COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY
Properties of thermostable lipases from Geobacillus bacteria are considered. The enzymes are divided into groups with regard to their thermostability. Coordinated amino acid substitutions are demonstrated in the highly thermostable group (half-inactivation time > 1000 min); V198A, Q203E, V204...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders
2015-01-01
|
| Series: | Вавиловский журнал генетики и селекции |
| Subjects: | |
| Online Access: | https://vavilov.elpub.ru/jour/article/view/191 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832575340372819968 |
|---|---|
| author | K. N. Sorokina M. A. Nuriddinov A. S. Rozanov V. A. Ivanisenko S. E. Peltek |
| author_facet | K. N. Sorokina M. A. Nuriddinov A. S. Rozanov V. A. Ivanisenko S. E. Peltek |
| author_sort | K. N. Sorokina |
| collection | DOAJ |
| description | Properties of thermostable lipases from Geobacillus bacteria are considered. The enzymes are divided into groups with regard to their thermostability. Coordinated amino acid substitutions are demonstrated in the highly thermostable group (half-inactivation time > 1000 min); V198A, Q203E, V204I, Q217E; and V294I, P306A, T307A, D312S, R313H, E316G, V324I, S334N, A343T. The hydrophilic moment of α helices, correlating with the charge and polarity of amino acid in the region, exerts the most significant influence on enzyme thermostability. Most thermostable lipases are characterized by structural stabilization of the lid domain in the 198А-217Е region. |
| format | Article |
| id | doaj-art-fae6b8285227469ba24d05e01605423a |
| institution | Kabale University |
| issn | 2500-3259 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders |
| record_format | Article |
| series | Вавиловский журнал генетики и селекции |
| spelling | doaj-art-fae6b8285227469ba24d05e01605423a2025-02-01T09:58:00ZengSiberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and BreedersВавиловский журнал генетики и селекции2500-32592015-01-01174/1666674175COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITYK. N. Sorokina0M. A. Nuriddinov1A. S. Rozanov2V. A. Ivanisenko3S. E. Peltek4Institute of Cytology and Genetics SB RAS, Novosibirsk, RussiaInstitute of Cytology and Genetics SB RAS, Novosibirsk, RussiaInstitute of Cytology and Genetics SB RAS, Novosibirsk, RussiaInstitute of Cytology and Genetics SB RAS, Novosibirsk, RussiaInstitute of Cytology and Genetics SB RAS, Novosibirsk, RussiaProperties of thermostable lipases from Geobacillus bacteria are considered. The enzymes are divided into groups with regard to their thermostability. Coordinated amino acid substitutions are demonstrated in the highly thermostable group (half-inactivation time > 1000 min); V198A, Q203E, V204I, Q217E; and V294I, P306A, T307A, D312S, R313H, E316G, V324I, S334N, A343T. The hydrophilic moment of α helices, correlating with the charge and polarity of amino acid in the region, exerts the most significant influence on enzyme thermostability. Most thermostable lipases are characterized by structural stabilization of the lid domain in the 198А-217Е region.https://vavilov.elpub.ru/jour/article/view/191bioinformaticslipasesthermostability |
| spellingShingle | K. N. Sorokina M. A. Nuriddinov A. S. Rozanov V. A. Ivanisenko S. E. Peltek COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY Вавиловский журнал генетики и селекции bioinformatics lipases thermostability |
| title | COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY |
| title_full | COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY |
| title_fullStr | COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY |
| title_full_unstemmed | COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY |
| title_short | COMPUTER ANALYSIS OF THE STRUCTURES OF LIPASES FROM Geobacillus BACTERIA AND IDENTIFICATION OF MOTIFS DETERMINING THEIR THERMOSTABILITY |
| title_sort | computer analysis of the structures of lipases from geobacillus bacteria and identification of motifs determining their thermostability |
| topic | bioinformatics lipases thermostability |
| url | https://vavilov.elpub.ru/jour/article/view/191 |
| work_keys_str_mv | AT knsorokina computeranalysisofthestructuresoflipasesfromgeobacillusbacteriaandidentificationofmotifsdeterminingtheirthermostability AT manuriddinov computeranalysisofthestructuresoflipasesfromgeobacillusbacteriaandidentificationofmotifsdeterminingtheirthermostability AT asrozanov computeranalysisofthestructuresoflipasesfromgeobacillusbacteriaandidentificationofmotifsdeterminingtheirthermostability AT vaivanisenko computeranalysisofthestructuresoflipasesfromgeobacillusbacteriaandidentificationofmotifsdeterminingtheirthermostability AT sepeltek computeranalysisofthestructuresoflipasesfromgeobacillusbacteriaandidentificationofmotifsdeterminingtheirthermostability |