Literature summary for 1.8.3.2 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 .

Search for more literature for 1.8.3.2

Activating Compound

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(Commentary)

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 [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/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Glycine max	-	cv Jack	-

Purification (Commentary)

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 and Products (Substrate)

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

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

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

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Glycine max

General Information

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 [mM/s]

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

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Release 2023.1 (January 2023)