1.8.4.2 2 glutathione + COX2-disulfide - Saccharomyces cerevisiae glutathione-disulfide + COX2-dithiol - ? 461442 1.8.4.2 2 glutathione + COX2-disulfide - Homo sapiens glutathione-disulfide + COX2-dithiol - ? 461442 1.8.4.2 2 glutathione + COX2-disulfide - Saccharomyces cerevisiae ATCC 204508 glutathione-disulfide + COX2-dithiol - ? 461442 1.8.4.2 2 glutathione + insulin disulfide - Chlamydomonas reinhardtii glutathione disulfide + insulin - ? 460456 1.8.4.2 2 glutathione + pilin FimA-disulfide - Corynebacterium matruchotii glutathione-disulfide + pilin FimA-dithiol - ? 461443 1.8.4.2 2 glutathione + pilin FimA-disulfide recombinant FimA expressed in Escherichia coli Corynebacterium matruchotii glutathione-disulfide + pilin FimA-dithiol - ? 461443 1.8.4.2 2 glutathione + pilin FimA-disulfide - Corynebacterium matruchotii ATCC 14266 glutathione-disulfide + pilin FimA-dithiol - ? 461443 1.8.4.2 2 glutathione + pilin FimA-disulfide recombinant FimA expressed in Escherichia coli Corynebacterium matruchotii ATCC 14266 glutathione-disulfide + pilin FimA-dithiol - ? 461443 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii Challis glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii ATCC 35105 glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii DL1 glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii V288 glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii BCRC 15272 glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein AtlS-disulfide - Streptococcus gordonii CH1 glutathione-disulfide + protein AtlS-dithiol - ? 461444 1.8.4.2 2 glutathione + protein-disulfide - Rhodobacter capsulatus glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Saccharomyces cerevisiae glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Homo sapiens glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Corynebacterium matruchotii glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii Challis glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii ATCC 35105 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Rhodobacter capsulatus NBRC 16581 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Corynebacterium matruchotii ATCC 14266 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii DL1 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii V288 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Rhodobacter capsulatus ATCC BAA-309 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Saccharomyces cerevisiae ATCC 204508 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii BCRC 15272 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Rhodobacter capsulatus SB1003 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + protein-disulfide - Streptococcus gordonii CH1 glutathione-disulfide + protein-dithiol - ? 461445 1.8.4.2 2 glutathione + SCO1-disulfide - Saccharomyces cerevisiae glutathione-disulfide + SCO1-dithiol - ? 461447 1.8.4.2 2 glutathione + SCO1-disulfide - Homo sapiens glutathione-disulfide + SCO1-dithiol - ? 461447 1.8.4.2 2 glutathione + SCO1-disulfide - Saccharomyces cerevisiae ATCC 204508 glutathione-disulfide + SCO1-dithiol - ? 461447 1.8.4.2 2 glutathione + SCO2-disulfide - Saccharomyces cerevisiae glutathione-disulfide + SCO2-dithiol - ? 461448 1.8.4.2 2,3-dimercaptopropanol + protein disulfide - Mus musculus 2,3-dimercaptopropanol disulfide + protein-dithiol - ? 260427 1.8.4.2 2,3-dimercaptopropanol + protein disulfide - Homo sapiens 2,3-dimercaptopropanol disulfide + protein-dithiol - ? 260427 1.8.4.2 2,3-dimercaptopropanol + protein disulfide - Rattus norvegicus 2,3-dimercaptopropanol disulfide + protein-dithiol - ? 260427 1.8.4.2 2,3-dimercaptopropanol + protein disulfide - Bos taurus 2,3-dimercaptopropanol disulfide + protein-dithiol - ? 260427 1.8.4.2 2-mercaptoethanol + protein disulfide - Rattus norvegicus 2-mercaptoethanol disulfide + protein-dithiol - ? 260426 1.8.4.2 2-mercaptoethanol + protein disulfide - Bos taurus 2-mercaptoethanol disulfide + protein-dithiol - ? 260426 1.8.4.2 2-mercaptoethanol glutathione disulfide + glutathione - Populus sp. 2-mercaptoethanol disulfide + glutathione disulfide - ? 460510 1.8.4.2 2-mercaptoethanol glutathione disulfide + glutathione - Chlamydomonas reinhardtii 2-mercaptoethanol disulfide + glutathione disulfide - ? 460510 1.8.4.2 alpha-lipoate + protein disulfide - Homo sapiens ? - ? 260440 1.8.4.2 apocytochrome c + glutathione disulfide - Helicobacter pylori apocytochrome c disulfide + 2 glutathione - ? 441051 1.8.4.2 apocytochrome c + glutathione disulfide - Helicobacter pylori ATCC 700392 apocytochrome c disulfide + 2 glutathione - ? 441051 1.8.4.2 cysteamine + protein disulfide - Mus musculus ? - ? 260435 1.8.4.2 cysteamine + protein disulfide - Homo sapiens ? - ? 260435 1.8.4.2 cysteamine + protein disulfide - Rattus norvegicus ? - ? 