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Literature summary extracted from

  • Okuda, A.; Matsusaki, M.; Higashino, Y.; Masuda, T.; Urade, R.
    Disulfide bond formation activity of soybean quiescin sulfhydryl oxidase (2014), FEBS J., 281, 5341-5355 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.3.2 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(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.2 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
1.8.3.2 gene GmQSOX2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree Glycine max

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.2 0.22
-
 RNAse A recombinant enzyme, pH 7.4, 25°C Glycine max
1.8.3.2 52.2
-
 dithiothreitol recombinant enzyme, pH 7.4, 25°C Glycine max

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.2 RNase A + O2 Glycine max
-
 RNase A disulfide + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Glycine max
-
 cv Jack
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.3.2 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 dithiothreitol + O2 low activity Glycine max dithiothreitol disulfide + H2O2
-
 ?
1.8.3.2 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 ?
-
 ?
1.8.3.2 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
-
 ?
1.8.3.2 RNase A + O2
-
 Glycine max RNase A disulfide + H2O2
-
 ?
1.8.3.2 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

EC Number Subunits Comment Organism
1.8.3.2 More isozyme domain structure, overview Glycine max
1.8.3.2 More isozyme domain structure, two splicing variants, overview Glycine max

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 GmQSOX1
-
 Glycine max
1.8.3.2 GmQSOX2
-
 Glycine max
1.8.3.2 QSOX
-
 Glycine max
1.8.3.2 quiescin sulfhydryl oxidase
-
 Glycine max

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.3.2 25
-
 assay at Glycine max

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.3.2 13.9
-
 dithiothreitol recombinant enzyme, pH 7.4, 25°C Glycine max
1.8.3.2 17.5
-
 RNAse A recombinant enzyme, pH 7.4, 25°C Glycine max

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.3.2 7.4
-
 assay at Glycine max

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 FAD
-
 Glycine max

General Information

EC Number General Information Comment Organism
1.8.3.2 physiological function enzymes GmQSOX1a,GmQSOX1b, and GmQSOX2a play important roles in protein folding in the endoplasmic reticulum Glycine max
1.8.3.2 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.3.2 0.266
-
 dithiothreitol recombinant enzyme, pH 7.4, 25°C Glycine max
1.8.3.2 70.45
-
 RNAse A recombinant enzyme, pH 7.4, 25°C Glycine max