Sulfhydryl oxidases

Sources, properties, production and applications

Greta Faccio (Corresponding Author), Outi Nivala, Kristiina Kruus, Johanna Buchert, Markku Saloheimo

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)

Abstract

The formation of disulfide bonds in proteins and small molecules can greatly affect their functionality. Sulfhydryl oxidases (SOXs) are enzymes capable of oxidising the free sulfhydryl groups in proteins and thiol-containing small molecules by using molecular oxygen as an electron acceptor. SOXs have been isolated from the intracellular compartments of many organisms, but also secreted SOXs are known. These latter enzymes are generally active on small compounds and their physiological role is unknown, whereas the intracellular enzymes prefer proteins as substrates and are involved in protein folding. An increasing number of scientific publications and patent applications on SOXs have been published in recent years. The present mini-review provides an up-to-date summary of SOXs from various families, their production and their actual or suggested applications. The sequence features and domain organisation of the characterised SOXs are reviewed, and special attention is paid to the physicochemical features of the enzymes. A review of patents and patent applications regarding this class of enzymes is also provided.
Original languageEnglish
Pages (from-to)957-966
Number of pages10
JournalApplied Microbiology and Biotechnology
Volume91
Issue number4
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

Fingerprint

Enzymes
Proteins
Patents
Protein Folding
Sulfhydryl Compounds
Disulfides
Publications
sulfhydryl oxidase
Electrons
Oxygen

Keywords

  • Application
  • disulfide bond
  • glutathione
  • sulfhydryl oxidase
  • thiol oxidase

Cite this

@article{392a1af4d51948d89231a49798386590,
title = "Sulfhydryl oxidases: Sources, properties, production and applications",
abstract = "The formation of disulfide bonds in proteins and small molecules can greatly affect their functionality. Sulfhydryl oxidases (SOXs) are enzymes capable of oxidising the free sulfhydryl groups in proteins and thiol-containing small molecules by using molecular oxygen as an electron acceptor. SOXs have been isolated from the intracellular compartments of many organisms, but also secreted SOXs are known. These latter enzymes are generally active on small compounds and their physiological role is unknown, whereas the intracellular enzymes prefer proteins as substrates and are involved in protein folding. An increasing number of scientific publications and patent applications on SOXs have been published in recent years. The present mini-review provides an up-to-date summary of SOXs from various families, their production and their actual or suggested applications. The sequence features and domain organisation of the characterised SOXs are reviewed, and special attention is paid to the physicochemical features of the enzymes. A review of patents and patent applications regarding this class of enzymes is also provided.",
keywords = "Application, disulfide bond, glutathione, sulfhydryl oxidase, thiol oxidase",
author = "Greta Faccio and Outi Nivala and Kristiina Kruus and Johanna Buchert and Markku Saloheimo",
year = "2011",
doi = "10.1007/s00253-011-3440-y",
language = "English",
volume = "91",
pages = "957--966",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "Springer",
number = "4",

}

Sulfhydryl oxidases : Sources, properties, production and applications. / Faccio, Greta (Corresponding Author); Nivala, Outi; Kruus, Kristiina; Buchert, Johanna; Saloheimo, Markku.

In: Applied Microbiology and Biotechnology, Vol. 91, No. 4, 2011, p. 957-966.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Sulfhydryl oxidases

T2 - Sources, properties, production and applications

AU - Faccio, Greta

AU - Nivala, Outi

AU - Kruus, Kristiina

AU - Buchert, Johanna

AU - Saloheimo, Markku

PY - 2011

Y1 - 2011

N2 - The formation of disulfide bonds in proteins and small molecules can greatly affect their functionality. Sulfhydryl oxidases (SOXs) are enzymes capable of oxidising the free sulfhydryl groups in proteins and thiol-containing small molecules by using molecular oxygen as an electron acceptor. SOXs have been isolated from the intracellular compartments of many organisms, but also secreted SOXs are known. These latter enzymes are generally active on small compounds and their physiological role is unknown, whereas the intracellular enzymes prefer proteins as substrates and are involved in protein folding. An increasing number of scientific publications and patent applications on SOXs have been published in recent years. The present mini-review provides an up-to-date summary of SOXs from various families, their production and their actual or suggested applications. The sequence features and domain organisation of the characterised SOXs are reviewed, and special attention is paid to the physicochemical features of the enzymes. A review of patents and patent applications regarding this class of enzymes is also provided.

AB - The formation of disulfide bonds in proteins and small molecules can greatly affect their functionality. Sulfhydryl oxidases (SOXs) are enzymes capable of oxidising the free sulfhydryl groups in proteins and thiol-containing small molecules by using molecular oxygen as an electron acceptor. SOXs have been isolated from the intracellular compartments of many organisms, but also secreted SOXs are known. These latter enzymes are generally active on small compounds and their physiological role is unknown, whereas the intracellular enzymes prefer proteins as substrates and are involved in protein folding. An increasing number of scientific publications and patent applications on SOXs have been published in recent years. The present mini-review provides an up-to-date summary of SOXs from various families, their production and their actual or suggested applications. The sequence features and domain organisation of the characterised SOXs are reviewed, and special attention is paid to the physicochemical features of the enzymes. A review of patents and patent applications regarding this class of enzymes is also provided.

KW - Application

KW - disulfide bond

KW - glutathione

KW - sulfhydryl oxidase

KW - thiol oxidase

U2 - 10.1007/s00253-011-3440-y

DO - 10.1007/s00253-011-3440-y

M3 - Article

VL - 91

SP - 957

EP - 966

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 4

ER -