260435 1.8.4.2 cysteamine + protein disulfide - Bos taurus ? - ? 260435 1.8.4.2 cysteamine + protein disulfide low activity Homo sapiens ? - ? 260435 1.8.4.2 dihydrolipoamide + protein disulfide - Rattus norvegicus ? - ? 260436 1.8.4.2 dihydrolipoate + protein disulfide - Rattus norvegicus ? - ? 260437 1.8.4.2 dihydrolipoate + protein disulfide - Bos taurus ? - ? 260437 1.8.4.2 dihydrolipoic acid + protein disulfide - Mus musculus ? - ? 260433 1.8.4.2 dihydrolipoic acid + protein disulfide - Homo sapiens ? - ? 260433 1.8.4.2 dihydrolipoic acid + protein disulfide - Rattus norvegicus ? - ? 260433 1.8.4.2 dihydrolipoic acid + protein disulfide - Bos taurus ? - ? 260433 1.8.4.2 dithiothreitol + insulin disulfide - Chlamydomonas reinhardtii dithiothreitol disulfide + insulin - ? 461013 1.8.4.2 dithiothreitol + protein disulfide - Escherichia coli ? - r 260432 1.8.4.2 dithiothreitol + protein disulfide - Rattus norvegicus ? - ? 260432 1.8.4.2 dithiothreitol + protein disulfide - Bos taurus ? - ? 260432 1.8.4.2 dithiothreitol + protein disulfide low activity Homo sapiens ? - ? 260432 1.8.4.2 dithiothreitol + protein disulfide protein disulfide: insulin or thioredoxin Brassica napus ? - r 260432 1.8.4.2 glutathionylated BSA + glutathione - Populus sp. BSA + glutathione disulfide - ? 461074 1.8.4.2 glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation Chlamydomonas reinhardtii glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase - ? 461070 1.8.4.2 glutathionylated glyceraldehyde-3-phosphate dehydrogenase + reduced GRX3 substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation Chlamydomonas reinhardtii glutathione + glyceraldehyde-3-phosphate dehydrogenase + oxidized GRX3 - ? 461071 1.8.4.2 glutathionylated isocitrate lyase + dithiothreitol - Chlamydomonas reinhardtii glutathione dithiothreitol disulfide + isocitrate lyase - ? 461072 1.8.4.2 glutathionylated isocitrate lyase + glutathione - Chlamydomonas reinhardtii glutathione disulfide + isocitrate lyase - ? 461073 1.8.4.2 glutathionylated isocitrate lyase + glutathione substrate is glutathionylated isocitrate lyase of Chlamydomonas rheinhardtii Populus sp. glutathione disulfide + isocitrate lyase - ? 461073 1.8.4.2 GSH + 5,5'-dithiobis(nitrobenzoic acid) - Desulfovibrio vulgaris ? - ? 426462 1.8.4.2 GSH + AtlS - Streptococcus gordonii GSSG + ? - ? 424824 1.8.4.2 GSH + insulin - Escherichia coli GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + insulin - Homo sapiens GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + insulin - Bos taurus GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + insulin proinsulin Mus musculus GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + insulin proinsulin Homo sapiens GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + insulin proinsulin Rattus norvegicus GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + insulin proinsulin Bos taurus GSSG + reduced insulin chain A and B - ? 260425 1.8.4.2 GSH + oxytoxin - Mus musculus ? - ? 260434 1.8.4.2 GSH + oxytoxin - Homo sapiens ? - ? 260434 1.8.4.2 GSH + oxytoxin - Rattus norvegicus ? - ? 260434 1.8.4.2 GSH + oxytoxin - Bos taurus ? - ? 260434 1.8.4.2 GSH + protein disulfide - Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide - Homo sapiens GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide - Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide - Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide - Bos taurus GSSG + protein-dithiol - r 260424 1.8.4.2 GSH + protein disulfide - Mycobacterium tuberculosis GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide protein disulfide: thioredoxin Escherichia coli GSSG + protein-dithiol - r 260424 1.8.4.2 GSH + protein disulfide very rapid disulfide interchange reaction Escherichia coli GSSG + protein-dithiol - r 260424 1.8.4.2 GSH + protein disulfide protein disulfide: e.g. of alcohol dehydrogenase, hexokinase, fructose-1,6-diphosphatase, malate dehydrogenase, glyceraldehyde phosphate dehydrogenase, glycerol phosphate dehydrogenase Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide prolactin is a poor substrate Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide protein disulfide: enzyme itself Escherichia coli GSSG + protein-dithiol - r 260424 1.8.4.2 GSH + protein disulfide physiological function Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide physiological function Homo sapiens GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide physiological function Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide physiological function Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide reductive degradation and assembly of proteins Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide reductive degradation and assembly of proteins Homo sapiens GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide