The Enzyme Database

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EC 3.4.24.56     
Accepted name: insulysin
Reaction: Degradation of insulin, glucagon and other polypeptides. No action on proteins
Other name(s): 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).
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9013-83-6
References:
1.  Duckworth, W.C. Insulin degradation: mechanisms, products, and significance. Endocrine Rev. 9 (1988) 319–345. [DOI] [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. [DOI] [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. [DOI] [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 3.4.24.56 created 1972 as EC 3.4.99.10, transferred 1976 EC 3.4.22.11, transferred 1978 to EC 3.4.99.45, transferred 1993 to to EC 3.4.24.56 (EC 3.4.99.46 created 1992, incorporated 2000)]
 
 


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