Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity (900 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2010 May; 92(5): 464-474.
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Paper type: Journal Article,
Impact factor: 3.787, 5-year impact factor: 3.728
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77951022274&partnerID=40&md5=0d5d364b736e3efba57602ea96b6f062
Keywords: Gamma-Glutamyltranspeptidase, Geobacillus Thermodenitrificans, Glutathione, N-Terminal Nucleophile Hydrolase, Thermophilic Enzymes, Amide, Amino Acid, Anilide, Gamma Glutamyltransferase, Glutamic Acid, Protein Precursor, Water, Article, Biotechnology, Catalysis, Chemical Analysis, Controlled Study, Drug Targeting, Enzyme Activity, Enzyme Purification, Enzyme Stability, Enzyme Structure, Enzyme Substrate, Enzyme Subunit, Escherichia Coli, Glutathione Metabolism, Hydrolysis, Molecular Cloning, Nonhuman, Oxidative Stress, Protein Cleavage, Protein Expression, Structure Analysis, Temperature, Amino Acid Sequence, Base Sequence, Biocatalysis, Dna Primers, Electrophoresis, Polyacrylamide Gel, Gamma-Glutamyl Hydrolase, Gamma-Glutamyltransferase, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Sequence Homology,
Affiliations:
*** IBB - CNR ***
CNR, Institute of Protein Biochemistry, Via Pietro Castellino 111, I-80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', Via Cinthia, I-80126 Naples, Italy
References:
Not available.
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2010 May; 92(5): 464-474.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.787, 5-year impact factor: 3.728
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77951022274&partnerID=40&md5=0d5d364b736e3efba57602ea96b6f062
Keywords: Gamma-Glutamyltranspeptidase, Geobacillus Thermodenitrificans, Glutathione, N-Terminal Nucleophile Hydrolase, Thermophilic Enzymes, Amide, Amino Acid, Anilide, Gamma Glutamyltransferase, Glutamic Acid, Protein Precursor, Water, Article, Biotechnology, Catalysis, Chemical Analysis, Controlled Study, Drug Targeting, Enzyme Activity, Enzyme Purification, Enzyme Stability, Enzyme Structure, Enzyme Substrate, Enzyme Subunit, Escherichia Coli, Glutathione Metabolism, Hydrolysis, Molecular Cloning, Nonhuman, Oxidative Stress, Protein Cleavage, Protein Expression, Structure Analysis, Temperature, Amino Acid Sequence, Base Sequence, Biocatalysis, Dna Primers, Electrophoresis, Polyacrylamide Gel, Gamma-Glutamyl Hydrolase, Gamma-Glutamyltransferase, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Sequence Homology,
Affiliations:
*** IBB - CNR ***
CNR, Institute of Protein Biochemistry, Via Pietro Castellino 111, I-80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', Via Cinthia, I-80126 Naples, Italy
References:
Not available.
Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
Gamma-glutamyltranspeptidases (gamma-GTs) catalyze the transfer of the gamma-glutamyl moiety of glutathione and related gamma-glutamyl amides to water (hydrolysis) or to amino acids and peptides (transpeptidation) and play a key role in glutathione metabolism. Recently, gamma-GTs have been considered attractive pharmaceutical targets for cancer and useful tools to produce gamma-glutamyl compounds. To find out gamma-GTs with special properties we have chosen microorganisms belonging to Geobacillus species which are source of several thermostable enzymes of potential interest for biotechnology. gamma-GT from Geobacillus thermodenitrificans (GthGT) was cloned, expressed in Escherichia coli, purified to homogeneity and characterized. The enzyme, synthesized as a precursor homotetrameric protein of 61-kDa per subunit, undergoes an internal post-translational cleavage of the 61 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits. The kinetic characterization of the hydrolysis reaction using L-glutamic acid gamma-(4-nitroanilide) as the substrate reveals that the active enzyme has K-m 7.6 mu M and V-max 0.36 mu mol min/mg. The optimum pH and temperature for the hydrolysis activity are 7.8 and 52 degrees C. respectively. GthGT hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress. Unlike other gamma-GTs, the mutation of the highly conserved catalytic nucleophile, Thr353, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action. Furthermore, GthGT does not show any transpeptidase activity, suggesting that the enzyme is a specialized gamma-glutamyl hydrolase. The GthGT homology-model structure reveals peculiar structural features, which should be responsible for the different functional properties of the enzyme and suggests the structural bases of protein thermostability. (C) 2010 Elsevier Masson SAS. All rights reserved.
