Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius
نویسندگان
چکیده
منابع مشابه
Hetero- and auto-activation of recombinant glutamyl endopeptidase from Bacillus intermedius.
Glutamyl endopeptidase from Bacillus intermedius (BIGEP) is a secretory serine proteinase specifically hydrolyzing peptide bonds involving alpha-carboxyl groups of glutamic and aspartic acids. In this work, different BIGEP forms (full-length precursor, precursor without signal peptide and mature part) were expressed in Escherichia coli and the process of enzyme maturation was studied in vitro. ...
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The present study primarily deals with the identification of substrate-binding site and elucidation of catalytic residue of the phytase from Bacillus sp. (Genbank Accession No. EF536824) employing molecular modeling and site-directed mutagenesis. Homology-based modeling of the Bacillus phytase revealed β-propeller structure with twelve active-site aminoacid residues, viz., D75, R77, Y78, H138, ...
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Quite a few years ago, while studying the inactivation of bradykinin by kidney extracts, an enzyme in a particulate (microsomal) fraction of rat kidney was found to release the C-terminal dipeptide (Phe-Arg) of bradykinin (Erdos & Yang, 1967). This enzyme, named kininase 11, was solubilized with deoxycholate and partially purified by gel filtration. It was subsequently also isolated from human ...
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The three-dimensional structure (3D structure) of Xyn11A, a family 11 xylanase from Bacillus firmus K-1, was obtained through homology modeling. To study the substrate-binding site of Xyn11A, six xylooligosaccharides, xylobiose to xyloheptaose (X2-X7), were docked into the active site of Xyn11A by molecular docking. Based on the docked energy and estimated free energy of binding combined with m...
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ژورنال
عنوان ژورنال: Protein Engineering Design and Selection
سال: 2004
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/gzh050