Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (497 views)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2012 Feb 15; 22(4): 1560-1564.
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Paper type: Journal Article,
Impact factor: 2.338, 5-year impact factor: 2.427
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84856650479&partnerID=40&md5=c2a1c1a6110bc59c42b21b52d5f6f2a5
Keywords: Ca Inhibitors, Carbonic Anhydrase Vii, Catalytic Activity, Cysteine Reactivity, Glutathionylation, Acetazolamide, Carbon Dioxide, Carbonate Dehydratase, Carbonate Dehydratase Ii, Esterase, Glutathione Transferase, Oxygen, Phosphatase, Scavenger, Sulfonamide, Unclassified Drug, Animal Cell, Article, Catalysis, Cell Protection, Controlled Study, Enzyme Activity, Enzyme Inhibition, Enzyme Mechanism, Enzyme Modification, Human, Human Cell, Hydration, Hydrolysis, In Vitro Study, In Vivo Study, Nonhuman, Oxidation, Oxidative Stress, Protein Analysis, Protein Expression, Protein Function, Protein Localization, Amino Acid Sequence, Carbonic Anhydrase Inhibitors, Cytosol, Enzyme Activation, Inhibitory Concentration 50, Molecular Sequence Data, Protein Isoforms, S-Nitrosoglutathione, Sequence Alignment, Spectrometry, Electrospray Ionization,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 0134 Napoli, Italy
Università Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
Universit Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
References:
Not available.
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2012 Feb 15; 22(4): 1560-1564.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.338, 5-year impact factor: 2.427
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84856650479&partnerID=40&md5=c2a1c1a6110bc59c42b21b52d5f6f2a5
Keywords: Ca Inhibitors, Carbonic Anhydrase Vii, Catalytic Activity, Cysteine Reactivity, Glutathionylation, Acetazolamide, Carbon Dioxide, Carbonate Dehydratase, Carbonate Dehydratase Ii, Esterase, Glutathione Transferase, Oxygen, Phosphatase, Scavenger, Sulfonamide, Unclassified Drug, Animal Cell, Article, Catalysis, Cell Protection, Controlled Study, Enzyme Activity, Enzyme Inhibition, Enzyme Mechanism, Enzyme Modification, Human, Human Cell, Hydration, Hydrolysis, In Vitro Study, In Vivo Study, Nonhuman, Oxidation, Oxidative Stress, Protein Analysis, Protein Expression, Protein Function, Protein Localization, Amino Acid Sequence, Carbonic Anhydrase Inhibitors, Cytosol, Enzyme Activation, Inhibitory Concentration 50, Molecular Sequence Data, Protein Isoforms, S-Nitrosoglutathione, Sequence Alignment, Spectrometry, Electrospray Ionization,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 0134 Napoli, Italy
Università Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
Universit Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
References:
Not available.
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic isoform. Cys183 and Cys217 were found to be the residues involved in reaction with glutathione for hCA VII. The two reactive cysteines were then mutated and the corresponding variant (C183S/C217S) expressed. The native enzyme, the variant and the S-glutathionylated adduct (sgCA VII) as well as hCA III were fully characterized for their CO 2 hydration, esterase/ phosphatase activities, and inhibition with sulfonamides. Our findings suggest that hCA VII could use the in vivo S-glutathionylation to function as an oxygen radical scavenger for protecting cells from oxidative damage, as the activity and affinity for inhibitors of the modified enzyme are similar to those of the wild type. © 2012 Elsevier Ltd. All rights reserved.
Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic isoform. Cys183 and Cys217 were found to be the residues involved in reaction with glutathione for hCA VII. The two reactive cysteines were then mutated and the corresponding variant (C183S/C217S) expressed. The native enzyme, the variant and the S-glutathionylated adduct (sgCA VII) as well as hCA III were fully characterized for their CO 2 hydration, esterase/ phosphatase activities, and inhibition with sulfonamides. Our findings suggest that hCA VII could use the in vivo S-glutathionylation to function as an oxygen radical scavenger for protecting cells from oxidative damage, as the activity and affinity for inhibitors of the modified enzyme are similar to those of the wild type. © 2012 Elsevier Ltd. All rights reserved.
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
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Buonanno M, Di Fiore A, Langella E, D’ambrosio K, Supuran CT, Monti SM, De Simone G
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Impact Factor: 3.687
View Export to BibTeX Export to EndNote
Monti DM, De Simone G, Langella E, Supuran CT, Di Fiore A, Monti SM
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J Enzym Inhib Med Ch (ISSN: 1475-6366, 1475-6374electronic, 1475-6366linking), 2017 Dec; 32(1): 5-12.
Impact Factor: 3.638
View Export to BibTeX Export to EndNote
Vitale R, Lista L, Cerrone C, Caserta G, Chino M, Maglio O, Nastri F, Pavone V, Lombardi A
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Impact Factor: 3.559
View Export to BibTeX Export to EndNote
Monti SM, Supuran CT, De Simone G, Di Fiore A
* Carbonic Anhydrase VII (306 views)
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Impact Factor: 0
View Export to BibTeX Export to EndNote
Del Giudice R, Monti DM, Truppo E, Arciello A, Supuran CT, De Simone G, Monti SM
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Impact Factor: 2.689
View Export to BibTeX Export to EndNote
Di Fiore A, Truppo E, Supuran CT, Alterio V, Dathan N, Bootorabi F, Parkkila S, Monti SM, De Simone G
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Bioorg Med Chem Lett (ISSN: 0960-894x), 2010 Sep 1; 20(17): 5023-5026.
Impact Factor: 2.661
View Export to BibTeX Export to EndNote
Hilvo M, De Simone G, Supuran CT, Parkkila S
* Advances in the Inhibitory and Structural Investigations on Carbonic Anhydrase Isozymes XIII and XV (380 views)
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Impact Factor: 1.156
View Export to BibTeX Export to EndNote
Hilvo M, Innocenti A, Monti SM, De Simone G, Supuran CT, Parkkila S
* Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV (799 views)
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Impact Factor: 4.399
View Export to BibTeX Export to EndNote
Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (670 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Bonomo RP, Cennamo G, Purrello R, Santoro AM, Zappala R
* Comparison Of Three Fungal Laccases From Rigidoporus Lignosus And Pleurotus Ostreatus: Correlation Between Conformation Changes And Catalytic Activity (453 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2001 Jan 1; 83(1): 67-75.
Impact Factor: 1.729
View Export to BibTeX Export to EndNote
19 Records (19 excluding Abstracts).
Total impact factor: 60.768 (60.768 excluding Abstracts).
Total 5 year impact factor: 50.199 (50.199 excluding Abstracts).
Total impact factor: 60.768 (60.768 excluding Abstracts).
Total 5 year impact factor: 50.199 (50.199 excluding Abstracts).
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