Výsledky vyhledávání - "Ilyas G. Khaliullin"

Akademický článek

The nature of the ligand's side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex.

Autor: Valery Kh Akparov, Vladimir I Timofeev, Galina E Konstantinova, Ilyas G Khaliullin, Inna P Kuranova, Tatiana V Rakitina, Vytas Švedas

Publikováno v: PLoS ONE, Vol 14, Iss 12, p e0226636 (2019)

The carboxypeptidase T (CPT) from Thermoactinomyces vulgaris has an active site structure and 3D organization similar to pancreatic carboxypeptidases A and B (CPA and CPB), but differs in broader substrate specificity. The crystal structures of CPT c

Externí odkaz: https://doaj.org/article/031ff4c64e8640399fe915818993388c

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Preparation, Crystallization, and Preliminary X-Ray Diffraction Study of Mutant Carboxypeptidase T Bearing the Primary Specificity Pocket and the Active-Site Loop of Carboxypeptidase B

Autor: Ilyas G. Khaliullin, Galina E. Konstantinova, Vladimir I. Timofeev, Inna P. Kuranova, V. Kh. Akparov

Publikováno v: Crystallography Reports. 65:900-902

Crystals of mutant carboxypeptidase T from Thermoactinomyces vulgaris (CPT11QG) with amino-acid substitutions G215S, Q249G, A251G, T257A, D260G, T262D, and L254I and with the insertion ins253T were grown in microgravity by the capillary counter-diffu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8c6cf2a1a8b248b92de62ef7e41a9522
https://doi.org/10.1134/s106377452006005x

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Mobile Loop in the Active Site of Metallocarboxypeptidases as an Underestimated Determinant of Substrate Specificity

Autor: Ilyas G. Khaliullin, Inna P. Kuranova, Tatiana V. Rakitina, Vladimir I. Timofeev, E. G. Konstantinova, V. Kh. Akparov, Vytas K. Švedas

Publikováno v: Biochemistry (Moscow). 83:1594-1602

It is generally accepted that the primary specificity of metallocarboxypeptidases is mainly determined by the structure of the so-called primary specificity pocket. However, the G215S/A251G/T257A/D260G/T262D mutant of carboxypeptidase T from Thermoac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aea6357da63604bc16e2adba5b5e9d87
https://doi.org/10.1134/s0006297918120167

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Crystal structures of carboxypeptidase T complexes with transition-state analogs

Autor: Ilyas G. Khaliullin, Valery Kh. Akparov, Inna P. Kuranova, Vladimir I. Timofeev, Vytas K. Švedas, Tatiana V. Rakitina

Publikováno v: Journal of Biomolecular Structure and Dynamics. 36:3958-3966

Metallocarboxypeptidases (MCPs) have been in a focus of biochemical studies since 1954 when carboxypeptidase A (CPA) was discovered as the second, after carbonic anhydrase, zinc-dependent enzyme up...

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b533cebdc7084585df9eda9330f4b2b7
https://doi.org/10.1080/07391102.2017.1404932

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Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine

Autor: Vladimir I. Timofeev, Galina E. Konstantinova, Ilyas G. Khaliullin, Valery Kh. Akparov, Inna P. Kuranova

Publikováno v: Biophysical Chemistry. 270:106535

Carboxypeptidase T (CPT) from Thermoactinomyces vulgaris (EC 3.4.17.18) has a broad substrate specificity, the mechanism of which remains unclear. It cleaves off arginine residues by 10, and lysine residues by 100 times worse than hydrophobic leucine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::483f9328ff1b6e91f57c5c61f9936967
https://doi.org/10.1016/j.bpc.2020.106535

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Structural insights into the broad substrate specificity of carboxypeptidase T fromThermoactinomyces vulgaris

Autor: Valery Kh. Akparov, Inna P. Kuranova, Galina G. Chestukhina, Vladimir I. Timofeev, Vytas K. Švedas, Ilyas G. Khaliullin

Publikováno v: FEBS Journal. 282:1214-1224

The crystal structures of carboxypeptidase T (CpT) complexes with phenylalanine and arginine substrate analogs - benzylsuccinic acid and (2-guanidinoethylmercapto)succinic acid - were determined by the molecular replacement method at resolutions of 1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9106f2e6811eedab9c05a36700f14c63
https://doi.org/10.1111/febs.13210

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Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific substrate

Autor: Vytas K. Švedas, Vladimir I. Timofeev, Ilyas G. Khaliullin, Valery Kh. Akparov, Inna P. Kuranova

Publikováno v: Journal of biomolecular structuredynamics. 36(4)

Carboxypeptidase B (EC 3.4.17.2) (CPB) is commonly used in the industrial insulin production and as a template for drug design. However, its ability to discriminate substrates with hydrophobic, hydrophilic, and charged side chains is not well underst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6964cf60b829c02dcc307174b235efa8
https://pubmed.ncbi.nlm.nih.gov/28274181

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The nature of the ligand’s side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex

Autor: Vytas K. Švedas, Tatiana V. Rakitina, Valery Kh. Akparov, Vladimir I. Timofeev, Inna P. Kuranova, Galina E. Konstantinova, Ilyas G. Khaliullin

Publikováno v: PLoS ONE, Vol 14, Iss 12, p e0226636 (2019)
PLoS ONE

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecd5491a25a782964a1cd34fba666295
https://doi.org/10.1371/journal.pone.0226636

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Kinetics of the thermal inactivation and the refolding of bacterial luciferases in Bacillus subtilis and in Escherichia coli differ

Autor: Ilya V. Manukhov, Ancha Baranova, Vera Schukina, Ilyas G. Khaliullin, Eugeny Gnuchikh, Gennady Zavilgelsky

Publikováno v: PLoS ONE, Vol 14, Iss 12, p e0226576 (2019)
PLoS ONE

Here we present a study of the thermal inactivation and the refolding of the proteins in Gram positive Bacillus subtilis. To enable use of bacterial luciferases as the models for protein thermal inactivation and refolding in B. subtilis cells, we dev

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e9ce69d1fd3259f6bdd4b4c71ce8fb8
https://doi.org/10.1371/journal.pone.0226576

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Molecular modeling of different substrate-binding modes and their role in penicillin acylase catalysis

Autor: Oleg V. Stroganov, Ilyas G. Khaliullin, Ghermes G. Chilov, Irina V. Shapovalova, Vytas K. Švedas, Nikolay V. Panin, Fedor N. Novikov

Publikováno v: The FEBS journal. 280(1)

Molecular modeling was addressed to understand different substrate-binding modes and clarify the role of two positively charged residues of the penicillin G acylase active site - βR263 and αR145 - in binding of negatively charged substrates. Althou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f9b2650e4a6c5342315892ed3e9b6e5
https://pubmed.ncbi.nlm.nih.gov/23121694

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