Reference on EC 1.8.4.2 - protein-disulfide reductase (glutathione)
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hillson, D.A.; Freedman, R.B.
Resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography
Biochem. J.
191
373-388
1980
Bos taurus
Hawkins, H.C.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Differences between protein disulphide-isomerase and glutathione-insulin transhydrogenase activities in ox liver
Biochem. J.
159
385-393
1976
Bos taurus
Ibbetson, A.L.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
Biochem. J.
159
377-384
1976
Rattus norvegicus
Varandani, P.T.
Glutathione-insulin transhydrogenase (protein-disulfide interchange enzyme)
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
753-765
1989
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
-
Varandani, P.T.
Mechanistic and structural aspects of glutathione-insulin transhydogenase (protein-disulfide interchange enzyme)
Dev. Biochem.
1
29-42
1978
Bos taurus, Homo sapiens, Rattus norvegicus
-
Morris, J.I.; Varandani, P.T.
Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)
Biochim. Biophys. Acta
949
169-180
1988
Homo sapiens, Rattus norvegicus
Chowdhary, B.K.; Smith, G.D.; Mahler, R.; Peters, T.J.
Studies on the subcellular localization and role of glutathione-insulin transhydrogenase in rat liver
Biosci. Rep.
3
323-329
1983
Rattus norvegicus
Hern, E.P.; Varandani, P.T.
Nonlatent and latent hepatic glutathione-insulin transhydrogenase activity during perinatal development and liver regeneration in rats and in rat placenta
Biochem. Biophys. Res. Commun.
116
909-915
1983
Rattus norvegicus
Spolter, P.D.; Vogel, J.M.
Rat-liver thiol: protein-disulphide oxidoreductase
Biochim. Biophys. Acta
167
525-537
1968
Rattus norvegicus
Varandani, P.T.
Insulin degradation. I. Purification and properties of glutathione-insulin transhydrogenase of rat liver
Biochim. Biophys. Acta
286
126-135
1972
Rattus norvegicus
Chandler, M.L.; Varandani, P.T.
Insulin degradation. II. The widespread distribution of glutathione-insulin transhydrogenase in the tissues of the rat
Biochim. Biophys. Acta
286
136-145
1972
Bos taurus, Rattus norvegicus
Varandani, P.T.
Insulin degradation. V. Unmasking of glutathione-insulin transhydrogenase in rat liver microsomal membrane
Biochim. Biophys. Acta
304
642-659
1973
Rattus norvegicus
Chandler, M.L.; Varandani, P.T.
Insulin degradation. 8. Protein thiols as co-substrates for glutathione-insulin transhydrogenase
Biochim. Biophys. Acta
320
258-266
1973
Bos taurus
Ansorge, S.; Bohley, P.; Kirschke, H.; Langner, J.; Wiederanders, B.; Hanson, H.
Metabolism of insulin and glucagon. Glutathione-insulin transhydrogenase from microsomes of rat liver
Eur. J. Biochem.
32
27-35
1973
Rattus norvegicus
Varandani, P.T.
Insulin degradation. X. Identification of insulin degrading activity of rat liver plasma membrane as glutathione-insulin transhydrogenase
Biochem. Biophys. Res. Commun.
55
689-696
1973
Rattus norvegicus
Hern, E.P.; Varandani, P.T.
Topology of glutathione-insulin transhydrogenase in rat liver microsomes
Biochim. Biophys. Acta
732
170-178
1983
Rattus norvegicus
Kohnert, K.D.; Hahn, H.J.; Zuhlke, H.; Schmidt, S.; Fiedler, H.
Breakdown of exogenous insulin by Langerhans islets of the pancreas in vitro
Biochim. Biophys. Acta
338
68-77
1974
Mus musculus, Rattus norvegicus
-
Schneider, F.; Schauer, R.; Martini, O.; Hahn, J.
Reversibility of glutathione-insulin-transhydrogenation (protein disulfide-reductase reaction)
Hoppe-Seyler's Z. Physiol. Chem.
348
391-400
1967
Bos taurus
Varandani, P.T.
Insulin degradation. XII. The amino acid composition, amino-terminal, and carbohydrate content of beef pancreatic glutathione-insulin transhydrogenase
Biochim. Biophys. Acta
371
577-581
1974
Bos taurus
Bjelland, S.; Wallevik, K.; Kroll, J.; Dixon, J.E.; Morin, J.E.; Freedman, R.B.; Lambert, N.; Varandani, P.T.; Nafz, M.A.
Immunological identity between bovine preparations of thiol:protein-disulphide oxidoreductase, glutathione-insulin transhydrogenase and protein-disulphide isomerase
Biochim. Biophys. Acta
747
197-199
1983
Bos taurus
Bjelland, S.
