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Enzyme Nomenclature
Information on EC 1.8.3.2 - thiol oxidase
Word Map on EC 1.8.3.2
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.8.3.2
-
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RECOMMENDED NAME
GeneOntology No.
thiol oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
ter bi substituted mechanism, O2 binds first
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
the CXXC motif in the active site sequence of Erv2p is catalytically essential, reaction mechanism involving reactive cysteine residues C121 and C124 of the A subunit, and C176 and C178 of the B subunit
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
the N-terminal cysteine pair of the enzyme is essential for in vivo activity and interacts with the primary redox centre
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif YPCCXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
thiol:oxygen oxidoreductase
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
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CAS REGISTRY NUMBER
COMMENTARY
9029-39-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
Erv1p is a FAD-dependent sulfhydryl oxidase and is an essential component of the redox regulated Mia40/Erv1 import and assembly pathway used by many of the cysteine-containing intermembrane space proteins
physiological function
-
enzyme gene eroA gene is essential for viability. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant; isoform ErvA gene ervA does not have an obvious role in the secretion of native proteins, including glucoamylase. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant
physiological function
protein Alr is able to substitute for the function of Saccharomyces cerevisiae Erv1. Alr is required for mitochondrial biogenesis of human Mia40, which is responsible for the import and oxidative folding of proteins destined for the intermembrane space of mitochondria. The defective accumulation of human Mia40 in mitochondria in a recently identified disease that is caused by amino acid exchange in Alr
physiological function
-
enzyme gene eroA gene is essential for viability. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant; isoform ErvA gene ervA does not have an obvious role in the secretion of native proteins, including glucoamylase. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant
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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
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
-
-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
-
-
-
-
?
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-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
-
2-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
?
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
-
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
-
-
-
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
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-
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
thioredoxin + O2
thioredoxin disulfide + H2O2
-
substrate from Escherichia coli
-
-
ir
additional information
?
-
no activity with glutathione, 2-mercaptoethanol, and di(2-mercaptoethanol)
-
-
-
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
?
-
-
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 might communicate with the respiratory chain via the mediation of cytochrome c
-
-
-
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
-
-
-
-
?
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
Q8GXX0
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
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
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
O00391
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
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
Q6IUU3
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
additional information
?
-
-
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
-
additional information
?
-
O08841
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
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
-
additional information
?
-
Q6ZRP7
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
?
-
-
enzyme appears to protect sperm structure and function against damage by endogeneous sulfhydryls
-
-
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm
FAD
-
firmly attached but nut covalently linked to the protein; one molecule of FAD per subunit
FAD
-
flavoprotein, 1 FAD molecule per enzyme subunit with 1 phosphorus atom per FAD as cofactor of the cofactor
FAD
-
required for activity, binding domain is located on the 60-kDa-enzyme fragment, electron-transfer mechanism in the native enzyme and the 60 kDA enzyme fragment
FAD
dependent on, N-terminal cysteine pair contributes to the correct arrangement of the FAD-binding fold
FAD
-
dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity
FAD
-
dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. No charge-transfer complex between a proximal thiolate and the oxidized flavin
FAD
-
dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview
FAD
-
dependent on. The three disulfides of the enzyme are not essential for FAD binding
FAD
turnover is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor
additional information
-
enzyme contains a thioredoxin domain, 1 redox-active disulfide per subunit
-
additional information
-
enzyme contains a thioredoxin and an ERV1 domain
-
additional information
-
enzyme contains a thioredoxin and a ERV1 domain
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Iron
MgSO4
-
in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RNAi
-
