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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

Reaction

2 R'C(R)SH +

O2
=
R'C(R)S-S(R)CR'
 +
H2O2

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 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.3 With oxygen as acceptor
                1.8.3.2 thiol oxidase

Activating Compound

Activating Compound on EC 1.8.3.2 - thiol oxidase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
soybean PDI family protein
-
cooperative refolding of unfolded RNase A by rGmQSOX1 and all tested soybean PDI family proteins of group I and group II, but not of group III. Most effective are GmPDIL-2 and GmPDIL-1 with rGmQSOX1. These PDI family proteins contain two classic CGHC motifs in the a and a' domains, except for the group III PDI family proteins, which have nonclassic active centre CXXC motifs. The combination of rGmQSOX1 and GmPDIL-2 with an a-b-b'-a' domain structure shows the highest level of refolding activity, while the GmPDIL-2 C101A/C104A/C440A/C443A mutant, in which all of the cysteines in the two active centres are replaced with alanines, is devoid of cooperative oxidative refolding activity with rGmQSOX1. The refolding activity of rGmQSOX1 combined with the C104A/C443A mutant is 18% of that of rGmQSOX1 combined with wild-type GmPDIL-2. Analysis of the cooperation mechanism, overview
-
staurosporine aglycone
-
-
Triton X-100
-
0-0.1% concentration, at most 30% activation
additional information
-