Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect
The evaluation of temperature effects on the structure and function of enzymes is necessary to understand the mechanisms underlying their adaptation to a constantly changing environment. In the current study, we investigated the influence of temperature variation on the activity, structural dynamics...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/15/8119 |
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| author | Anna A. Deeva Albert E. Lisitsa Lev A. Sukovatyi Tatiana N. Melnik Valentina A. Kratasyuk Elena V. Nemtseva |
| author_facet | Anna A. Deeva Albert E. Lisitsa Lev A. Sukovatyi Tatiana N. Melnik Valentina A. Kratasyuk Elena V. Nemtseva |
| author_sort | Anna A. Deeva |
| collection | DOAJ |
| description | The evaluation of temperature effects on the structure and function of enzymes is necessary to understand the mechanisms underlying their adaptation to a constantly changing environment. In the current study, we investigated the influence of temperature variation on the activity, structural dynamics, thermal inactivation and denaturation of <i>Photobacterium leiognathi</i> and <i>Vibrio harveyi</i> luciferases belonging to different subfamilies, as well as the role of sucrose in maintaining the enzymes functioning and stability. We used the stopped-flow technique, differential scanning calorimetry and molecular dynamics to study the activity, inactivation rate, denaturation and structural features of the enzymes under various temperatures. It was found that <i>P. leiognathi</i> luciferase resembles the properties of cold-adapted enzymes with high activity in a narrow temperature range and slightly lower thermal stability than <i>V. harveyi</i> luciferase, which is less active, but more thermostable. Differences in activity at the studied temperatures can be associated with the peculiarities of the mobile loop conformational changes. The presence of sucrose does not provide an advantage in activity but increases the stability of the enzymes. Differential scanning calorimetry experiments showed that luciferases probably follow different denaturation schemes. |
| first_indexed | 2024-03-09T10:08:35Z |
| format | Article |
| id | doaj.art-68f0a87e09a44df9865889089da56a84 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T10:08:35Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-68f0a87e09a44df9865889089da56a842023-12-01T22:56:50ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-07-012315811910.3390/ijms23158119Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is PerfectAnna A. Deeva0Albert E. Lisitsa1Lev A. Sukovatyi2Tatiana N. Melnik3Valentina A. Kratasyuk4Elena V. Nemtseva5Biophysics Department, Siberian Federal University, 660041 Krasnoyarsk, RussiaBiophysics Department, Siberian Federal University, 660041 Krasnoyarsk, RussiaBiophysics Department, Siberian Federal University, 660041 Krasnoyarsk, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaBiophysics Department, Siberian Federal University, 660041 Krasnoyarsk, RussiaBiophysics Department, Siberian Federal University, 660041 Krasnoyarsk, RussiaThe evaluation of temperature effects on the structure and function of enzymes is necessary to understand the mechanisms underlying their adaptation to a constantly changing environment. In the current study, we investigated the influence of temperature variation on the activity, structural dynamics, thermal inactivation and denaturation of <i>Photobacterium leiognathi</i> and <i>Vibrio harveyi</i> luciferases belonging to different subfamilies, as well as the role of sucrose in maintaining the enzymes functioning and stability. We used the stopped-flow technique, differential scanning calorimetry and molecular dynamics to study the activity, inactivation rate, denaturation and structural features of the enzymes under various temperatures. It was found that <i>P. leiognathi</i> luciferase resembles the properties of cold-adapted enzymes with high activity in a narrow temperature range and slightly lower thermal stability than <i>V. harveyi</i> luciferase, which is less active, but more thermostable. Differences in activity at the studied temperatures can be associated with the peculiarities of the mobile loop conformational changes. The presence of sucrose does not provide an advantage in activity but increases the stability of the enzymes. Differential scanning calorimetry experiments showed that luciferases probably follow different denaturation schemes.https://www.mdpi.com/1422-0067/23/15/8119bacterial luciferaseenzyme activityprotein stabilitysucrosethermal inactivationthermal denaturation |
| spellingShingle | Anna A. Deeva Albert E. Lisitsa Lev A. Sukovatyi Tatiana N. Melnik Valentina A. Kratasyuk Elena V. Nemtseva Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect International Journal of Molecular Sciences bacterial luciferase enzyme activity protein stability sucrose thermal inactivation thermal denaturation |
| title | Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect |
| title_full | Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect |
| title_fullStr | Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect |
| title_full_unstemmed | Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect |
| title_short | Structure-Function Relationships in Temperature Effects on Bacterial Luciferases: Nothing Is Perfect |
| title_sort | structure function relationships in temperature effects on bacterial luciferases nothing is perfect |
| topic | bacterial luciferase enzyme activity protein stability sucrose thermal inactivation thermal denaturation |
| url | https://www.mdpi.com/1422-0067/23/15/8119 |
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