silences QSOX. Survival of QSOX-silenced insects is reduced over controls following blood digestion, most likely due to the compromised ability of mosquitoes to scavenge and/or prevent damage caused by blood meal-derived oxidative stress. Higher lipid peroxidation and mortality in QSOX-silenced mosquitoes may be an indication that the redox balance is altered in these insects after a blood meal
-
EDTA
-
inhibition of enzyme from kidney and small intestine, no inhibition of enzyme from skin and seminal vesivles
Zn2+
-
weak binding to the four-electron-reduced enzyme, rapid inhibition, modeling of metal binding
Zn2+
-
upon coordination with Zn2+, full reduction of Erv2p requires 6 electrons. Strongly inhibits Erv2p when assayed using tris(2-carboxyethyl)phosphine as the reducing substrate of the oxidase. Restoration of 1 mM EDTA effects rapid recovery of 80% of the original activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
-
high concentrations of H2O2, inducing apoptosis, cause an increase of QSOX1 mRNA and protein
L-Cys
-
fungus is not able to use L-Cys as sulfur source instead of sulfate. Presence of L-Cys induces production of an excessive amount of both intracellular and extracellular enzyme
MgSO4
-
in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium
additional information
-
enzyme expression in endometrial glandular epithelium is inducible by estradiol in presence of cycloheximide, and by serum deprivation
-
additional information
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
O2
-
with 0.3 mM reduced thioredoxin as the substrate of the reductive half-reaction and an initial oxygen concentration of around 0.3 mM such that the reduced thioredoxin would be depleted by 10% during the course of the reaction
0.018
O2
-
25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.027
O2
-
25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
0.057
O2
-
25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
0.062
O2
-
25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
0.087
O2
-
25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
0.0174
Reduced ribonuclease
-
corresponds to a sulfhydryl concentration of 0.14 mM
-
additional information
additional information
-
the activity with small thiols is dominated by the Km value
-
additional information
additional information
the activity with small thiols is dominated by the Km value
-
additional information
additional information
-
redox potential of wild-type and mutant enzymes
-
additional information
additional information
-
oxygen consumption kinetic parameters for the WT and Erv1p mutants, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
O2
Saccharomyces cerevisiae
-
25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.8
O2
Saccharomyces cerevisiae
-
25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
1.1
O2
Saccharomyces cerevisiae
-
25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
1.3
O2
Saccharomyces cerevisiae
-
25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
1.5
O2
Saccharomyces cerevisiae
-
25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
O2
Saccharomyces cerevisiae
-
25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
9
0.0024
O2
Saccharomyces cerevisiae
-
25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
9
0.0039
O2
Saccharomyces cerevisiae
-
25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
9
0.0041
O2
Saccharomyces cerevisiae
-
25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
9
0.0093
O2
Saccharomyces cerevisiae
-
25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
9
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a continuous fluorescence assay for sulfhydryl oxidase
additional information
-
several assay methods are used dependent on the substrate, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8 - 8.2
-
oxidation of 5,5'-dithiobis(2-nitrobenzoic acid) and reactivation of ribonuclease
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
pH 5.0: about 40% of maximal activity, pH 11: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
endometrial cells. Enzyme level increases during a serum depletion-induced quiescence, decreases when cells enter the g1 phase after serum stimulation, and is restored during the S and G2/M phases
-
high expression in neurons producing disulfide-bounded neuropeptides
additional information
-
highest enzyme expression in reticular structures, such as the basal forebrain, reticular thalamic nucleus, and reticular nuclei of the brainstem
-
especially in neurons throughout the rostrocaudal extent of the brain as well as in the spinal cord, in olfactory bulbs, isocortex, hippocampus, basal telencephalon, several thalamic and hypothalamic nuclei, cerebellum, and brainstem nuclei
additional information
tissue expression and distribution, high enzyme concentration in cell types associated with heavy secretory loads
additional information
-
enzyme is expressed in a large number of different cell types and tissues
additional information
-
detailed analysis of cellular and subcellular enzyme localization, overview
additional information
-
in-situ detection of enzyme expression in pituitary gland
additional information
-
enzyme is expressed in a large number of different cell types and tissues
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform EroA is retained in the ER lumen by a C-terminal retention motif
-
isoform EroA is retained in the ER lumen by a C-terminal retention motif
-
-
QSOX1a-V5 is a glycosylated, transmembrane protein localized to the Golgi apparatus
-
high concentration of Evr1p
protein Alr is required for mitochondrial biogenesis of human Mia40, which is responsible for the import and oxidative folding of proteins destined for the intermembrane space of mitochondria
