Experimental evidence for the involvement of amino acid residue Glu398 in the autocatalytic processing of Bacillus licheniformis γ-glutamyltranspeptidase

γ-Glutamyl transpeptidase from Bacillus pumilus KS 12: Decoupling autoprocessing from catalysis and molecular characterization of N-terminal region

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Biophysical characterization of Bacillus licheniformis and Escherichia coli γ-glutamyltranspeptidases: A comparative analysis

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Purification and Characterization of γ-Glutamyltranspeptidase fromBacillus subtilisSK11.004

(2011) Yuying Shuai et al.   JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

Unfolding analysis of the mature and unprocessed forms of Bacillus licheniformis γ-glutamyltranspeptidase

(2011) Chih-Peng Hung et al.   JOURNAL OF BIOLOGICAL PHYSICS

Effects of C-terminal truncation on autocatalytic processing of Bacillus licheniformis γ-glutamyl transpeptidase

(2010) Hui-Ping Chang et al.   BIOCHEMISTRY-MOSCOW

Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity

(2010) Immacolata Castellano et al.   BIOCHIMIE

Role of the Conserved Thr399 and Thr417 Residues of Bacillus licheniformis γ-Glutamyltranspeptidase as Evaluated by Mutational Analysis

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