Výsledky vyhledávání - "K. A. Novototskaya-Vlasova"

Effect of Cysteine Residue Substitution in the GCSAG Motif of the PMGL2 Esterase Active Site on the Enzyme Properties

Autor: D. A. Dolgikh, Alena Yu. Nikolaeva, Konstantin M. Boyko, E. A. Kryukova, S. A. Yakimov, K. A. Novototskaya-Vlasova, Mikhail P. Kirpichnikov, Lada E. Petrovskaya, M.V. Kryukova

Publikováno v: Biochemistry (Moscow). 85:709-716

The gene coding for PMGL2 esterase, which belongs to the family of mammalian hormone-sensitive lipases (HSLs), was discovered by screening a metagenomic DNA library from a permafrost soil. The active site of PMGL2 contains conserved GXSXG motif which

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e722b197ba65b79eb1131791231db7fd
https://doi.org/10.1134/s0006297920060085

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Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure

Autor: Konstantin M. Boyko, Alena Yu. Nikolaeva, D. A. Korzhenevsky, K. A. Novototskaya-Vlasova, Dmitry A. Dolgikh, G.Y. Lomakina, Elizaveta Rivkina, Lada E. Petrovskaya, Vladimir Popov, M.V. Kryukova, Mikhail P. Kirpichnikov, E. A. Kryukova

Publikováno v: Biomolecules, Vol 11, Iss 57, p 57 (2021)
Biomolecules
Volume 11
Issue 1
'Biomolecules ', vol: 11, pages: 57-1-57-18 (2021)

The gene coding for a novel cold-active esterase PMGL3 was previously obtained from a Siberian permafrost metagenomic DNA library and expressed in Escherichia coli. We elucidated the 3D structure of the enzyme which belongs to the hormone-sensitive l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::682b7534240095f9791e4d2d81a1910c
https://www.mdpi.com/2218-273X/11/1/57

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Crystal structure of PMGL2 esterase from the hormone-sensitive lipase family with GCSAG motif around the catalytic serine

Autor: Marya V. Kryukova, D. A. Korzhenevsky, Dmitry A. Dolgikh, Konstantin M. Boyko, Vladimir Popov, Mikhail P. Kirpichnikov, Lada E. Petrovskaya, Alena Yu. Nikolaeva, Elizaveta Rivkina, K. A. Novototskaya-Vlasova

Publikováno v: PLoS ONE
PLoS ONE, Vol 15, Iss 1, p e0226838 (2020)

Lipases comprise a large class of hydrolytic enzymes which catalyze the cleavage of the ester bonds in triacylglycerols and find numerous biotechnological applications. Previously, we have cloned the gene coding for a novel esterase PMGL2 from a Sibe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::866a993cc92d598295835ff7c973bea3
https://pubmed.ncbi.nlm.nih.gov/31990908

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Fusion with the cold-active esterase facilitates autotransporter-based surface display of the 10th human fibronectin domain in Escherichia coli

Autor: S. Sh. Gapizov, K. A. Novototskaya-Vlasova, Elizaveta Rivkina, A. V. Zlobinov, Dmitry A. Dolgikh, Mikhail P. Kirpichnikov, Shingarova Ln, E. F. Boldyreva, Lada E. Petrovskaya

Publikováno v: Extremophiles : life under extreme conditions. 22(1)

Cell surface display is a popular approach for the construction of whole-cell biocatalysts, live vaccines, and screening of combinatorial libraries. To develop a novel surface display system for the popular scaffold protein 10th human fibronectin typ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa382d74201c0e7bcb3688c1deb65f3f
https://pubmed.ncbi.nlm.nih.gov/29256084

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Cell surface display of cold-active esterase EstPc with the use of a new autotransporter from Psychrobacter cryohalolentis K5T

Autor: Lada E. Petrovskaya, K. A. Novototskaya-Vlasova, D. A. Dolgikh, E. A. Kryukova, Mikhail P. Kirpichnikov, Elizaveta Rivkina

