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
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1.8.3.2
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hepatocytes
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intermembrane
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oxidases
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relay
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qsoxs
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thioredoxin
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redox-active
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hepatectomy
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hepatotrophic
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reoxidized
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hepatectomized
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flavoenzyme
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fad-dependent
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fad-binding
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oxidoreductins
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flavin-linked
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redox-regulated
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isoalloxazine
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3h-tdr
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diagnostics
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medicine
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nutrition
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analysis
- 1.8.3.2
- hepatocytes
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intermembrane
- oxidases
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relay
-
qsoxs
- thioredoxin
-
redox-active
-
hepatectomy
-
hepatotrophic
-
reoxidized
-
hepatectomized
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flavoenzyme
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fad-dependent
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fad-binding
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oxidoreductins
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flavin-linked
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redox-regulated
- isoalloxazine
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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
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1.8.3.2 thiol oxidaseAdvanced search results
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results (Engineering
Engineering on EC 1.8.3.2 - thiol oxidase
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PROTEIN VARIANTS 
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
E174A
dimer interface mutant. The kcat-value of the mutant enzyme is 3.1fold lower than the value of the wild-type enyme
E174A/H227A
dimer interface mutant. The kcat-value of the mutant enzyme is 6.8fold lower than the value of the wild-type enyme
E174K
dimer interface mutant. The kcat-value of the mutant enzyme is 6.7fold lower than the value of the wild-type enyme
E183D
salt bridge mutant. The kcat-value of the mutant enzyme is 1.2fold lower than the value of the wild-type enyme
E183R
salt bridge mutant. The kcat-value of the mutant enzyme is 1.1fold higher than the value of the wild-type enyme
H114A
active-site mutant. The occlusion bodies (OBs) of the mutant have a ragged surface and contain mostly occlusion-derived virus with a single nucleocapsid (ODVs). The occlusion bodies (OBs) of the mutant contain lower numbers of ODVs and have a significantly reduced oral infectivity in comparison to control virus. The kcat-value of the mutant enzyme is 4.1fold lower than the value of the wild-type enyme
H161A
active site mutant. kcat value is too low to be reliably quantitated
H227A
dimer interface mutant. The kcat-value of the mutant enzyme is 3.4fold lower than the value of the wild-type enyme
H227D
dimer interface mutant. The occlusion bodies (OBs) of the mutant contain lower numbers of ODVs and have a significantly reduced oral infectivity in comparison to control virus. kcat value is too low to be reliably quantitated
Q235A
active site mutant. kcat value is too low to be reliably quantitated
R127A/E183A
salt bridge mutant. The occlusion bodies (OBs) of the mutant have a ragged surface and contain mostly occlusion-derived virus with a single nucleocapsid (ODVs). The occlusion bodies (OBs) of the mutant contain lower numbers of ODVs and have a significantly reduced oral infectivity in comparison to control virus. The kcat-value of the mutant enzyme is 1.2fold lower than the value of the wild-type enyme
R127E
salt bridge mutant. The kcat-value of the mutant enzyme is 1.4fold lower than the value of the wild-type enyme
R127E/E183R
salt bridge mutant. The kcat-value of the mutant enzyme is 1.1fold lower than the value of the wild-type enyme
C124A
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site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
C15A
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site-directed mutagenesis, increased activity compared to the wild-type enzyme
C15A/C124A
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site-directed mutagenesis, decreased activity compared to the wild-type enzyme
C15A/C74A/C85A/C124A
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site-directed mutagenesis, increased activity compared to the wild-type enzyme
C74A/C85A
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site-directed mutagenesis, decreased activity compared to the wild-type enzyme
E143K/E144K
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site-directed mutagenesis, substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential
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
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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
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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
D24A
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the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
N131A
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the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
N34A
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enhancement of catalytic activity for GSH, whereas the catalytic activity for gamma-glutamylcysteine remains unchanged. The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
N34Q
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the mutant enzyme oxidizes GSH more efficiently (201%) than the wild-type enzyme
P129A
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the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
S32A
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the mutant enzyme oxidizes GSH more efficiently (169%) than the wild-type enzyme. About 1.5fold increase in GSSG production compared to that of the parental ERV1 gene
S32A/N34A
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the mutant enzyme oxidizes GSH more efficiently (240%) than the wild-type enzyme and shows comparable activity for gamma-glutamylcysteine (96%). The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
S32T
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the mutant enzyme oxidizes GSH more efficiently (178%) than the wild-type enzyme
S32T/N34A
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the mutant enzyme shows almost the same activity for GSH (192%) compared to mutant enzyme S32A, S32T, and N34A, and high activity for gamma-glutamylcysteine (161%). The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
W132A
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the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
N131A
Saccharomyces cerevisiae NBRC 10505
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the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
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N34A
Saccharomyces cerevisiae NBRC 10505
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enhancement of catalytic activity for GSH, whereas the catalytic activity for gamma-glutamylcysteine remains unchanged. The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
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P129A
Saccharomyces cerevisiae NBRC 10505
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the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
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S32A
Saccharomyces cerevisiae NBRC 10505
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the mutant enzyme oxidizes GSH more efficiently (169%) than the wild-type enzyme. About 1.5fold increase in GSSG production compared to that of the parental ERV1 gene
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S32T
Saccharomyces cerevisiae NBRC 10505
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the mutant enzyme oxidizes GSH more efficiently (178%) than the wild-type enzyme
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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
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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
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imported into mitochondria with similar efficiencies as wild-type Erv1
C30S/C33S
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imported into mitochondria with similar efficiencies as wild-type Erv1
C30S/C33S
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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
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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
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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
construction of a mutant ac92-knockout virus
additional information
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construction of a mutant ac92-knockout virus
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
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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
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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
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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
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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
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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
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the wild-type CGAC motif in the thioredoxin domain of enzyme TbQSOX is replaced by the more oxidizing CPHC or more reducing CGPC sequence, resulting in mutants CIPHCII and CIGPCII. Construction of a truncated mutant containing only the thioredoxin domain TbQSOX-TRX, corresponding to residues 20-199
