Data from: Characterisation of a cold-adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS-131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation Article Swipe
Yato Akane
,
Kato Yuki
,
Hayashi, Fuyuko
,
Asaka Rio
,
Ogawa Atsuko
,
Oda, Tokuro
,
Tsuji Sayaka
,
Unno Masashi
,
Soh Nobuaki
,
Watanabe Keiichi
,
Horitani Masaki
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.5281/zenodo.14719404
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.5281/zenodo.14719404
Microorganisms living in cold environments such as the Antarctic and deep sea usually possess cold-adapted enzymes, which are known to have high catalytic efficiency and low stability owing to their flexible structures. Research on cold-adapted enzymes has not progressed much due to the challenge of these enzymes being less stable. However, several cold-adapted enzymes with high thermal stability have recently been reported. In this study, we investigated the biochemical properties of glucokinases from the psychrophilic Pseudoalteromonas sp. AS-131 (PsGK) isolated from the Antarctic Ocean and mesophilic Escherichia coli (EcGK). We demonstrated that PsGK is a cold-adapted enzyme with high thermal stability. A comparison of the crystal structures and spectroscopic studies revealed that PsGK has an additional disulfide bond connecting the N- and C-termini. To test whether this bond is important for stability, we prepared a PsGK variant by removing the bond and observed a significant reduction in thermal stability. In addition, the introduction of the artificial disulfide bonds in homologous positions in EcGK increased the thermal stability without the reduction of maximum activity. These results confirmed that the introduction of a disulfide bond at the proper position, such as the connection of the N- and C-termini, significantly improved stability without changing the nature of enzymes. Our findings propose a new strategy that will contribute to the industrial application of enzymes.
Related Topics
Concepts
Psychrophile
Thermal stability
Mesophile
Enzyme
Chemistry
Biochemistry
Catalytic efficiency
Escherichia coli
Thermostability
Extremophile
Hydrolase
Thermophile
Pseudoalteromonas
Candida antarctica
Disulfide bond
Crystallography
Biology
Peptide bond
Biophysics
Adaptation (eye)
Hyperthermophile
Catalysis
Stereochemistry
Protein structure
Thermal
Metadata
- Type
- other
- Landing Page
- https://doi.org/10.5281/zenodo.14719404
- OA Status
- green
- OpenAlex ID
- https://openalex.org/W7109167769
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W7109167769Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.5281/zenodo.14719404Digital Object Identifier
- Title
-
Data from: Characterisation of a cold-adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS-131 reveals how the enzyme achieves high thermal stability without loss of cold adaptationWork title
- Type
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otherOpenAlex work type
- Publication year
-
2025Year of publication
- Publication date
-
2025-12-05Full publication date if available
- Authors
-
Yato Akane, Kato Yuki, Hayashi, Fuyuko, Asaka Rio, Ogawa Atsuko, Oda, Tokuro, Tsuji Sayaka, Unno Masashi, Soh Nobuaki, Watanabe Keiichi, Horitani MasakiList of authors in order
- Landing page
-
https://doi.org/10.5281/zenodo.14719404Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
-
https://doi.org/10.5281/zenodo.14719404Direct OA link when available
- Concepts
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Psychrophile, Thermal stability, Mesophile, Enzyme, Chemistry, Biochemistry, Catalytic efficiency, Escherichia coli, Thermostability, Extremophile, Hydrolase, Thermophile, Pseudoalteromonas, Candida antarctica, Disulfide bond, Crystallography, Biology, Peptide bond, Biophysics, Adaptation (eye), Hyperthermophile, Catalysis, Stereochemistry, Protein structure, ThermalTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
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