-
Erv1 requires the redox-regulated receptor Mia40 for its import into mitochondria. Interacts via disulfide bonds with Mia40. It does not need two CX2C motifs for import into mitochondria
-
associated to basal-lateral region of the plasma membrane
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PDB
SCOP
CATH
ORGANISM
UNIPROT
African swine fever virus (strain Badajoz 1971 Vero-adapted)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15000
-
2 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
22000
33000
2 * 33000, calculated and crystallization data
44000
45000
47000
64000
65000
66000
70000
78000
90000
22000
-
2 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
dimer
-
2 * 14000, SDS-PAGE, after centrifugation of infected cell extracts in glycerol gradients
dimer
the viral enzyme uses an alternate dimerization mode compared to other viral sulfhydryl oxidases, overview. The dimer interface involves helices alpha2 and alpha3
dimer
2 * 33000, calculated and crystallization data
dimer
-
monomers are linked via a disulfide bridge C15-C124, which is not critical for dimer formation, structure modeling using the enzymes crystal structure
dimer
-
crystal structure, stabilization by extensive noncovalent interactions and a network of hydrogen bonds, structure fo the dimer interface
dimer
-
2 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
monomer
-
1 * 21000, SDS-PAGE, under reducing conditions; 1 * 23000, SDS-PAGE, under reducing conditions
additional information
-
structure determination, comparison, and modelling, overview
additional information
structure determination, comparison, and modelling, overview
additional information
-
structural analysis, modeling of the conserved central domain, the plant enzyme contains a unique C-terminally located CXXXXC motif and no N-terminally localized cysteine pair, which is typical for enzymes of the Erv1/Alr sulfhydryl oxidase family
additional information
-
2 enzyme fragments by partial proteolysis: a 30 kDa nonglycosylated monomeric fragment containing a thioredoxin domain with a CXXC motif, and a 60 kDa glycosylated dimeric fragment with bound FAD and catalytic activity, the latter different from intact enzyme activity
additional information
-
enzyme contains an N-terminal thioredoxin domain, an intervening domain, and a C-terminal ALR/ERV domain, redox-active motif CXXC
additional information
enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
-
structure, active site structure containinbg a CXXC motif
additional information
-
Erv1p contains three conserved disulfide bonds arranged in two CXXC motifs and one CX16C motif in the highly conserved central catalytic core. 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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
flavoprotein
glycoprotein
proteolytic modification
glycoprotein
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
glycoprotein
-
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
-
glycoprotein
2 putative N-glycosylation sites at residues 133-135 and 246-248
glycoprotein
-
two potential sites for N-glycosylation. One of them is used and the 64000 Da purified protein is transformed to 61000 da by the action of endoglycosidase F
proteolytic modification
sequence contains a signal peptide of 23 amino acids
proteolytic modification
-
sequence contains a signal peptide of 23 amino acids
-
proteolytic modification
cleavage of 32 amino acids at the proteolytic site
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified unlabeled and selenomethionine-labeled pB119L-DELTAC, the protein crystallizes readily under a wide range of conditions, multiple anomalous dispersion, X-ray diffraction structure determination and analysis at 1.9 A resolution
crystal structure to 0.98 A resolution shows a configuration of the active-site cysteine residues and bound cofactor similar to that observed in other Erv sulfhydryl oxidases. Protein has a complex quaternary structural arrangement comprising a dimer of pseudodimers with a striking 40-degree kink in the interface helix between subunits
partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv family enzymes. One pseudo-dimer subunit has lost its cofactor and catalytic activity
-
purified recombinant liver enzyme, native enzyme and selenomethionine enzyme, the latter is produced by microseeding with native enzyme, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
crystal structures at 2.0 A resolution of the C-terminal domain and at 3.0 A resolution of a C30S/C133S double mutant. The C-terminal domain exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The N-terminal domain is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the N-terminal domain to the C-terminal domain of another subunit. The four-helix bundle of the C-terminal domain forms a wide platform for the electron donor N-terminal domain. Moreover,the amphipathic helix close to the shuttle redox enter may be critical for the recognition of Mia40, the upstream electron donor
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
enzyme retains more than 80% of the initial activity with glutathione after 24 h incubation at 30-60°C
50
60
additional information
60
-
15 min, 85% loss of activity. 30 min, complete loss of activity
additional information
-
dithiothreitol, 1 mM, increases the stability to heating
additional information
-
dithiothreitol, 1 mM, increases the stability to heating
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme, 10% ethanol, 0.01% H2O2, or in 0.02% sodium azide, loss of only small amounts of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer containing 1 mM EDTA, pH 7.5, stable for at least 1 year
