The maturation mechanism of γ-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies

The maturation mechanism of γ-glutamyl transpeptidases: Insights from the crystal structure of a precursor mimic of the enzyme from Bacillus licheniformis and from site-directed mutagenesis studies (113 visite)

Pica A, Chi M-C, Chen Y-Y, D'Ischia M, Lin L-L, Merlino A

Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2016; 1864(2): 195-203.

Tipo di articolo: Journal Article,

Impact factor: 5.476, Impact factor a 5 anni: 5.725

Url: https://www2.scopus.com/inward/record.uri?eid=2-s2.0-84948453364&partnerID=40&md5=6569aec1c5036717080cf6d0ed6aa37a

Parole chiave: Autoprocessing, Single-Point Mutation, X-Ray Crystallography, γ-Glutamyltranspeptidase, γ-Gt Precursor, Alanine, Bacterial Enzyme, Carbonyl Derivative, Enzyme Precursor, Gamma Glutamyltransferase, Hydroxyl Group, Threonine, Article, Bacillus Licheniformis, Controlled Study, Crystal Structure, Enzyme Activity, Enzyme Mechanism, Enzyme Structure, Hydrogen Bond, Nonhuman, Nucleophilicity, Priority Journal, Site Directed Mutagenesis, X Ray Crystallography,

Affiliazioni:

*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone, 16, Naples, Italy
Department of Applied Chemistry, National Chiayi University, 300 Syuefu Road, Chiayi City, Taiwan

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γ-Glutamyl transpeptidases (γ-GTs) are members of N-terminal nucleophile hydrolase superfamily. They are synthetized as single-chain precursors, which are then cleaved to form mature enzymes. Basic aspects of autocatalytic processing of these pro-enzymes are still unknown. Here we describe the X-ray structure of the precursor mimic of Bacillus licheniformis γ-GT (BlGT), obtained by mutating catalytically important threonine to alanine (T399A-BlGT), and report results of autoprocessing of mutants of His401, Thr415, Thr417, Glu419 and Arg571. Data suggest that Thr417 is in a competent position to activate the catalytic threonine (Thr399) for nucleophilic attack of the scissile peptide bond and that Thr415 plays a major role in assisting the process. On the basis of these new structural results, a possible mechanism of autoprocessing is proposed. This mechanism, which guesses the existence of a six-membered transition state involving one carbonyl and two hydroxyl groups, is in agreement with all the available experimental data collected on γ-GTs from different species and with our new Ala-scanning mutagenesis data. © 2015 Elsevier B.V. All rights reserved.

Interrogazione effettuata: [atitle, keywords] "Autoprocessing" OR [atitle, keywords] "Single-Point Mutation" OR [atitle, keywords] "X-Ray Crystallography" OR [atitle, keywords] "γ-Glutamyltranspeptidase" OR [atitle, keywords] "γ-Gt Precursor" OR [atitle, keywords] "Bacterial Enzyme" OR [atitle, keywords] "Carbonyl Derivative"

Nessun risultato.

Interrogazione effettuata: [ptitle] "Autoprocessing" OR [ptitle] "Single-Point Mutation" OR [ptitle] "X-Ray Crystallography" OR [ptitle] "γ-Glutamyltranspeptidase" OR [ptitle] "γ-Gt Precursor" OR [ptitle] "Bacterial Enzyme" OR [ptitle] "Carbonyl Derivative"

Nessun risultato.

Interrogazione effettuata: [btitle, keywords] "Autoprocessing" [btitle, keywords] "Single-Point Mutation" [btitle, keywords] "X-Ray Crystallography" [btitle, keywords] "γ-Glutamyltranspeptidase" [btitle, keywords] "γ-Gt Precursor" [btitle, keywords] "Bacterial Enzyme" [btitle, keywords] "Carbonyl Derivative"

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Di Fiore A, Scozzafava A, Winum JY, Montero JL, Pedone C, Supuran CT, De Simone G
* Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties (151 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2007 Mar 15; 17(6): 1726-1731.
Impact Factor: 2.604
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Menchise V, De Simone G, Di Fiore A, Scozzafava A, Supuran CT
* Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1, 3, 4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)1, 3, 4-thiadiazole-2-sulfon amide to human isoform II (124 visite)
Bioorganic & Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Dec 15; 16(24): 6204-6208.
Impact Factor: 2.538
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Di Fiore A, Pedone C, D'Ambrosio K, Scozzafava A, De Simone G, Supuran CT
* Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib (138 visite)
Bioorg Med Chem Lett Bioorganic And Medicinal Chemistry Letters (ISSN: 0960-894x), 2006 Jan 15; 16(2): 437-442.
Impact Factor: 2.538
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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 (105 visite)
J Proteome Res (ISSN: 1535-3893), 2005 Nov; 4(6): 1972-1980.
Impact Factor: 6.901
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Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus (139 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Dec 16; 42(49): 14397-14407.
Impact Factor: 3.922
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Esposito L, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A
* Crystal Structure Of The Alcohol Dehydrogenase From The Hyperthermophilic Archaeon Sulfolobus Solfataricus At 1. 85 Angstrom Resolution (136 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2002 Apr 26; 318(2): 463-477.
Impact Factor: 5.359
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Esposito L, Vitagliano L, Zagari A, Mazzarella L
Pyramidalization of backbone carbonyl carbon atoms in proteins (135 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Oct; 9(10): 2038-2042.
Impact Factor: 3.869
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47 Records (47 escludendo Abstract e Conferenze).
Impact factor totale: 179.086 (179.086 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 167.613 (167.613 escludendo Abstract e Conferenze).

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