Download Gamma-Glutamyl Transpeptidases: Structure and Function by Immacolata Castellano, Antonello Merlino PDF

By Immacolata Castellano, Antonello Merlino

Gamma-Glutamyl Transpeptidases (γ-GTs) are participants of the N-terminal nucleophile hydrolase superfamily, enzymes that cleave the γ-glutamyl amide bond of glutathione to disencumber cysteinylglycine. The published γ-glutamyl staff will be transferred to water (hydrolysis) or to amino acids or brief peptides (transpeptidation). γ-GT performs a key function within the gamma glutamyl cycle via regulating the mobile degrees of the antioxidant glutathione, consequently it's a serious enzyme in holding mobile redox homeostasis.γ-GT is upregulated in the course of irritation and in numerous human tumors, and it truly is taken with many physiological problems regarding oxidative rigidity, similar to Parkinson’s affliction and diabetes. in addition, this enzyme is used as a marker of liver illness and melanoma. This ebook covers present wisdom concerning the structure-function dating of γ-GTs and provides information regarding functions of γ-GTs in several fields starting from medical biochemistry to biotechnology and biomedicine.​

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Clin Chem 37(5):662–666 46. Castellano I, Merlino A, Rossi M, La Cara F (2010) Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: an enzyme specialized in hydrolase activity. Biochimie 92(5):464–474 47. Boanca G, Sand A, Barycki JJ (2006) Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma-glutamyltranspeptidase. J Biol Chem 281(28):19029–19037 48. Suzuki H, Kumagai H (2002) Autocatalytic processing of gamma-glutamyltranspeptidase.

Site directed mutagenesis has been used to reveal which residues are important for the catalytic activity of c-GTs. Mutations investigated in the human enzyme are reported in Table 3. 26 Gamma-Glutamyl Transpeptidases Fig. 8 Quest for Inhibitors Rational design of c-GT inhibitors has encountered a lot of difficulties, due to uncertainty about c-GT reaction mechanisms. Compounds which are known to inhibit c-GT include the glutamine analogs Acivicin (L-(aS,5S)-a-amino-3-chloro4,5-dihydro-5-isoxazoleacetic acid), 6-diazo-5-oxo-L-norleucine (DON), and Azaserine (O-diazoacetyl-L-serine) [83] (Fig.

Biochemistry 48(11):2459–2467 References 49 42. Suzuki H, Kajimoto Y, Kumagai H (2002) Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial gamma-glutamyltranspeptidase. J Agric Food Chem 50(2):313–318 43. Chang HP, Liang WC, Lyu RC, Chi MC, Wang TF, Su KL, Hung HC, Lin LL (2010) Effects of C-terminal truncation on autocatalytic processing of Bacillus licheniformis gamma-glutamyl transpeptidase. Biochemistry (Mosc) 75(7):919–929 44. Lin LL, Chou PR, Hua YW, Hsu WH (2006) Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacillus licheniformis.

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