reductive degradation and assembly of proteins Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide reductive degradation and assembly of proteins Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide modulation of enzymatic activity from latent to active form and vice versa Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide modulation of enzymatic activity from latent to active form and vice versa Homo sapiens GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide modulation of enzymatic activity from latent to active form and vice versa Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide modulation of enzymatic activity from latent to active form and vice versa Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide major contributor to the inactivation of oxytoxin by lactating mammary gland Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide enzyme not directly involved in the subcellular processing of receptor-bound internalized insulin Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide feedback control via insulin in the liver Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide feedback control via insulin in the liver Homo sapiens GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide feedback control via insulin in the liver Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide feedback control via insulin in the liver Bos taurus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide synthesis of protein disulfide bond Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide disulfide bonding step in folding pathway of many periplasmic and outer membrane proteins with structural disulfide bonds Escherichia coli GSSG + protein-dithiol - r 260424 1.8.4.2 GSH + protein disulfide initial step in sequential insulin degradation Rattus norvegicus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide enzyme plays a role in formation of intramonomer bonds common to all immunoglobulin molecules Mus musculus GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein disulfide - Mycobacterium tuberculosis Rv3219 GSSG + protein-dithiol - ? 260424 1.8.4.2 GSH + protein-disulfide - Desulfovibrio vulgaris GSSG + protein-dithiol - ? 424826 1.8.4.2 GSH + protein-disulfide - Streptococcus gordonii GSSG + protein-dithiol - ? 424826 1.8.4.2 GSH + vasopressin - Mus musculus ? - ? 260429 1.8.4.2 GSH + vasopressin - Homo sapiens ? - ? 260429 1.8.4.2 GSH + vasopressin - Rattus norvegicus ? - ? 260429 1.8.4.2 GSH + vasopressin - Bos taurus ? - ? 260429 1.8.4.2 GSH + vasotocin - Bos taurus ? - ? 260430 1.8.4.2 GSSG + reduced ribonuclease - Escherichia coli GSH + oxidized ribonuclease - r 260431 1.8.4.2 GSSG + reduced ribonuclease - Bos taurus GSH + oxidized ribonuclease - ? 260431 1.8.4.2 hydroxyethyl disulfide + protein disulfide - Homo sapiens ? - ? 260439 1.8.4.2 insulin disulfide + dithiothreitol - Wuchereria bancrofti insulin + dithiothreitol disulfide - ? 441475 1.8.4.2 insulin disulfide + dithiothreitol - Campylobacter jejuni subsp. jejuni insulin + dithiothreitol disulfide - ? 441475 1.8.4.2 L-cysteine + protein disulfide - Rattus norvegicus cystine + protein-dithiol - ? 260428 1.8.4.2 L-cysteine + protein disulfide - Bos taurus cystine + protein-dithiol - ? 260428 1.8.4.2 additional information reduction of choleragen Bos taurus ? - ? 89 1.8.4.2 additional information redox reaction between different Dsn proteins Escherichia coli ? - ? 89 1.8.4.2 additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Mus musculus ? - ? 89 1.8.4.2 additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Homo sapiens ? - ? 89 1.8.4.2 additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Rattus norvegicus ? - ? 89 1.8.4.2 additional information the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme Bos taurus ? - ? 89 1.8.4.2 additional information immunoglobulin IgM and IgG Mus musculus ? - ? 89 1.8.4.2 additional information immunoglobulin IgM and IgG Homo sapiens ? - ? 89 1.8.4.2 additional information immunoglobulin IgM and IgG Rattus norvegicus ? - ? 89 1.8.4.2 additional information immunoglobulin IgM and IgG Bos taurus ? - ? 89 1.8.4.2 additional information glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species Rattus norvegicus ? - ? 89 1.8.4.2 additional information glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species Bos taurus ? - ? 89 1.8.4.2 additional information scrambled lysozyme Mus musculus ? - ? 89 1.8.4.2 additional information scrambled lysozyme Homo sapiens ? - ? 89 1.8.4.2 additional information scrambled lysozyme Rattus norvegicus ? - ? 89 1.8.4.2 additional information scrambled lysozyme Bos taurus ? - ? 89 1.8.4.2 additional information scrambled trypsin inhibitor and proinsulin Homo sapiens ? - ? 