Characterization of sulfhydryl oxidase from Aspergillus tubingensis

 |  Login

Show simple item record

dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en Nivala, Outi Faccio, Greta Arvas, Mikko Permi, Perttu Buchert, Johanna Kruus, Kristiina Mattinen, Maija Liisa 2018-02-09T10:07:22Z 2018-02-09T10:07:22Z 2017-12-08
dc.identifier.citation Nivala , O , Faccio , G , Arvas , M , Permi , P , Buchert , J , Kruus , K & Mattinen , M L 2017 , ' Characterization of sulfhydryl oxidase from Aspergillus tubingensis ' BMC Biochemistry , vol 18 , no. 1 , 15 . DOI: 10.1186/s12858-017-0090-4 en
dc.identifier.issn 1471-2091
dc.identifier.other PURE UUID: e31477bc-926d-4db2-9261-bbc5117f4fcf
dc.identifier.other PURE ITEMURL:
dc.identifier.other PURE LINK:
dc.identifier.other PURE FILEURL:
dc.description.abstract CONCLUSIONS: AtSOX (55 kDa) is a fungal secreted flavin-dependent enzyme with good stability to both pH and temperature. A Michaelis-Menten behaviour was observed with reduced glutathione as a substrate. Based on the location of SOX enzyme encoding genes close to NRPSs, SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides. BACKGROUND: Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. RESULTS: The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initial activity was retained after incubation at 50 °C for 20 h. AtSOX contains a non-covalently bound flavin cofactor. The enzyme oxidised a sulfhydryl group of glutathione to form a disulfide bond, as verified by nuclear magnetic resonance spectroscopy. AtSOX preferred glutathione as a substrate over cysteine and dithiothreitol. The activity of the enzyme was totally inhibited by 10 mM zinc sulphate. Peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, were not oxidised by the enzyme. Based on the analysis of 33 fungal genomes, SOX enzyme encoding genes were found close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, AtSOX was evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin, namely GliT, HlmI and DepH, were also evolutionary closely related to AtSOX whereas fungal thioreductases were more distant. en
dc.format.extent 1
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries BMC Biochemistry en
dc.relation.ispartofseries Volume 18, issue 1 en
dc.rights openAccess en
dc.subject.other Biochemistry en
dc.subject.other Molecular Biology en
dc.subject.other 1182 Biochemistry, cell and molecular biology en
dc.title Characterization of sulfhydryl oxidase from Aspergillus tubingensis en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department VTT Technical Research Centre of Finland
dc.contributor.department University of Jyväskylä
dc.contributor.department Luke Natural Resources Institute Finland
dc.contributor.department Department of Bioproducts and Biosystems
dc.subject.keyword Aspergillus tubingensis
dc.subject.keyword Dithiol oxidase
dc.subject.keyword Glutathione oxidation
dc.subject.keyword Nonribosomal peptide synthesis
dc.subject.keyword Secondary metabolism
dc.subject.keyword Secreted sulfhydryl oxidase
dc.subject.keyword Biochemistry
dc.subject.keyword Molecular Biology
dc.subject.keyword 1182 Biochemistry, cell and molecular biology
dc.identifier.urn URN:NBN:fi:aalto-201802091510
dc.identifier.doi 10.1186/s12858-017-0090-4
dc.type.version publishedVersion

Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record

Search archive

Advanced Search

article-iconSubmit a publication


My Account