-20°C, purified enzyme from egg white, in 20 mM Tris buffer, stable for months
-
4°C, 50 mM potassium phosphate buffer containing 1 mM EDTA, pH 7.5, stable for at least 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from egg white form a riboflavin-binding, protein-deficient strain, several steps
-
intact enzyme and proteolytically cleaved enzyme in 30 kDa and 60 kDa fragments
-
pB119L is located in the insoluble fraction, it can be solubilized by addition of arginine, and a truncated version lacking 16 residues at the carboxy terminus is a soluble protein
recobinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
-
recombinant enzyme from Escherichia coli by heat treatment, ethanol precipitation, ion exchange chromatography, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel chelate chromatography
-
recombinant His-tagged full length enzyme and C-terminal fragment from Escherichia coli strain BL21 to homogeneity by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant liver enzymes from Escherichia coli strain BL21(DE3)
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis expression in human embryonic kidney HEK cells and in rat kangaroo kidney epithelium Pt-K2 cells
DNA and amino acid sequence determination and analysis, gene structure
expression in Escherichia coli
expression in Escherichia coli strains DH5alpha and BL21(DE3) of wild-type enzyme and a His-tagged truncated enzyme form comprising the 15 kDa C-terminus, expression of full-length point mutants
expression of His6-tagged Alrp in Escherichia coli, expression of GFP-fusion enzyme in cell culture
-
expression of wild-type and mutant enzymes in Escherichia coli strain BC21
-
gene AtErv1, DNA and amino acid sequence analysis, subcloning in Escherichia coli strain DH5alpha, expression of full length enzyme and 15 kDa C-terminal fragment as His-tagged proteins in Escherichia coli strain BL21, transient expression of the enzyme fused to GFP in protoplasts of Arabidopsis thaliana and of Physcomitrella patens with localization in the mitochondria, no complementation of the enzyme-defective yeast mutant erv-ts and yeast deletion mutant DELTAerv1
-
gene cpQSOx1, primary gene sequence, DNA and amino acid sequence analysis, stable expression of the wild-type enzyme in MCF-7 cells with intra- and extracellular localization of the recombinant enzyme, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene SOXN, DNA and amino acid sequence determination, gene maps to chromosome 9q34.3, subcloning in Escherichia coli strain DH10B, in vitro-transcription and -translation
genes ERV1 and ERV2, DNA and amino acid sequence determination and analysis, gene structure, phylogenetic analysis
-
genes QSCN6 or QSOX1, and QSOX2, DNA and amino acid sequence determination and analysis, QSCN6 or QSOX1 is located on chromosome 1q25.2, QSOX2 on chromosome 9q34, gene structure
overexpression of wild-type and mutant liver enzymes in Escherichia coli strain BL21(DE3) with a longer or shorter linker His-tag, overview
-
truncated version of Erv2p, without the N-terminal 34 residues, cloned into a pET24(a+) plasmid carrying kanamycin resistance. Amplified in DH5alpha Escherichia coli strain. Expressed from the Escherichia coli strain BL21(DE3) or BL21(DE3 star)
-
DNA and amino acid sequence determination and analysis, gene structure
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform EroA is transcriptionally up-regulated in response to endoplasmic reticulum stress
isoform ErvA is slightly downregulated in response to dithiothreitol stress yet up-regulated in response to expression of a heterologous protein
isoform EroA is transcriptionally up-regulated in response to endoplasmic reticulum stress
-
isoform EroA is transcriptionally up-regulated in response to endoplasmic reticulum stress
-
-
isoform ErvA is slightly downregulated in response to dithiothreitol stress yet up-regulated in response to expression of a heterologous protein
-
isoform ErvA is slightly downregulated in response to dithiothreitol stress yet up-regulated in response to expression of a heterologous protein
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
yes
a truncated pB119L version lacking 16 residues at the carboxy terminus, i.e. pB119L-DELTAC, is a soluble protein
C72A/C75A
activity indistinguishable from wild-type. Contrary to wild-type, mutant is not modified by maleimide-functionalized polyethylene glycol in presence of dithiothreitol
C124A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
C15A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
C15A/C124A
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
C15A/C74A/C85A/C124A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
C74A/C85A
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
R194H
mutation isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins
C62S
-
site directed mutagenesis, inactive mutant, Cys62 is involved in redox cycling of the FAD moiety
C62S/C65S
-
site directed mutagenesis, inactive mutant, Cys62 and Cys65 are involved in redox cycling of the FAD moiety
C65S
-
site directed mutagenesis, inactive mutant, Cys65 is involved in redox cycling of the FAD moiety
C130S
site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain
C130S/C133S
-
site-directed mutagenesis, the active site mutant shows no or very little activity, and the mutant shows a shifted protein-bound FAD spectrum compared to the wild-type enzyme Erv1p, the active site disulfide is located proximal to the isoalloxazine ring of FADa nd the mutation changes bound-FAD absorption slightly, the mutant is active in presence of DTT, but not with tris(2-carboxyethyl)phosphine
C133S
C159S
site-directed mutagenesis, about 70% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C159S/C176S
