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Citation for Study 21339

Citation title: "Characterization of sulfhydryl oxidase from Aspergillus tubingensis.".

Study name: "Characterization of sulfhydryl oxidase from Aspergillus tubingensis.".

This study is part of submission 21339 (Status: Published).

Citation

Nivala O., Faccio G., Arvas M., Permi P., Buchert J., Kruus K., & Mattinen M. 2017. Characterization of sulfhydryl oxidase from Aspergillus tubingensis. BMC Biochemistry, .

Authors

• Nivala O. (submitter)
• Faccio G.
• Arvas M.
• Permi P.
• Buchert J.
• Kruus K.
• Mattinen M.

Abstract

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 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. 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.

Keywords

Secreted sulfhydryl oxidase, dithiol oxidase, Aspergillus tubingensis, glutathione oxidation, nonribosomal peptide synthesis, secondary metabolism

External links

About this resource

• Canonical resource URI: http://purl.org/phylo/treebase/phylows/study/TB2:S21339
• Other versions: Nexus NeXML
• Show BibTeX reference

  		@ARTICLE{TreeBASE2Ref27465,
  	 author = {Outi  Nivala and Greta  Faccio and Mikko  Arvas and Perttu  Permi and Johanna  Buchert and Kristiina  Kruus and Maija-Liisa  Mattinen},
  	 title = {Characterization of sulfhydryl oxidase from Aspergillus tubingensis.},
  	 year = {2017},
  	 keywords = {Secreted sulfhydryl oxidase, dithiol oxidase, Aspergillus tubingensis, glutathione oxidation, nonribosomal peptide synthesis, secondary metabolism},
  	 doi = {},
  	 url = {http://},
  	 pmid = {},
  	 journal = {BMC Biochemistry},
  	 volume = {},
  	 number = {},
  	 pages = {},
  	 abstract = {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 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.
  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.}
  }
  		

• Show RIS reference

  		TY  - JOUR
  ID  - 27465
  AU  - Nivala,Outi 
  AU  - Faccio,Greta 
  AU  - Arvas,Mikko 
  AU  - Permi,Perttu 
  AU  - Buchert,Johanna 
  AU  - Kruus,Kristiina 
  AU  - Mattinen,Maija-Liisa 
  T1  - Characterization of sulfhydryl oxidase from Aspergillus tubingensis.
  PY  - 2017
  KW  - Secreted sulfhydryl oxidase
  KW  - dithiol oxidase
  KW  - Aspergillus tubingensis
  KW  - glutathione oxidation
  KW  - nonribosomal peptide synthesis
  KW  - secondary metabolism
  UR  - http://dx.doi.org/
  N2  - 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 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.
  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.
  L3  - 
  JF  - BMC Biochemistry
  VL  - 
  IS  - 
  ER  -