1.8.3.2: thiol oxidase
This is an abbreviated version!
For detailed information about thiol oxidase, go to the full flat file.
Word Map on EC 1.8.3.2
-
1.8.3.2
-
hepatocytes
-
intermembrane
-
oxidases
-
relay
-
qsoxs
-
thioredoxin
-
redox-active
-
hepatectomy
-
hepatotrophic
-
reoxidized
-
hepatectomized
-
flavoenzyme
-
fad-dependent
-
fad-binding
-
oxidoreductins
-
flavin-linked
-
redox-regulated
-
isoalloxazine
-
3h-tdr
-
diagnostics
-
medicine
-
nutrition
-
analysis
- 1.8.3.2
- hepatocytes
-
intermembrane
- oxidases
-
relay
-
qsoxs
- thioredoxin
-
redox-active
-
hepatectomy
-
hepatotrophic
-
reoxidized
-
hepatectomized
-
flavoenzyme
-
fad-dependent
-
fad-binding
-
oxidoreductins
-
flavin-linked
-
redox-regulated
- isoalloxazine
-
3h-tdr
- diagnostics
- medicine
- nutrition
- analysis
Reaction
2 R'C(R)SH
+
Synonyms
Ac92, AcMNPV P33, ALR, ALRp, AtSOX, augmenter of liver regeneration, DTT-oxidase, E10R, egg white oxidase, Ero1, Ero1p, ERV/ALR sulfhydryl oxidase, Erv1, Erv1p, Erv2, ERv2p, FAD-linked sulfhydryl oxidase, FAD-linked sulfhydryl oxidase ALR, FAD-sulfhydryl oxidase, flavin adenine dinucleotide-linked sulfhydryl oxidase, flavin-dependent sulfhydryl oxidase, GmQSOX1, GmQSOX2, hepatic regenerative stimulator substance, hepatopoietin, mitochondrial FAD-linked sulfhydryl oxidase ERV1, More, neuroblastoma-derived sulfhydryl oxidase, oxidase, thiol, P33, pB119L, protein pB119L, QSCN6, QSOX, QSOx1, QSOX1b, QSOX2, QSOX3, Quiescin Q6, quiescin Q6 sulfhydryl oxidase, quiescin Q6 sulfhydryl oxidase 1, quiescin Q6/sulfhydryl oxidase, quiescin sulfhydryl oxidase, quiescin sulfhydryl oxidase 1, quiescin sulhydryl oxidase, quiescin-like flavin-dependent sulfhydryl oxidase, Quiescin-sulfhydryl oxidase, quiescin/sulfhydryl oxidase, quiescin/sulfhydryl oxidase 1b, quiescin/sulphydryl oxidase, rQSOX, sfALR, SOX, Sox1, Sox2, SOXN, sulfhydryl oxidase, sulfhydryl oxidase SOx-3, sulfhydryl oxidase, P33, sulphydryl oxidase, thiol oxidase Erv1, thiooxidase
ECTree
1.8.3.2 thiol oxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.8.3.2 - thiol oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 R'C(R)SH + O2
R'C(R)S-S(R)CR' + H2O2
-
the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
cysteine + O2
cystine + H2O2
artificial in vitro substrate
-
-
ir
D-penicillamine + O2
? + H2O
-
33% of the activity with dithiothreitol
-
-
?
dithiothreitol + reduced cytochrome c
dithiothreitol disulfide + oxidized cytochrome c
-
cytochrome c is about 100fold more effective than O2 as reducing cosubstrate
-
-
?
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
-
-
-
-
?
protein A1aB1b + O2
protein A1aB1b disulfide + H2O2
-
precursor of the soybean seed storage protein glycinin, recombinantly expressed as His-tagged protein in Escherichia coli strain BL21(DE3). Recombinant GmQSOX1 catalyses disulfide-bond formation but is unable to refold the reduced and denatured precursor A1aB1b into a native form
-
-
?
protein SfP53 + O2
protein SfP53 disulfide + H2O2
-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
-
-
-
-
?
reduced thioredoxin + O2
thioredoxin disulfide + H2O2
-
-
-
r
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
-
-
-
-
?
thioglycolate + O2
? + H2O
-
11.1% of the activity with dithiothreitol
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
highest sulfhydryl oxidation activity using dithiothreitol as a substrate
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
Aspergillus tubingensis D-85248
-
the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol
-
-
?
