γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (438 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
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
References:
Not available.
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
Export to BibTeX Export to EndNote
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
References:
Not available.
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
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Lin L-L, Chen Y-Y, Chi M-C, Merlino A
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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 (374 views)
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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 (291 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 (683 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 (388 views)
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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 (681 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 (284 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 (567 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 (735 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 (374 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 (291 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 (683 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 (388 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 (681 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).
438 views. Last view on Sunday 12 November 2023, 1:29:01
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