γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (425 views)
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
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Paper type: Journal Article,
Impact factor: 5.615, 5-year impact factor: 6.359
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Keywords: Autoproteolytic Activation, Biotechnological Applications, Gamma-Glutamylhydrolase, Gamma-Glutamyltransferase, Gamma-Glutamyltranspeptidase, Glutathione, Acivicin, Antineoplastic Agent, Bacterial Enzyme, Enzyme Inhibitor, Gamma Glutamyltransferase, Gamma Glutamyltranspeptidase Inhibitor, Glutaurine, Hydroxyl Group, Levodopa, Unclassified Drug, Amino Acid Sequence, Amino Terminal Sequence, Beta Sheet, Binding Site, Biochemistry, Carboxy Terminal Sequence, Catalysis, Crystal Structure, Enzyme Activity, Fermentation, Gamma Glutamyl Transferase Blood Level, Glutathione Metabolism, Molecular Weight, Nonhuman, Nucleotide Sequence, Protein Conformation, Protein Degradation, Protein Glycosylation, Protein Hydrolysis, Protein Modification, Protein Structure, Review, Salt Tolerance, Sequence Alignment, Sequence Analysis, Thermostability, Tuberculosis, Animals, Glutamine, Molecular Conformation, Molecular Sequence Data, Sequence Homology,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, CNR, via Pietro Castellino 111, 80131 Naples, Italy
Department of Chemical Sciences, University of Naples 'Federico II', Complesso Universitario di Monte Sant'Angelo, via cintia, 80126 Naples, Italy
Institute of Biostructures and Bioimages, CNR, via Mezzocannone 16, 80100 Naples, Italy
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West, M. B., Wickham, S., Quinalty, L. M., Pavlovicz, R. E., Li, C., Hanigan, M. H., Autocatalytic cleavage of human gammaglutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95 (2011) J Biol Chem, 286 (33), pp. 28876-28888
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Lin, L. L., Chou, P. R., Hua, Y. W., Hsu, W. H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacillus licheniformis (2006) Appl Microbiol Biotechnol, 73 (1), pp. 103-112
Lyu, R. C., Hu, H. Y., Kuo, L. Y., Lo, H. F., Ong, P. L., Chang, H. P., Lin, L. L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59 (2), pp. 101-106
Tate, S. S., Meister, A., Gamma-Glutamyl transpeptidase from kidney (1985) Methods Enzymol, 113, pp. 400-419
Yang, J. C., Liang, W. C., Chen, Y. Y., Chi, M. C., Lo, H. F., Chen, H. L., Lin, L. L., Biophysical characterization of Bacillus licheniformis and Escherichia coli gamma-glutamyltranspeptidases: A comparative analysis (2011) Int J Biol Macromol, 48 (3), pp. 414-422
Hsu, W. H., Ong, P. L., Chen, S. C., Lin, L. L., Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase (2009) Indian J Biochem Biophys, 46 (4), pp. 281-288
Longley, D. B., Johnston, P. G., Molecular mechanisms of drug resistance (2005) J Pathol, 205, pp. 275-292
Jones, A. W., Smith, D. A., Watkins, J. C., Structure-activity relations of dipeptide antagonists of excitatory amino acids (1984) Neuroscience, 13, pp. 573-581
Vermeulen, N., G nzle, M. G., Vogel, R. F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Glynn, B. P., Johnson, D. B., Gamma-Glutamyltransferase from Marthasterias glacialis: Purification procedures and enzyme characterisation (1985) Comp Biochem Physiol B, 80 (4), pp. 941-948
Hussein, A. S., Walter, R. D., Purification and characterization of gamma-glutamyl transpeptidase from Ascaris suum (1996) Mol Biochem Parasitol, 77 (1), pp. 41-47
Riou, J. Y., Buissiere, J., Richard, C., Guibourdenche, M., Gamma-Glutamyl-transferase activity in the family ''Neisseriaceae'' (author's transl) (1982) Ann Microbiol (Paris, 133 (3), pp. 387-392
Young, J. D., Ellory, J. C., Wright, P. C., Evidence against the participation of the gamma-glutamyltransferase- gamma-glutamylcylclotransferase pathway in amino acid transport by rabbit erythrocytes (1975) Biochem J, 152 (3), pp. 713-715
Hwang, S. Y., Ryang, J. H., Lim, W. J., Yoo, I. D., Oishi, K., Purification and properties of gamma-glutamyl transpeptidase from Bacillus sp. KUN-17 (1996) J Microbiol Biotechnol, 6 (4), pp. 238-244
Braun, J. P., Benard, P., Burgat, V., Rico, A. G., Gamma Glutamyl Transferase in domestic animals (1983) Vet Res Commun, 6 (2), pp. 77-90
Goore, M. Y., Thompson, J. F., Gamma-glutamyl transpeptidase from kidney bean fruit. I. Purification and mechanism of action (1967) Biochim Biophys Acta, 132, pp. 15-26
Curthoys, N. P., Hughey, R. P., Characterization and physiological function of rat renal gamma-glutamyltranspeptidase (1979) Enzyme, 24 (6), pp. 383-403