2-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + O2
? + H2O
-
-
-
?
dithiothreitol + O2
? + H2O
-
anaerobically, the ferricenium ion is a facile alternative electron acceptor
production of H2O2
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
artificial in vitro substrate
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
r
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
intact enzyme and 60-kDa-enzyme fragment
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
the enzyme forms large amounts of neutral semiquinone, which arises between flavin centers within the dimer, during aerobic turnover with DTT
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
disulfide oxidase activity, reduction of flavin to a stable neutral semiquinone, further reduction can occur by addition of dithionite
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
Evr2p, not Evr1p
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
low concentrations of dithiothreitol stimulate the import efficiency of Erv1, whereas higher concentrations of dithiothreitol decrease it
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
best small thiol substrate
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
Evr2p, not Evr1p
-
-
?
GSH + O2 + O2
GSSG + H2O
-
13.5% of the activity with dithiothreitol
-
-
?
GSH + O2 + O2
GSSG + H2O
-
0.7% of the activity with dithiothreitol
-
?
N-acetylcysteine + O2
? + H2O
-
12.6% of the activity with dithiothreitol
-
-
?
N-acetylcysteine + O2
? + H2O
-
4.6% of the activity with dithiothreitol
-
-
?
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
-
i.e. PDI
-
-
ir
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
-
-
-
?
protein Mia40 + O2
protein Mia40 disulfide + H2O
-
recombinantly expressed substrate amino acids 284-403, which is the C-terminal domain of Mia40, electron transfer between the shuttle and active site disulfides of Erv1p. Both intersubunit and intermolecular electron transfer can occur, overview
-
-
?
R-SH + O2
R-S-S-R + H2O2
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a role in synaptic strengthening and in redox activities in the brain
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
best substrates are cysteine residues in reduced proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
disulfide bridge C15-C124 is not required for activity
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in secreted peptide/protein folding in the brain
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in the extracellular matrix as well as in intracellular folding of secreted proteins or hormons like LH and FSH, enzyme acts as an endogenous redox modulator of hormonal secretion, enzyme expression is regulated by estrogens
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
3 cysteine pairs are required for optimal enzyme function
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
reductively denatured pancreatic ribonuclease A
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
production of H2O2
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
intact enzyme, but not 60-kDa-enzyme fragment
-
-
ir
RNase A + O2
RNase A disulfide + H2O2
-
recombinant GmQSOX1 catalyses disulfide-bond formation but is unable to refold the reduced and denatured RNase A into a native form, cooperative refolding of unfolded RNase A by rGmQSOX1 and soybean PDI family proteins of group I and group II, overview. Most effective are GmPDIL-2 and GmPDIL-1 with rGmQSOX1
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
-
substrate from Escherichia coli
-
-
ir
additional information
?
-
no activity with glutathione, 2-mercaptoethanol, and di(2-mercaptoethanol)
-
-
?
additional information
?
-
-
peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme
-
-
-
additional information
?
-
Aspergillus tubingensis D-85248
-
peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme
-
-
-
additional information
?
-
-
enzyme does not catalyze thiol-disulfide interchange
-
-
?
additional information
?
-
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
?
additional information
?
-
-
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
?
additional information
?
-
-
the enzyme may play an important role in the introduction of disulfide bridges in egg white proteins
-
-
?
additional information
?
-
-
possible role for oxidase in protein secretory pathway
-
-
?
additional information
?
-
-
preferred substrates are protein or peptide sulfhydryl groups, even of denatured cytoplasmic proteins, low molecular weight thiols, such as cysteine or glutathione, are poorer substrates
-
-
?
additional information
?
-
-
a 30 kDa enzyme fragment shows no catalytic activity of its own
-
-
?
additional information
?
-
-
preferred substrates are protein or peptide sulfhydryl groups, but not low molecular weight thiols, such as cysteine or glutathione
-
-
?
additional information
?