-
site-directed mutagenesis, the mutant shows the same protein-bound FAD spectrum as the wild-type enzyme Erv1p
C176S
site-directed mutagenesis, about 60% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C30S
C30S/C33S
C33S
site-directed mutagenesis, about 50% reduced activity in vitro compared to the wild-type enzyme, no complementation of an enzyme-defect mutant strain
C69S
about 5% of wild-type activity with substrate dithiothreitol, 0.5% with substrate rRNase
C72S
about 5% of wild-type activity with substrate dithiothreitol, 0.5% with substrate rRNase
additional information
C133S
site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain
C133S
-
imported into mitochondria with similar efficiencies as wild-type Erv1
C30S
site-directed mutagenesis, about 70% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C30S
-
imported into mitochondria with similar efficiencies as wild-type Erv1
C30S/C33S
-
imported into mitochondria with similar efficiencies as wild-type Erv1
C30S/C33S
-
site-directed mutagenesis, the mutant shows the same protein-bound FAD spectrum as the wild-type enzyme Erv1p
additional information
-
construction of a mutant missing the active site disulfide, the mutant also exhibits a fast increase in absorption at 340 nm upon reaction with CO2-, the flavin is reduced directly by the CO2- radicals, and as for WT AtErv1 more disulfides than FAD are reduced, overview. A mutant missing the shuttle disulfide shows fast formation of RSS*R radicals at 340 nm, no intermediate phase of radical disappearance, and radical decay in a much slower pseudo-first order process compared to the structural mutant and the wild-type enzyme, The direct reduction of FAD to the semiquinone is 2fold slower than the disulfide radical formation, overview
additional information
recombinant enzyme does not apparently transfer electrons from its Trx domain to its Erv domain to accomplish rapid oxidation of highly reducing model dithiol substrates, and the measured sulfhydryl oxidase activity reflects the activity of the Erv domain alone, limited by a high KM for dithiothreitol and likely other thiol substrates
additional information
antisense constructs of the SOXN gene in Tet21N neuroblastoma cells confer resistance to IFN-gamma-induced apoptosis, while ectopic overexpression in sense direction sensitizes the cells to induced cell death
additional information
-
the conserved C-terminal domain of the human Alrp can functionally replace the yeast domain in vivo, genetic system to study function of sulfhydryl oxidases, overview
additional information
construction of a His-tagged truncated enzyme form comprising the 15 kDa C-terminus, the mutant shows in vitro activity similar to the wild-type enzyme, dimerization behaviour of the mutant enzymes, overview
additional information
-
the conserved C-terminal domain of the human Alrp can functionally replace the yeast domain in vivo, genetic system to study function of sulfhydryl oxidases, overview, enzyme-defective Erv1p mutant shows highly altered mitochondrial membrane morphology with loss of cristae, overview
additional information
replacement of either cysteine of the proximal disulfide, i.e. CIII or CIV with serine essentially abolishes activity both towards dithiothreitol and rRNase. Mutations of the terminal CxxC disulfide do not show significant loss of activity towards dithiothreitol or rRNase, the visible spectra of both CVS and CVIS mutants are comparable to that of the wild-type protein
additional information
-
replacement of either cysteine of the proximal disulfide, i.e. CIII or CIV with serine essentially abolishes activity both towards dithiothreitol and rRNase. Mutations of the terminal CxxC disulfide do not show significant loss of activity towards dithiothreitol or rRNase, the visible spectra of both CVS and CVIS mutants are comparable to that of the wild-type protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
nutrition
additional information
analysis
-
development of a fast and reliable qualitative plate test for screening secreted fungal sulfhydryl oxidases. Screening is based on the Ellman's reagent, i.e. 5,5'-dithiobis(2-nitrobenzoic acid)
analysis
-
development of a fast and reliable qualitative plate test for screening secreted fungal sulfhydryl oxidases. Screening is based on the Ellman's reagent, i.e. 5,5'-dithiobis(2-nitrobenzoic acid). Enzymes could be identified in Aspergillus tubingensis, Chaetomium globusum, Melanocarpus albomyces, Penicillium aurantiogriseum, Penicillium funiculosum, Coniophora puteana and Trametes hirsuta
medicine
-
protective role of QSOX1 against apoptosis. QSOX1 short transcript overexpression slows down proliferation and protects cells from oxidative stress-induced cell death
medicine
mutation R194H has been isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins
nutrition
-
elimination of cooked flavour in ultra-high temperature commercially sterile milk, may have other applications for flavour modification
additional information
-
overexpression of QSOX1a suppresses the lethality of a complete deletion of endoplasmic reticulum oxidase 1 in yeast and restores disulfide bond formation. The enzyme has a minimal role in catalysis of disulfide bonds within the endoplasmic reticulum
additional information
-
functions exclusively in the reducing environment of the cytosol and functions in partnership with auxiliary proteins
additional information
-
functions exclusively in the reducing environment of the cytosol and functions in partnership with auxiliary proteins
additional information
-
Erv1 represents a substrate of the Mia40-dependent translocation pathway
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.3.2)
Information