Gamma-glutamyltranspeptidases (gamma-GTs) catalyze the transfer of the gamma-glutamyl moiety of glutathione and related gamma-glutamyl amides to water (hydrolysis) or to amino acids and peptides (transpeptidation) and play a key role in glutathione metabolism. Recently, gamma-GTs have been considered attractive pharmaceutical targets for cancer and useful tools to produce gamma-glutamyl compounds. To find out gamma-GTs with special properties we have chosen microorganisms belonging to Geobacillus species which are source of several thermostable enzymes of potential interest for biotechnology. gamma-GT from Geobacillus thermodenitrificans (GthGT) was cloned, expressed in Escherichia coli, purified to homogeneity and characterized. The enzyme, synthesized as a precursor homotetrameric protein of 61-kDa per subunit, undergoes an internal post-translational cleavage of the 61 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits. The kinetic characterization of the hydrolysis reaction using L-glutamic acid gamma-(4-nitroanilide) as the substrate reveals that the active enzyme has K-m 7.6 mu M and V-max 0.36 mu mol min/mg. The optimum pH and temperature for the hydrolysis activity are 7.8 and 52 degrees C. respectively. GthGT hydrolyses the physiological antioxidant glutathione, suggesting an involvement of the enzyme in the cellular defense mechanism against oxidative stress. Unlike other gamma-GTs, the mutation of the highly conserved catalytic nucleophile, Thr353, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action. Furthermore, GthGT does not show any transpeptidase activity, suggesting that the enzyme is a specialized gamma-glutamyl hydrolase. The GthGT homology-model structure reveals peculiar structural features, which should be responsible for the different functional properties of the enzyme and suggests the structural bases of protein thermostability. (C) 2010 Elsevier Masson SAS. All rights reserved.
Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
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Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity
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View Export to BibTeX Export to EndNote
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Impact Factor: 6.718
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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 (1632 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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Truppo E, Supuran CT, Sandomenico A, Vullo D, Innocenti A, Di Fiore A, Alterio V, De Simone G, Monti SM
* Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (703 views)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2012 Feb 15; 22(4): 1560-1564.
Impact Factor: 2.338
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Cirillo G, Colangelo AM, Bianco MR, Cavaliere C, Zaccaro L, Sarmientos P, Alberghina L, Papa M
* BB14, a Nerve Growth Factor (NGF)-like peptide shown to be effective in reducing reactive astrogliosis and restoring synaptic homeostasis in a rat model of peripheral nerve injury (782 views)
Biotechnology Advances (ISSN: 0734-9750), 2012 Jan; 30(1): 223-232.
Impact Factor: 9.599
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Castellano I, Merlino A
* γ-glutamyltranspeptidases: Sequence, structure, biochemical properties, and biotechnological applications (1209 views)
Cell Mol Life Sci (ISSN: 1420-682x), 2012; 69(20): 3381-3394.
Impact Factor: 5.615
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De Rosa V, Erkekoǧlu P, Forestier A, Favier A, Hincal F, Diamond AM, Douki T, Rachidi W
* Low doses of selenium specifically stimulate the repair of oxidative DNA damage in LNCaP prostate cancer cells (1579 views)
Free Radic Res Free Radical Research (ISSN: 1071-5762), 2012; 46(2): 105-115.
Impact Factor: 3.279
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Merlino A, Russo Krauss I, Albino A, Pica A, Vergara A, Masullo M, De Vendittis E, Sica F
* Improving Protein Crystal Quality by the Without-Oil Microbatch Method: Crystallization and Preliminary X-ray Diffraction Analysis of Glutathione Synthetase from Pseudoalteromonas haloplanktis (770 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067electronic), 2011 Sep; 12(9): 6312-6319.
Impact Factor: 2.598
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Cirillo G, Bianco MR, Colangelo AM, Cavaliere C, Daniele DL, Zaccaro L, Alberghina L, Papa M
* Reactive astrocytosis-induced perturbation of synaptic homeostasis is restored by nerve growth factor (736 views)
Neurobiology Of Disease (ISSN: 0969-9961), 2011 Mar; 41(3): 630-639.
Impact Factor: 5.403
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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 (745 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2011; 15(2): 259-270.
Impact Factor: 2.941
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Alterio V, Aurilia V, Romanelli A, Parracino A, Saviano M, D'Auria S, De Simone G
* Crystal structure of an S-formylglutathione hydrolase from pseudoalteromonas haloplanktis TAC125 (825 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2010 Sep; 93(8): 669-677.