-
-
recombinant GmQSOX1 expressed in Escherichia coli forms disulfide bonds on reduced and denatured RNase A, but does not show any refolding activity. The reduced and denatured RNase A is effectively refolded by recombinant GmQSOX1 in the presence of the soybean protein disulfide isomerase family protein GmPDIL-2 in the absence of glutathione redox buffer. Low activity withDTT, glutathione is a poor substrate
-
-
?
additional information
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
?
additional information
?
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme might communicate with the respiratory chain via the mediation of cytochrome c
-
-
?
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
?
additional information
?
-
-
nuclear sfALR interacts with the Jun activation-domain binding protein (JAB1) mediating the interaction between ALR and activator protein-1 (AP-1) via the phosphorylation of c-Jun
-
-
?
additional information
?
-
-
quiescin-sulfhydryl oxidase (QSOX) catalyzes the facile direct introduction of disulfide bonds into unfolded, reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains, the affinity of QSOX for monomer is significantly lower than that for octamer. QSOX exhibits much lower affinity for N-terminally truncated murine prion protein (PrP89-230) than for the full-length murine prion protein (PrP23-231), suggesting that the N-terminal region of prion protein is critical for the interaction of prion protein with QSOX
-
-
?
additional information
?
-
-
catalytic mechanism of the short, cytokine, form of augmenter of liver regeneration (sfALR) using model thiol substrates of the enzyme. While 2-mercaptoethanol is a very poor substrate of enzyme sfALR, it rapidly generates a mixed disulfide intermediate allowing the thiolate of C145 to form a strong charge-transfer complex with the flavin. Glutathione is unable to form charge-transfer complexes and is no substrate of the oxidase
-
-
?
additional information
?
-
-
enzyme appears to protect sperm structure and function against damage by endogeneous sulfhydryls
-
-
?
additional information
?
-
redox cycling of the FAD moiety is essential for enzyme activity
-
-
?
additional information
?
-
-
essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic but not of mitochondrial Fe-S proteins
-
-
?
additional information
?
-
-
Erv2p functions in the generation of microsomal disulfide bonds acting in parallel with Ero1p, the essential FAD-dependent oxidase of protein disulfide isomerase
-
-
?
additional information
?
-
-
Evr1p is involved in cellular iron homeostasis, physiological role of the ERV1/ALR family enzymes, overview
-
-
?
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
?
additional information
?
-
does not oxidize reduced thioredoxin
-
-
?
additional information
?
-
-
Erv2p is a modest catalyst of disulfide bond formation. None of the monothiols (at 10 mM), including beta-mercaptoethanol, N-acetylcysteamine, reduced glutathione and CoASH, prove detectable substrates of the yeast oxidase at pH 7.5. In contrast, dithiols are significant substrates
-
-
?
additional information
?
-
-
Erv1p contains three conserved disulfide bonds arranged in two CXXC motifs and one CX16C motif, the CX16C disulfide plays an important role in stabilizing the folding of Erv1p, both CXXC disulfides are required for Erv1 oxidase activity, but none of the disulfide is essential for FAD binding, overview
-
-
?
additional information
?
-
unfolded reduced proteins are more than 200fold more effective substrates on a per-thiol basis than glutathione, and some 10fold better than the parasite bis-glutathione analog, trypanothione. The CxxC motif in the single Trx domain is crucial for efficient catalysis of the oxidation of both reduced RNase and the model substrate dithiothreitol. The proximal disulfide CIII-CIV, which interacts with the flavin, is catalytically crucial. Turnover is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor
-
-
?
additional information
?
-
-
unfolded reduced proteins are more than 200fold more effective substrates on a per-thiol basis than glutathione, and some 10fold better than the parasite bis-glutathione analog, trypanothione. The CxxC motif in the single Trx domain is crucial for efficient catalysis of the oxidation of both reduced RNase and the model substrate dithiothreitol. The proximal disulfide CIII-CIV, which interacts with the flavin, is catalytically crucial. Turnover is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor
-
-
?
additional information
?
-
-
redox potentials of TbQSOX-bound FAD and of the CIIIXXCIV proximal disulfide, overview. Determining the redox potential of the CIXXCII motif requires isolating the redox-active TRX domain from the HRR-ERV domains to prevent transfer of reducing equivalents from the CIXXCII dithiol to the CIIIXXCIV and FAD centers of TbQSOX, overview
-
-
?