Publikováno v: Extremophiles. 19:161-170

We have cloned the gene coding for AT877-a new predicted member of the autotransporter protein family with an esterase passenger domain from permafrost bacterium Psychrobacter cryohalolentis K5(T). Expression of AT877 gene in Escherichia coli resulte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::193ec86851db6f18ed3f72982c1646bd
https://doi.org/10.1007/s00792-014-0695-0

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Expression and chaperone-assisted refolding of a new cold-active lipase from Psychrobacter cryohalolentis K5T

Autor: Lada E. Petrovskaya, K. A. Novototskaya-Vlasova, Mikhail P. Kirpichnikov, Elena V. Kryukova, Elizaveta Rivkina, Dmitry A. Dolgikh

Publikováno v: Protein Expression and Purification. 91:96-103

We describe cloning and expression of genes coding for lipase Lip2Pc and lipase-specific foldase LifPc from a psychrotrophic microorganism Psychrobacter cryohalolentis K5(T) isolated from a Siberian cryopeg (the lense of overcooled brine within perma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59600e0c279cd7f1097753b58c45f21e
https://doi.org/10.1016/j.pep.2013.07.011

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Expression and characterization of a new esterase with GCSAG motif from a permafrost metagenomic library

Autor: Evgeny N. Nikolaev, E. V. Spirina, K. A. Novototskaya-Vlasova, Elizaveta Rivkina, Maria G. Zavialova, Ekaterina V. Durdenko, Lada E. Petrovskaya, G.Y. Lomakina

Publikováno v: FEMS microbiology ecology. 92(5)

As a result of construction and screening of a metagenomic library prepared from a permafrost-derived microcosm, we have isolated a novel gene coding for a putative lipolytic enzyme that belongs to the hormone-sensitive lipase family. It encodes a po

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daca698cca1f1fcc114d083b22fcd34e
https://pubmed.ncbi.nlm.nih.gov/26929439

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Cloning, purification, and characterization of a cold-adapted esterase produced byPsychrobacter cryohalolentisK5Tfrom Siberian cryopeg

Autor: S.A. Yakimov, David Gilichinsky, K. A. Novototskaya-Vlasova, Lada E. Petrovskaya

Publikováno v: FEMS Microbiology Ecology. 82:367-375

A psychrotrophic gram-negative bacterium Psychrobacter cryohalolentis K5(T) was previously isolated from a cryopeg within Siberian permafrost and its genome has been completely sequenced. To clone and characterize potential cold-active lipases/estera

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5acdf0142e0cc5a6d18b305934ffaf8e
https://doi.org/10.1111/j.1574-6941.2012.01385.x

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Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter

Autor: Marina S. Drutskaya, Andrey P. Anisimov, Andrey Kruglov, Dmitry V. Kuprash, K. A. Novototskaya-Vlasova, Anna N. Kondakova, Elizaveta Rivkina, Kirill V. Korneev, Nikolay P. Arbatsky, Yu. A. Knirel, Sergei A. Nedospasov

Publikováno v: Biochemistry. Biokhimiia. 79(12)

Correlation between the chemical structure of lipid A from various Gram-negative bacteria and biological activity of their lipopolysaccharide (LPS) as an agonist of the innate immune receptor Toll-like receptor 4 was investigated. Purified LPS specie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd09fec0afcdd9f6b1bc4a3fdb94b365
https://pubmed.ncbi.nlm.nih.gov/25716726

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Characterization of a cold-active lipase from Psychrobacter cryohalolentis K5(T) and its deletion mutants

Autor: Lada E. Petrovskaya, K. A. Novototskaya-Vlasova, D. A. Dolgikh, Elizaveta Rivkina, Mikhail P. Kirpichnikov

Publikováno v: Biochemistry. Biokhimiia. 78(4)

A gene coding for cold-active lipase from the psychrotrophic Gram-negative bacterium Psychrobacter cryohalolentis K5(T) isolated from a Siberian cryopeg has been cloned and expressed in Escherichia coli. The recombinant protein Lip1Pc with a 6× hist

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a39a7bffbb2c32800449552e1460591
https://pubmed.ncbi.nlm.nih.gov/23590441

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