[51] Nonlysosomal insulin-degrading proteinases in mammalian cells

Kirschner, Richard J.; Goldberg, Alfred L.

doi:10.1016/s0076-6879(81)80053-5

Cited by 12 publications

(3 citation statements)

References 13 publications

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“…Human insulinase is an endopeptidase that acts on insulin, glucagon and other polypeptides up to about Mr 7000 (Kirschner & Goldberg, 1981). Activity is inhibited by EDTA and 1,10phenanthroline (Goldberg et al, 1981;Kayalar & Wong, 1989), indicating that the enzyme is a metalloendopeptidase.…”

Section: Introductionmentioning

confidence: 99%

Homologues of insulinase, a new superfamily of metalloendopeptidases

Rawlings¹,

Barrett²

1991

Biochemical Journal

102

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On the basis of a statistical analysis of an alignment of the amino acid sequences, a new superfamily of metalloendopeptidases is proposed, consisting of human insulinase, Escherichia coli protease III and mitochondrial processing endopeptidases from Saccharomyces and Neurospora. These enzymes do not contain the 'HEXXH' consensus sequence found in all previously recognized zinc metalloendopeptidases.

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Section: Introductionmentioning

confidence: 99%

Homologues of insulinase, a new superfamily of metalloendopeptidases

Rawlings¹,

Barrett²

1991

Biochemical Journal

102

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“…The molecular mass of the IDE is described as being 110 kDa for the monomeric protein (KIRSCHNER andGOLDBERG 1981, SHII et al 1986).…”

Section: Discussionmentioning

confidence: 99%

“…The pure enzyme is a neutral metalloprotease with a molecular mass of 108 kDa (gel filtration, native PAGE) (FRICKE and AURICH 1992), which corresponds well to the results for the protease I11 (CHENG and ZIPSER 1979, DYKSTRA and KUSHNER 1985, FINCH et al 1986). The molecular mass of the IDE is described as being 110 kDa for the monomeric protein (KIRSCHNER andGOLDBERG 1981, SHII et al 1986).…”

Section: Discussionmentioning

confidence: 99%

A periplasmic insulin‐cleaving proteinase (ICP) from Acinetobacter calcoaceticus sharing properties with protease III from Escherichia coli and IDE from eucaryotes

Fricke

Betz

Friebe

1995

J. Basic Microbiol.

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A periplasmic insulin-cleaving proteinase (ICP), purified to its electrophoretic homogeneity in the SDS-PAGE from the Gram-negative bacterium Acinetobacter calcoaceticus, was examined and compared in its properties with the protease III (protease Pi, pitrilysin, EC 3.4.99.44) of Escherichia coli and the insulin-destroying proteinase (IDE, insulinase, EC 3.4.99.45) from eucaryotes. The enzyme was proven to be a metalloprotease like protease III and IDE, as was shown by the inhibitory effects exerted by EDTA and o-phenanthroline. Furthermore, dialysis against EDTA and o-phenanthroline led to a complete loss of activity, which could be restored by addition of Co2+, and, to a lesser extent, but at a lower metal ion concentration by Zn2+. Similar to protease III and IDE, ICP prefers the cleavage of small polypeptides (insulin, insulin B-chain, glucagon) to the cleavage of proteins (casein, human serum albumin, globin) and was inactive against synthetic amino acid derivates (esters, p-nitranilides, and furoylacroleyl substrates) of subtilisin, thermolysin, trypsin, and chymotrypsin. The peptide-bond-specificity of the ICP in the cleavage of the oxidized insulin B-chain was investigated and the results were compared to the specificity of protease III of E. coli, IDE, protease-24,11, and thermolysin. Cleavage sites in the oxidized insulin B-chain generated by ICP are Asn3-Gln4, His10-Leu11, Ala14-Leu15, Leu17-Val18, Gly23-Phe24, Phe24-Phe25, and Phe25-Tyr26. Principally, ICP cleaves between hydrophobic amino acids and amides. The ICP shares one of the only two cleavage sites with the protease III and four sites with the IDE.

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Metalloproteinases

Hofmann¹

1985

Metalloproteins

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[51] Nonlysosomal insulin-degrading proteinases in mammalian cells

Cited by 12 publications

References 13 publications

Homologues of insulinase, a new superfamily of metalloendopeptidases

Homologues of insulinase, a new superfamily of metalloendopeptidases

A periplasmic insulin‐cleaving proteinase (ICP) from Acinetobacter calcoaceticus sharing properties with protease III from Escherichia coli and IDE from eucaryotes

Metalloproteinases

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