Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands.
| Title: | Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands. |
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| Authors: | de Almeida Santos, Gustavo, Englund, Andrea N. B., Dalleywater, Eirin L., Røhr, Åsmund Kjendseth |
| Source: | FEBS Open Bio; Dec2024, Vol. 14 Issue 12, p2038-2058, 21p |
| Subject Terms: | COPPER proteins, HALOBACTERIUM, MANGROVE forests, PHENOLS, BIOMASS, MELANINS |
| Abstract: | Tyrosinases (TYRs) are type‐3 copper proteins that are widely distributed in nature. They can hydroxylate and oxidize phenolic molecules and are mostly known for producing melanins that confer protection against photo induced damage. TYRs are also thought to play an important role in the 'latch mechanism', where high concentrations of phenolic compounds inhibit oxidative decomposition of organic biomass and subsequent CO2 release, especially relevant in wetland environments. In the present study, we describe two TYRs, HcTyr1 and HcTyr2, from halophilic bacterium Hahella sp. CCB MM4 previously isolated at Matang mangrove forest in Perak, Malaysia. The structure of HcTyr1 was determined by X‐ray crystallography at a resolution of 1.9 Å and represents an uncharacterized group of prokaryotic TYRs as demonstrated by a sequence similarity network analysis. The genes encoding the enzymes were cloned, expressed, purified and thoroughly characterized by biochemical methods. HcTyr1 was able to self‐cleave its lid‐domain (LID) in a protease independent manner, whereas the LID of HcTyr2 was essential for activity and stability. Both enzymes showed variable activity in the presence of different metals, surfactants and NaCl, and were able to oxidize lignin constituents. The high salinity tolerance of HcTyr1 indicates that the enzyme can be an efficient catalyst in the habitat of the host. [ABSTRACT FROM AUTHOR] |
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| Items | – Name: Title Label: Title Group: Ti Data: Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22de+Almeida+Santos%2C+Gustavo%22">de Almeida Santos, Gustavo</searchLink><br /><searchLink fieldCode="AR" term="%22Englund%2C+Andrea+N%2E+B%2E%22">Englund, Andrea N. B.</searchLink><br /><searchLink fieldCode="AR" term="%22Dalleywater%2C+Eirin+L%2E%22">Dalleywater, Eirin L.</searchLink><br /><searchLink fieldCode="AR" term="%22Røhr%2C+Åsmund+Kjendseth%22">Røhr, Åsmund Kjendseth</searchLink> – Name: TitleSource Label: Source Group: Src Data: FEBS Open Bio; Dec2024, Vol. 14 Issue 12, p2038-2058, 21p – Name: Subject Label: Subject Terms Group: Su Data: <searchLink fieldCode="DE" term="%22COPPER+proteins%22">COPPER proteins</searchLink><br /><searchLink fieldCode="DE" term="%22HALOBACTERIUM%22">HALOBACTERIUM</searchLink><br /><searchLink fieldCode="DE" term="%22MANGROVE+forests%22">MANGROVE forests</searchLink><br /><searchLink fieldCode="DE" term="%22PHENOLS%22">PHENOLS</searchLink><br /><searchLink fieldCode="DE" term="%22BIOMASS%22">BIOMASS</searchLink><br /><searchLink fieldCode="DE" term="%22MELANINS%22">MELANINS</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Tyrosinases (TYRs) are type‐3 copper proteins that are widely distributed in nature. They can hydroxylate and oxidize phenolic molecules and are mostly known for producing melanins that confer protection against photo induced damage. TYRs are also thought to play an important role in the 'latch mechanism', where high concentrations of phenolic compounds inhibit oxidative decomposition of organic biomass and subsequent CO2 release, especially relevant in wetland environments. In the present study, we describe two TYRs, HcTyr1 and HcTyr2, from halophilic bacterium Hahella sp. CCB MM4 previously isolated at Matang mangrove forest in Perak, Malaysia. The structure of HcTyr1 was determined by X‐ray crystallography at a resolution of 1.9 Å and represents an uncharacterized group of prokaryotic TYRs as demonstrated by a sequence similarity network analysis. The genes encoding the enzymes were cloned, expressed, purified and thoroughly characterized by biochemical methods. HcTyr1 was able to self‐cleave its lid‐domain (LID) in a protease independent manner, whereas the LID of HcTyr2 was essential for activity and stability. Both enzymes showed variable activity in the presence of different metals, surfactants and NaCl, and were able to oxidize lignin constituents. The high salinity tolerance of HcTyr1 indicates that the enzyme can be an efficient catalyst in the habitat of the host. [ABSTRACT FROM AUTHOR] – Name: Abstract Label: Group: Ab Data: <i>Copyright of FEBS Open Bio is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1002/2211-5463.13906 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 21 StartPage: 2038 Subjects: – SubjectFull: COPPER proteins Type: general – SubjectFull: HALOBACTERIUM Type: general – SubjectFull: MANGROVE forests Type: general – SubjectFull: PHENOLS Type: general – SubjectFull: BIOMASS Type: general – SubjectFull: MELANINS Type: general Titles: – TitleFull: Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: de Almeida Santos, Gustavo – PersonEntity: Name: NameFull: Englund, Andrea N. B. – PersonEntity: Name: NameFull: Dalleywater, Eirin L. – PersonEntity: Name: NameFull: Røhr, Åsmund Kjendseth IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 12 Text: Dec2024 Type: published Y: 2024 Identifiers: – Type: issn-print Value: 22115463 Numbering: – Type: volume Value: 14 – Type: issue Value: 12 Titles: – TitleFull: FEBS Open Bio Type: main |
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