Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | Glycine max |
Cloned (Comment) | Organism |
---|---|
gene GmQSOX1, in two slicing variants GmQSOX1a and GmQSOX1b, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of the two variants without the putative signal peptide as soluble His-tagged proteins in Escherichia coli strain Rosetta-gami B (DE3) | Glycine max |
gene GmQSOX2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree | Glycine max |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.22 | - |
RNAse A | recombinant enzyme, pH 7.4, 25°C | Glycine max | |
52.2 | - |
dithiothreitol | recombinant enzyme, pH 7.4, 25°C | Glycine max |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
RNase A + O2 | Glycine max | - |
RNase A disulfide + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Glycine max | - |
cv Jack | - |
Purification (Comment) | Organism |
---|---|
recombinant soluble His-tagged GmQSOX1a and GmQSOX1b from Escherichia coli strain Rosetta-gami B (DE3) by nickel affinity chromatography and gel filtration | Glycine max |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dithiothreitol + O2 | low activity | Glycine max | dithiothreitol disulfide + H2O2 | - |
? | |
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 | Glycine max | ? | - |
? | |
protein A1aB1b + O2 | 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 | Glycine max | protein A1aB1b disulfide + H2O2 | - |
? | |
RNase A + O2 | - |
Glycine max | RNase A disulfide + H2O2 | - |
? | |
RNase A + O2 | 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 | Glycine max | RNase A disulfide + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | isozyme domain structure, overview | Glycine max |
More | isozyme domain structure, two splicing variants, overview | Glycine max |
Synonyms | Comment | Organism |
---|---|---|
GmQSOX1 | - |
Glycine max |
GmQSOX2 | - |
Glycine max |
QSOX | - |
Glycine max |
quiescin sulfhydryl oxidase | - |
Glycine max |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Glycine max |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
13.9 | - |
dithiothreitol | recombinant enzyme, pH 7.4, 25°C | Glycine max | |
17.5 | - |
RNAse A | recombinant enzyme, pH 7.4, 25°C | Glycine max |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Glycine max |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Glycine max |
General Information | Comment | Organism |
---|---|---|
physiological function | enzymes GmQSOX1a,GmQSOX1b, and GmQSOX2a play important roles in protein folding in the endoplasmic reticulum | Glycine max |
physiological function | 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. Enzymes GmQSOX1a,GmQSOX1b, and GmQSOX2a play important roles in protein folding in the endoplasmic reticulum | Glycine max |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.266 | - |
dithiothreitol | recombinant enzyme, pH 7.4, 25°C | Glycine max | |
70.45 | - |
RNAse A | recombinant enzyme, pH 7.4, 25°C | Glycine max |