Chem. 267 (1992) 2414-2420. [PMID: 1733942]

[EC created 1972 as EC, transferred 1976 EC, transferred 1978 to EC, transferred 1993 to to EC (EC created 1992, incorporated 2000)]

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