Impact Factor: 2.572
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Erkekoǧlu P, Rachidi W, De Rosa V, Giray B, Favier A, Hincal F
* Protective effect of selenium supplementation on the genotoxicity of di(2-ethylhexyl)phthalate and mono(2-ethylhexyl)phthalate treatment in LNCaP cells (1196 views)
Free Radic Biol Med (ISSN: 0891-5849, 0891-5849linking, 1873-4596electronic), 2010 Aug 15; 49(4): 559-566.
Impact Factor: 5.707
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Pedone E, Limauro D, Bartolucci S
* The Machinery for Oxidative Protein Folding in Thermophiles (vol 10, pg 157, 2008) (756 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2010 Jan; 12(1): 157-169.
Impact Factor: 8.209
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Doti N, Marasco D, Pedone C, Sabatella M, Ruvo M
* Optimizing A Kinase Assay For Ikkbeta On An Hts Station (774 views)
J Biomol Screen (ISSN: 1087-0571, 1552-454x, 1552-454xelectronic), 2009 Dec; 14(10): 1263-1268.
Impact Factor: 2.395
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Bellia F, Calabrese V, Guarino F, Cavallaro M, Cornelius C, De Pinto V, Rizzarelli E
* Carnosinase levels in aging brain: redox state induction and cellular stress response (947 views)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 2009 Nov; 11(11): 2759-2775.
Impact Factor: 7.581
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Calabrese V, Cornelius C, Rizzarelli E, Owen JB, Dinkova-Kostova AT, Butterfield DA
* Nitric oxide in cell survival: a janus molecule (2081 views)
Antioxid Redox Signal (ISSN: 1557-7716, 1523-0864, 1523-0864linking), 2009 Nov; 11(11): 2717-2739.
Impact Factor: 7.581
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Limauro D, Saviano M, Galdi I, Rossi M, Bartolucci S, Pedone E
* Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (629 views)
Protein Engineering Design & Selection (ISSN: 1741-0126), 2009 Jan; 22(1): 19-26.
Impact Factor: 2.596
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Pedone E, Limauro D, Bartolucci S
* The machinery for oxidative protein folding in thermophiles (664 views)
Antioxid Redox Signal (ISSN: 1523-0864, 1557-7716, 1523-0864linking), 2008 Jan; 10(1): 157-169.
Impact Factor: 6.19
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Agostini S, Bolzati C, Didonè E, Cavazza-Ceccato M, Refosco F, Aloj L, Arra C, Aurilio M, Tornesello AL, Tesauro D, Morelli G
* The (Tc(N)(PNP))2+ metal fragment labeled cholecystokinin-8 (CCK8) peptide for CCK-2 receptors imaging: In vitro and in vivo studies (748 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2007 Apr; 13(4): 211-219.
Impact Factor: 1.768
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Pedone E, Limauro D, D'Alterio R, Rossi M, Bartolucci S
* Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (734 views)
Febs Journal (ISSN: 1742-464x), 2006 Dec; 273(23): 5407-5420.
Impact Factor: 3.033
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D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S
* A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics (983 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Sep 29; 362(4): 743-752.
Impact Factor: 4.89
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Cappiello M, Alterio V, Amodeo P, Del Corso A, Scaloni A, Pedone C, Moschini R, De Donatis GM, De Simone G, Mura U
* A new spot test for sulfhydryl-containing compounds (793 views)
Anal Biochem, 2006 Mar 14; 79(1-2): 610-611.
Impact Factor: 2.305
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Cappiello M, Alterio V, Amodeo P, Del Corso A, Scaloni A, Pedone C, Moschini R, De Donatis GM, De Simone G, Mura U
* Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase (1577 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Mar 14; 45(10): 3226-3234.
Impact Factor: 3.633
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Mannini R, Rivieccio V, D'Auria S, Tanfani F, Ausili A, Pedone C, Grimaldi G, Facchiano A
* Structure/function of KRAB repression domains: Structural properties of KRAB modules inferred from hydrodynamic, circular dichroism, and FTIR spectroscopic analyses (1129 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 15; 62(3): 604-616.
Impact Factor: 3.73
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Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
* Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (793 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2006 Feb 10; 356(1): 155-164.
Impact Factor: 4.89
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Pedone E, Saviano M, Bartolucci S, Rossi M, Ausili A, Scire A, Bertoli E, Tanfani F
* Temperature-, SDS-, and pH-induced conformational changes in protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus: A dynamic simulation and fourier transform infrared spectroscopic study (835 views)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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Pedone E, Ren B, Ladenstein R, Rossi M, Bartolucci S
* Functional properties of the protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus - A member of a novel protein family related to protein disulfide-isomerase (717 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 Sep; 271(16): 3437-3448.