89 1.8.4.2 additional information scrambled trypsin inhibitor and proinsulin Rattus norvegicus ? - ? 89 1.8.4.2 additional information scrambled trypsin inhibitor and proinsulin Bos taurus ? - ? 89 1.8.4.2 additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Mus musculus ? - ? 89 1.8.4.2 additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Homo sapiens ? - ? 89 1.8.4.2 additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Rattus norvegicus ? - ? 89 1.8.4.2 additional information thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical Bos taurus ? - ? 89 1.8.4.2 additional information DsbB protein re-oxidizes the reduced DsbA protein Escherichia coli ? - ? 89 1.8.4.2 additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Mus musculus ? - ? 89 1.8.4.2 additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Homo sapiens ? - ? 89 1.8.4.2 additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Rattus norvegicus ? - ? 89 1.8.4.2 additional information enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease Bos taurus ? - ? 89 1.8.4.2 additional information reduction of ricin and other plant thiols Rattus norvegicus ? - ? 89 1.8.4.2 additional information reduction of ricin and other plant thiols Bos taurus ? - ? 89 1.8.4.2 additional information bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery Bacillus subtilis ? - ? 89 1.8.4.2 additional information ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the the reduction of the cysteinyls in the heme binding site of apocytochrome c Bacillus subtilis ? - ? 89 1.8.4.2 additional information StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis Bacillus subtilis ? - ? 89 1.8.4.2 additional information the enzyme is required for efficient disulfide bond formation in the periplasm Escherichia coli ? - ? 89 1.8.4.2 additional information multifunctional enzyme that efficiently catalyzes disulfide reduction, disulfide isomerization, and dithiol oxidation Homo sapiens ? - ? 89 1.8.4.2 additional information addition of GSH-dependent protein disulfide oxidoreductase to flour significantly increases dough extensibility (from 17 to 49% for cultivars with different quality), which implies the ability of the enzyme to disrupt disulfide bonds in high-molecular-weight gluten polymers Triticum aestivum ? - ? 89 1.8.4.2 additional information the enzyme is unable to reduce insulin Desulfovibrio vulgaris ? - ? 89 1.8.4.2 additional information GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities Chlamydomonas reinhardtii ? - - 89 1.8.4.2 additional information no substrate: insulin disulfide, 2-mercaptoethanol glutathione disulfide Chlamydomonas reinhardtii ? - - 89 1.8.4.2 additional information COA6 interacts with COX2 and SCO proteins in vivo Saccharomyces cerevisiae ? - - 89 1.8.4.2 additional information COA6 interacts with COX2 and SCO proteins in vivo Homo sapiens ? - - 89 1.8.4.2 additional information at least in vitro SCO1 is the dominant interacting partner of COA6 compared to SCO2. H3 and C-terminal residues of COA6 are critical for its interaction with SCO1 Homo sapiens ? - - 89 1.8.4.2 additional information MdbACm directly catalyzes disulfide bond formation in proteins in vitro Corynebacterium matruchotii ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii ? - - 89 1.8.4.2 additional information yeast Coa6 interacts with both Sco1 and Sco2 Saccharomyces cerevisiae ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii Challis ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii ATCC 35105 ? - - 89 1.8.4.2 additional information MdbACm directly catalyzes disulfide bond formation in proteins in vitro Corynebacterium matruchotii ATCC 14266 ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii DL1 ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii V288 ? - - 89 1.8.4.2 additional information COA6 interacts with COX2 and SCO proteins in vivo Saccharomyces cerevisiae ATCC 204508 ? - - 89 1.8.4.2 additional information yeast Coa6 interacts with both Sco1 and Sco2 Saccharomyces cerevisiae ATCC 204508 ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii BCRC 15272 ? - - 89 1.8.4.2 additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii CH1 ? - - 89 1.8.4.2 reduced dithiothreitol + NADP+ - Rattus norvegicus oxidized dithiothreitol + NADPH + H+ - r 451783 1.8.4.2 SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues - Streptococcus pyogenes SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond - ? 461690 1.8.4.2 SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues the superantigen SpeA contains 3 cysteine residues (Cys 87, Cys90, and Cys98) and has a disulfide bond formed between Cys87 and Cys98 Streptococcus pyogenes SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond - ? 461690 1.8.4.2 thioglycolic acid + protein disulfide - Rattus norvegicus ? - ? 260438