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Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum
Prokaryotic α–carbonic anhydrases (α-CA) are metalloenzymes that catalyze the reversible hydration of CO(2) to bicarbonate and proton. We had reported the first crystal structure of a pyschrohalophilic α–CA from a deep-sea bacterium, Photobacterium profundum SS9. In this manuscript, we report the fi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
AIMS Press
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10462458/ https://www.ncbi.nlm.nih.gov/pubmed/37649802 http://dx.doi.org/10.3934/microbiol.2023028 |
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author | Somalinga, Vijayakumar Foss, Emily Grunden, Amy M. |
author_facet | Somalinga, Vijayakumar Foss, Emily Grunden, Amy M. |
author_sort | Somalinga, Vijayakumar |
collection | PubMed |
description | Prokaryotic α–carbonic anhydrases (α-CA) are metalloenzymes that catalyze the reversible hydration of CO(2) to bicarbonate and proton. We had reported the first crystal structure of a pyschrohalophilic α–CA from a deep-sea bacterium, Photobacterium profundum SS9. In this manuscript, we report the first biochemical characterization of P. profundum α–CA (PprCA) which revealed several catalytic properties that are atypical for this class of CA's. Purified PprCA exhibited maximal catalytic activity at psychrophilic temperatures with substantial decrease in activity at mesophilic and thermophilic range. Similar to other α–CA's, Ppr9A showed peak activity at alkaline pH (pH 11), although, PprCA retained 88% of its activity even at acidic pH (pH 5). Exposing PprCA to varying concentrations of oxidizing and reducing agents revealed that N-terminal cysteine residues in PprCA may play a role in the structural stability of the enzyme. Although inefficient in CO(2) hydration activity under mesophilic and thermophilic temperatures, PprCA exhibited salt-dependent thermotolerance and catalytic activity under extreme halophilic conditions. Similar to other well-characterized α–CA's, PprCA is also inhibited by monovalent anions even at low concentrations. Finally, we demonstrate that PprCA accelerates CO(2) biomineralization to calcium carbonate under alkaline conditions. |
format | Online Article Text |
id | pubmed-10462458 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | AIMS Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-104624582023-08-30 Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum Somalinga, Vijayakumar Foss, Emily Grunden, Amy M. AIMS Microbiol Research Article Prokaryotic α–carbonic anhydrases (α-CA) are metalloenzymes that catalyze the reversible hydration of CO(2) to bicarbonate and proton. We had reported the first crystal structure of a pyschrohalophilic α–CA from a deep-sea bacterium, Photobacterium profundum SS9. In this manuscript, we report the first biochemical characterization of P. profundum α–CA (PprCA) which revealed several catalytic properties that are atypical for this class of CA's. Purified PprCA exhibited maximal catalytic activity at psychrophilic temperatures with substantial decrease in activity at mesophilic and thermophilic range. Similar to other α–CA's, Ppr9A showed peak activity at alkaline pH (pH 11), although, PprCA retained 88% of its activity even at acidic pH (pH 5). Exposing PprCA to varying concentrations of oxidizing and reducing agents revealed that N-terminal cysteine residues in PprCA may play a role in the structural stability of the enzyme. Although inefficient in CO(2) hydration activity under mesophilic and thermophilic temperatures, PprCA exhibited salt-dependent thermotolerance and catalytic activity under extreme halophilic conditions. Similar to other well-characterized α–CA's, PprCA is also inhibited by monovalent anions even at low concentrations. Finally, we demonstrate that PprCA accelerates CO(2) biomineralization to calcium carbonate under alkaline conditions. AIMS Press 2023-06-19 /pmc/articles/PMC10462458/ /pubmed/37649802 http://dx.doi.org/10.3934/microbiol.2023028 Text en © 2023 the Author(s), licensee AIMS Press https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0 (https://creativecommons.org/licenses/by/4.0/) ) |
spellingShingle | Research Article Somalinga, Vijayakumar Foss, Emily Grunden, Amy M. Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum |
title | Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum |
title_full | Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum |
title_fullStr | Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum |
title_full_unstemmed | Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum |
title_short | Biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, Photobacterium profundum |
title_sort | biochemical characterization of a psychrophilic and halotolerant α–carbonic anhydrase from a deep-sea bacterium, photobacterium profundum |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10462458/ https://www.ncbi.nlm.nih.gov/pubmed/37649802 http://dx.doi.org/10.3934/microbiol.2023028 |
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