Impact Factor: 3.26
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D'Ambrosio K, Kauffmann B, Rouhier N, Benedetti E, Jacquot JP, Aubry A, Corbier C
* Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione (1343 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2003 Jun; 59: 1043-1045.
Impact Factor: 2.208
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Orru S, Vitagliano L, Esposito L, Mazzarella L, Marino G, Ruoppolo M
Effect of deamidation on folding of ribonuclease (997 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Dec; 9(12): 2577-2582.
Impact Factor: 3.869
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Del Vecchio S, Ciarmiello A, Salvatore M
Clinical imaging of multidrug resistance in cancer (675 views)
Q J Nucl Med (ISSN: 1124-3937, 1125-0135), 1999 Jun; 43(2): 125-131.
Impact Factor: 2.125
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Wink DA, Vodovotz Y, Grisham MB, DeGraff W, Cook JC, Pacelli R, Krishna M, Mitchell JB
Antioxidant effects of nitric oxide (590 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic), 1998; 301: 413-424.
Impact Factor: 2.823
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Cook JA, Krishna MC, Pacelli R, DeGraff W, Liebmann J, Mitchell JB, Russo A, Wink DA
Nitric oxide enhancement of melphalan-induced cytotoxicity (797 views)
Br J Cancer (ISSN: 0007-0920, 0007-0920print, 0007-0920linking), 1997 Sep; 76(3): 325-334.
Impact Factor: 2.938
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Wink DA, Cook JA, Kim SY, Vodovotz Y, Pacelli R, Krishna MC, Russo A, Mitchell JB, Jourd'heuil D, Miles AM, Grisham MB
Superoxide modulates the oxidation and nitrosation of thiols by nitric oxide-derived reactive intermediates (1041 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 1997 Apr 25; 272(17): 11147-11151.
Impact Factor: 6.963
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Wink DA, Cook JA, Christodoulou D, Krishna MC, Pacelli R, Kim S, DeGraff W, Gamson J, Vodovotz Y, Russo A, Mitchell JB
Nitric oxide and some nitric oxide donor compounds enhance the cytotoxicity of cisplatin (902 views)
Nitric Oxide Biology And Chemistry (ISSN: 1089-8603), 1997 Feb; 1(1): 88-94.
Impact Factor: 2.151
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Wink DA, Cook JA, Pacelli R, DeGraff W, Gamson J, Liebmann J, Krishna MC, Mitchell JB
The effect of various nitric oxide-donor agents on hydrogen peroxide-mediated toxicity: A direct correlation between nitric oxide formation and protection (1157 views)
Arch Bioch Bioph (ISSN: 0003-9861, 0003-9861linking), 1996 Jul 15; 331(2): 241-248.
Impact Factor: 2.649
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Wink DA, Grisham MB, Miles AM, Nims RW, Krishna MC, Pacelli R, Teague D, Poore CM, Cook JA, Ford PC
Determination of selectivity of reactive nitrogen oxide species for various substrates (805 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic, 0076-6879linking), 1996; 268: 120-130.
Impact Factor: 2.435
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Wink DA, Cook JA, Pacelli R, Liebmann J, Krishna MC, Mitchell JB
Nitric oxide (NO) protects against cellular damage by reactive oxygen species (963 views)
Toxicology Letters (ISSN: 0378-4274), 1995 Dec; 82-3: 221-226.
Impact Factor: 1.128
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Pacelli R, Wink DA, Cook JA, Krishna MC, DeGraff W, Friedman N, Tsokos M, Samuni A, Mitchell JB
NITRIC-OXIDE POTENTIATES HYDROGEN PEROXIDE-INDUCED KILLING OF ESCHERICHIA-COLI (1107 views)
Journal Of Experimental Medicine (ISSN: 0022-1007), 1995 Nov 1; 182(5): 1469-1479.
Impact Factor: 14.384
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Bonomo RP, De Flora A, Rizzarelli E, Santoro AM, Tabbì G, Tonetti M
Copper(II) complexes encapsulated in human red blood cells (939 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1995 Sep; 59(4): 773-784.
Impact Factor: 1.342
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44 Records (44 excluding Abstracts).
Total impact factor: 183.876 (183.876 excluding Abstracts).
Total 5 year impact factor: 191.928 (191.928 excluding Abstracts).
Total impact factor: 183.876 (183.876 excluding Abstracts).
Total 5 year impact factor: 191.928 (191.928 excluding Abstracts).
900 views. Last view on Wednesday 16 April 2025, 14:36:08
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