Penninckx, M. J., Jaspers, C. J., Characterization of gammaglutamylamidase-glutaminase activity in Saccharomyces cerevisiae (1985) Biochimie, 67 (9), pp. 999-1006
Barnes, I. H., Bagnall, M. C., Browning, D. D., Thompson, S. A., Manning, G., Newell, D. G., Gamma-glutamyl transpeptidase has a role in the persistent colonization of the avian gut by Campylobacter jejuni (2007) Microb Pathog, 43 (5-6), pp. 198-207
Kim, H. G., Park, H. J., Kang, H. J., Lim, H. W., Kim, K., Park, E. H., Ahn, K., Lim, C. J., The Schizosaccharomyces pombe gene encoding gamma-glutamyl transpeptidase I is regulated by non-fermentable carbon sources and nitrogen starvation (2005) J Microbiol, 43 (1), pp. 44-48
Singh, S. N., Srivastava, A. K., Chatterjee, R. K., Gamma-glutamyl transpeptidase activity in adult Setaria cervi and Acanthocheilonema viteae and the effect of inhibitors (1996) J Parasit Dis, 20 (2), pp. 163-166
Morrow, A. L., Williams, K., Sand, A., Boanca, G., Barycki, J. J., Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis (2007) Biochemistry, 46 (46), pp. 13407-13414
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
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Paper type: Journal Article,
Impact factor: 5.615, 5-year impact factor: 6.359
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84867576301&partnerID=40&md5=1c5e99bc36100901383f143ab6086d15
Keywords: Autoproteolytic Activation, Biotechnological Applications, Gamma-Glutamylhydrolase, Gamma-Glutamyltransferase, Gamma-Glutamyltranspeptidase, Glutathione, Acivicin, Antineoplastic Agent, Bacterial Enzyme, Enzyme Inhibitor, Gamma Glutamyltransferase, Gamma Glutamyltranspeptidase Inhibitor, Glutaurine, Hydroxyl Group, Levodopa, Unclassified Drug, Amino Acid Sequence, Amino Terminal Sequence, Beta Sheet, Binding Site, Biochemistry, Carboxy Terminal Sequence, Catalysis, Crystal Structure, Enzyme Activity, Fermentation, Gamma Glutamyl Transferase Blood Level, Glutathione Metabolism, Molecular Weight, Nonhuman, Nucleotide Sequence, Protein Conformation, Protein Degradation, Protein Glycosylation, Protein Hydrolysis, Protein Modification, Protein Structure, Review, Salt Tolerance, Sequence Alignment, Sequence Analysis, Thermostability, Tuberculosis, Animals, Glutamine, Molecular Conformation, Molecular Sequence Data, Sequence Homology,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, CNR, via Pietro Castellino 111, 80131 Naples, Italy
Department of Chemical Sciences, University of Naples 'Federico II', Complesso Universitario di Monte Sant'Angelo, via cintia, 80126 Naples, Italy
Institute of Biostructures and Bioimages, CNR, via Mezzocannone 16, 80100 Naples, Italy
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γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications
γ-Glutamyltranspeptidases (γ-GTs) are ubiquitous enzymes that catalyze the hydrolysis of γ-glutamyl bonds in glutathione and glutamine and the transfer of the released γ-glutamyl group to amino acids or short peptides. These enzymes are involved in glutathione metabolism and play critical roles in antioxidant defense, detoxification, and inflammation processes. Moreover, γ-GTs have been recently found to be involved in many physiological disorders, such as Parkinson's disease and diabetes. In this review, the main biochemical and structural properties of γ-GTs isolated from different sources, as well as their conformational stability and mechanism of catalysis, are described and examined with the aim of contributing to the discussion on their structure-function relationships. Possible applications of γ-glutamyltranspeptidases in different fields of biotechnology and medicine are also discussed. © Springer Basel AG 2012.
γ-Glutamyltranspeptidases (γ-GTs) are ubiquitous enzymes that catalyze the hydrolysis of γ-glutamyl bonds in glutathione and glutamine and the transfer of the released γ-glutamyl group to amino acids or short peptides. These enzymes are involved in glutathione metabolism and play critical roles in antioxidant defense, detoxification, and inflammation processes. Moreover, γ-GTs have been recently found to be involved in many physiological disorders, such as Parkinson's disease and diabetes. In this review, the main biochemical and structural properties of γ-GTs isolated from different sources, as well as their conformational stability and mechanism of catalysis, are described and examined with the aim of contributing to the discussion on their structure-function relationships. Possible applications of γ-glutamyltranspeptidases in different fields of biotechnology and medicine are also discussed. © Springer Basel AG 2012.
γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications
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γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications
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Monti SM, De Simone G, Supuran CT, Alterio V
* CDCA1 From Thalassiosira weissflogii as Representative Member of ζ-Class CAs: General Features and Biotechnological Applications (276 views)
Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 351-359.
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Di Fiore A, Alterio V, Monti SM, De Simone G, D’Ambrosio K
* Thermostable carbonic anhydrases in biotechnological applications (491 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(7): 15456-15480.
Impact Factor: 3.257
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Lin L-L, Chen Y-Y, Chi M-C, Merlino A
* Low resolution X-ray structure of γ-glutamyltranspeptidase from Bacillus licheniformis: Opened active site cleft and a cluster of acid residues potentially involved in the recognition of a metal ion (625 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014; 1844(9): 1523-1529.
Impact Factor: 4.882
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Pica A, Russo Krauss I, Castellano I, La Cara F, Graziano G, Sica F, Merlino A
* Effect Of Nacl On The Conformational Stability Of The Thermophilic Gamma-Glutamyltranspeptidase From Geobacillus Thermodenitrificans: Implication For Globular Protein Halotolerance (356 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Jan; 1834(1): 149-157.
Impact Factor: 3.191
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Lin LL, Merlino A
* Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase from Bacillus licheniformis (280 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2013; 69(6): 669-672.
Impact Factor: 0.568
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Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A
* Exploring The Unfolding Mechanism Of Gamma-Glutamyltranspeptidases: The Case Of The Thermophilic Enzyme From Geobacillus Thermodenitrificans (566 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2012 Apr; 1824(4): 571-577.
Impact Factor: 3.733
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Castellano I, Di Salle A, Merlino A, Rossi M, La Cara F
* Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts (347 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2011; 15(2): 259-270.
Impact Factor: 2.941
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Castellano I, Merlino A, Rossi M, La Cara F
* Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity (659 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2010 May; 92(5): 464-474.
Impact Factor: 3.787
View Export to BibTeX Export to EndNote
* CDCA1 From Thalassiosira weissflogii as Representative Member of ζ-Class CAs: General Features and Biotechnological Applications (276 views)
Carbonic Anhydrases As Biocatalysts, 2015 Jan 08; N/D: 351-359.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Di Fiore A, Alterio V, Monti SM, De Simone G, D’Ambrosio K
* Thermostable carbonic anhydrases in biotechnological applications (491 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(7): 15456-15480.
Impact Factor: 3.257
View Export to BibTeX Export to EndNote
Lin L-L, Chen Y-Y, Chi M-C, Merlino A
* Low resolution X-ray structure of γ-glutamyltranspeptidase from Bacillus licheniformis: Opened active site cleft and a cluster of acid residues potentially involved in the recognition of a metal ion (625 views)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2014; 1844(9): 1523-1529.
Impact Factor: 4.882
View Export to BibTeX Export to EndNote
Pica A, Russo Krauss I, Castellano I, La Cara F, Graziano G, Sica F, Merlino A
* Effect Of Nacl On The Conformational Stability Of The Thermophilic Gamma-Glutamyltranspeptidase From Geobacillus Thermodenitrificans: Implication For Globular Protein Halotolerance (356 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Jan; 1834(1): 149-157.
Impact Factor: 3.191
View Export to BibTeX Export to EndNote
Lin LL, Merlino A
* Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase from Bacillus licheniformis (280 views)
Nucleosides Nucleotides Nucleic Acids (ISSN: 1744-3091, 1744-4309), 2013; 69(6): 669-672.
Impact Factor: 0.568
View Export to BibTeX Export to EndNote
Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A
* Exploring The Unfolding Mechanism Of Gamma-Glutamyltranspeptidases: The Case Of The Thermophilic Enzyme From Geobacillus Thermodenitrificans (566 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2012 Apr; 1824(4): 571-577.
Impact Factor: 3.733
View Export to BibTeX Export to EndNote
Castellano I, Di Salle A, Merlino A, Rossi M, La Cara F
* Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts (347 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2011; 15(2): 259-270.
Impact Factor: 2.941
View Export to BibTeX Export to EndNote
Castellano I, Merlino A, Rossi M, La Cara F
* Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity (659 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2010 May; 92(5): 464-474.
Impact Factor: 3.787
View Export to BibTeX Export to EndNote
8 Records (8 excluding Abstracts).
Total impact factor: 22.359 (22.359 excluding Abstracts).
Total 5 year impact factor: 21.268 (21.268 excluding Abstracts).
Total impact factor: 22.359 (22.359 excluding Abstracts).
Total 5 year impact factor: 21.268 (21.268 excluding Abstracts).
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