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dc.contributor.author
Yakushi, Toshiharu
dc.contributor.author
Takahashi, Ryota
dc.contributor.author
Matsutani, Minenosuke
dc.contributor.author
Kataoka, Naoya
dc.contributor.author
Hours, Roque Alberto
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dc.contributor.author
Ano, Yoshitaka
dc.contributor.author
Adachi, Osao
dc.contributor.author
Matsushita, Kazunobu
dc.date.available
2021-10-12T16:54:25Z
dc.date.issued
2020-06
dc.identifier.citation
Yakushi, Toshiharu; Takahashi, Ryota; Matsutani, Minenosuke; Kataoka, Naoya; Hours, Roque Alberto; et al.; The membrane-bound sorbosone dehydrogenase of Gluconacetobacter liquefaciens is a pyrroloquinoline quinone-dependent enzyme; Elsevier Science Inc.; Enzyme and Microbial Technology; 137; 6-2020; 1-10
dc.identifier.issn
0141-0229
dc.identifier.uri
http://hdl.handle.net/11336/143291
dc.description.abstract
Membrane-bound sorbosone dehydrogenase (SNDH) of Gluconacetobacter liquefaciens oxidizes L-sorbosone to 2-keto-L-gulonic acid (2KGLA), a key intermediate in vitamin C production. We constructed recombinant Escherichia coli and Gluconobacter strains harboring plasmids carrying the sndh gene from Ga. liquefaciens strain RCTMR10 to identify the prosthetic group of SNDH. The membranes of the recombinant E. coli showed L-sorbosone oxidation activity, only after the holo-enzyme formation with pyrroloquinoline quinone (PQQ), indicating that SNDH is a PQQ-dependent enzyme. The sorbosone-oxidizing respiratory chain was thus heterologously reconstituted in the E. coli membranes. The membranes that contained SNDH showed the activity of sorbosone:ubiquinone analogue oxidoreductase. These results suggest that the natural electron acceptor for SNDH is membranous ubiquinone, and it functions as the primary dehydrogenase in the sorbosone oxidation respiratory chain in Ga. liquefaciens. A biotransformation experiment showed L-sorbosone oxidation to 2KGLA in a nearly quantitative manner. Phylogenetic analysis for prokaryotic SNDH homologues revealed that they are found only in the Proteobacteria phylum and those of the Acetobacteraceae family are clustered in a group where all members possess a transmembrane segment. A three-dimensional structure model of the SNDH constructed with an in silico fold recognition method was similar to the crystal structure of the PQQ-dependent pyranose dehydrogenase from Coprinopsis cinerea. The structural similarity suggests a reaction mechanism under which PQQ participates in L-sorbosone oxidation.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc.
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dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
2-KETO-L-GULONIC ACID
dc.subject
ACETIC ACID BACTERIA
dc.subject
GLUCONACETOBACTER
dc.subject
L-SORBOSONE
dc.subject
PYRROLOQUINOLINE QUINONE
dc.subject
SORBOSONE DEHYDROGENASE
dc.subject.classification
Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
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dc.subject.classification
Biotecnología Industrial
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dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
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dc.title
The membrane-bound sorbosone dehydrogenase of Gluconacetobacter liquefaciens is a pyrroloquinoline quinone-dependent enzyme
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-09-06T17:13:51Z
dc.journal.volume
137
dc.journal.pagination
1-10
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Yakushi, Toshiharu. Yamaguchi University; Japón
dc.description.fil
Fil: Takahashi, Ryota. Yamaguchi University; Japón
dc.description.fil
Fil: Matsutani, Minenosuke. Yamaguchi University; Japón
dc.description.fil
Fil: Kataoka, Naoya. Yamaguchi University; Japón
dc.description.fil
Fil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
dc.description.fil
Fil: Ano, Yoshitaka. Ehime University; Japón
dc.description.fil
Fil: Adachi, Osao. Yamaguchi University; Japón
dc.description.fil
Fil: Matsushita, Kazunobu. Yamaguchi University; Japón
dc.journal.title
Enzyme and Microbial Technology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.enzmictec.2020.109511
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022920300041?via%3Dihub
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