PMID: 6170356Jun 1, 1981Paper

Intramolecular general acid catalysis in the binding reactions of alpha 2-macroglobulin and complement components C3 and C4

Bioscience Reports
S G Davies, Robert B Sim

Abstract

The complement system proteins C3 and C4 and the plasma protease inhibitor alpha 2-macroglobulin, when activated by limited proteolysis, can bind covalently to other macromolecules. The three proteins also exhibit an unusual internal peptide-bond cleavage reaction when denatured. The covalent binding reaction is likely to occur by a transacylation mechanism involving an internal thiolester in the three proteins. However, the activated species of these proteins are much more reactive than simple thiolesters. Studies of molecular models of the thiolester region in C3 show that an intramolecular acid catalysis mechanism can both account for the exceptional reactivity of the activated form of these proteins and provide an explanation for the denaturation-induced peptide bond cleavage.

References

Aug 1, 1979·The Biochemical Journal·A J BarrettC A Sayers
Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·R P Swenson, J B Howard
Jul 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·S K Law, R P Levine
May 1, 1981·The Biochemical Journal·G S SalvesenA J Barrett
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Jan 1, 1981·The Biochemical Journal·R B SimE Sim

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Citations

Jan 1, 1983·Springer Seminars in Immunopathology·B F Tack
Feb 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·M L ThomasB F Tack
Jan 1, 1983·Annals of the New York Academy of Sciences·B W Erickson, S A Khan
Jan 16, 2020·Biology·Richard A PhillipsSigrun Lange
Apr 1, 1987·British Journal of Haematology·V BellottiE Zoppone
Jan 1, 1984·CRC Critical Reviews in Biochemistry·R R Porter
Mar 3, 2020·Comparative Biochemistry and Physiology. Part D, Genomics & Proteomics·Bergljót MagnadóttirSigrun Lange
Jul 13, 2006·Journal of Molecular Biology·Folmer FredslundLars Sottrup-Jensen

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