原创力文档the cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for s-glutathiolation and oxidative oligomerizationcysteine-rich蛋白甲拌磷oligopeptidase s-glutathiolation模型的结构要求和氧化寡聚化.pdfVIP
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the cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for s-glutathiolation and oxidative oligomerizationcysteine-rich蛋白甲拌磷oligopeptidase s-glutathiolation模型的结构要求和氧化寡聚化
The Cysteine-Rich Protein Thimet Oligopeptidase as
a Model of the Structural Requirements for S-
glutathiolation and Oxidative Oligomerization
1 ´ 2,4 1 2 3
Alberto Malvezzi , Patrıcia M. Higa , Antonia T.-do Amaral , Gustavo M. Silva , Fabio C. Gozzo ,
4 4 1 5 2
Emer S. Ferro , Leandro M. Castro , Leandro de Rezende , Gisele Monteiro , Marilene Demasi *
´ ˜ ˜ ˜ ´
1 Instituto de Quımica, Universidade de Sao Paulo, Sao Paulo-SP, Brazil, 2 Instituto Butantan, Sao Paulo-SP, Brazil, 3 Instituto de Quımica, Universidade Estadual de
ˆ ´ ˜ ˜ ˆ ˆ
Campinas, Campinas-SP, Brazil, 4 Instituto de Ciencias Biomedicas, Universidade de Sao Paulo, Sao Paulo-SP, Brazil, 5 Faculdade de Ciencias Farmaceuticas, Universidade
˜ ˜
de Sao Paulo, Sao Paulo-SP, Brazil
Abstract
Thimet oligopeptidase (EP24.15) is a cysteine-rich metallopeptidase containing fifteen Cys residues and no intra-protein
disulfide bonds. Previous work on this enzyme revealed that the oxidative oligomerization of EP24.15 is triggered by S-
glutathiolation at physiological GSSG levels (10–50 mM) via a mechanism based on thiol-disulfide exchange. In the present
work, our aim was to identify EP24.15 Cys residues that are prone to S-glutathiolation and to determine which structural
features in the cysteinyl
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