Tissue distribution and molecular heterogeneity of bovine thiol:protein-disulphide oxidoreductase (disulphide interchange enzyme)
Comp. Biochem. Physiol. B
87
907-914
1987
Bos taurus
Bjelland, S.; Foltmann, B.; Wallevik, K.
Purification of thiol:protein-disulfide oxidoreductase from bovine liver
Anal. Biochem.
142
463-466
1984
Bos taurus
Roth, R.A.
Bacitracin: an inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase
Biochem. Biophys. Res. Commun.
98
431-438
1981
Rattus norvegicus
Varandani, P.T.; Plumley, H.
Mechanism of action of glutathione-insulin transhydrogenase. Presence of a functional sulfhydryl group for activity
Biochim. Biophys. Acta
151
273-275
1968
Bos taurus
Barbieri, L.; Batelli, M.G.; Stirpe, F.
Reduction of ricin and other plant toxins by thiol:protein disulfide oxidoreductases
Arch. Biochem. Biophys.
216
380-383
1982
Bos taurus, Rattus norvegicus
Chandler, M.L.; Varandani, P.T.
Insulin degradation. XV. Use of different assay methods for the study of mechanism of action of glutathione-insulin transhydrogenase
Biochim. Biophys. Acta
397
307-317
1975
Bos taurus
Moss, J.; Stanley, S.J.; Morin, J.E.; Dixon, J.E.
Activation of choleragen by thiol: protein disulfide oxidoreductase
J. Biol. Chem.
255
11085-11087
1980
Bos taurus
Pace, M.; Pietta, P.G.; Fiorino, A.; Pocaterra, E.; Dixon, J.E.
Nonspecific reaction of a thiol: protein disulfide oxidoreductase with the disulfide bonds of insulin
Experientia
41
1332-1335
1985
Bos taurus
Pace, M.; Dixon, J.E.
The nature of the multiple forms of bovine thiol:protein disulfide oxidoreductase
Int. J. Pept. Protein Res.
14
409-413
1979
Bos taurus
Varandani, P.T.; Nafz, M.A.; Chandler, M.L.
Interaction of insulin analogs, glucagon, growth hormone, vasopressin, oxytocin, and scrambled forms of ribonuclease and lysozyme with glutathione-insulin transhydrogenase (thiol: protein-disulfide oxidoreductase): dependence upon conformation
Biochemistry
14
2115-2120
1975
Bos taurus
Carmichael, D.F.; Morin, J.E.; Dixon, J.E.
Purification and characterization of a thiol:protein disulfide oxidoreductase from bovine liver
J. Biol. Chem.
252
7163-7167
1977
Bos taurus
Hillson, D.A.; Freedman, R.B.
Bovine liver thiol-protein disulphide oxidoreductases. An alternative method for differential purification and resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase
Biochem. J.
191
389-393
1980
Bos taurus
Tomizawa, H.H.
Glutathione-insulin transhydrogenase (steer liver)
Methods Enzymol.
17B
515-519
1971
Bos taurus
-
Morin, J.E.; Dixon, J.E.; Chang, P.P.; Moss, J.
Identification of thiol:protein disulfide oxidoreductase activity in cultured human fibroblasts: dependence of enzyme activity on growth conditions
Biochem. Biophys. Res. Commun.
111
872-877
1983
Homo sapiens
Ferrier, B.M.; Hendrie, J.M.; Cardy, C.A.
Glutathione-insulin transhydrogenase activity in pregnant mouse mammary gland: hormonal influences studied in tissue culture
Can. J. Biochem.
55
340-345
1977
Mus musculus
Kohnert, K.D.; Jahr, H.; Schmidt, S.; Hahn, H.J.; Zuhlke, H.
Demonstration of insulin degradation by thiol-protein disulfide oxidoreductase (glutathione-insulin transhydrogenase) and proteinases of pancreatic islets
Biochim. Biophys. Acta
422
254-259
1976
Rattus norvegicus
Roth, R.A.; Koshland, M.E.
Role of disulfide interchange enzyme in immunoglobulin synthesis
Biochemistry
20
6594-6599
1981
Mus musculus
Lambert, N.; Freedman, R.B.
Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction
Biochem. J.
213
235-243
1983
Bos taurus
Varandani, P.T.
Insulin degradation in insulinoma: evidence for the occurrence of an inactive form of glutathione-insulin transhydrogenase and for the absence of insulin A and B chains degrading protease(s)
Biochem. Biophys. Res. Commun.
60
1119-1126
1974
Homo sapiens
Varandani, P.T.; Nafz, M.A.
Interaction of glutathione-insulin transhydrogenase (disulfide interchange enzyme) with phospholipids
Biochim. Biophys. Acta
438
358-369
1976
Bos taurus, Rattus norvegicus
Morin, J.E.; Carmichael, C.F.; Dixon, J.E.
Characterization, kinetics and comparative properties of thiol:protein disulfide oxidoreductase
Arch. Biochem. Biophys.
189
354-363
1978
Bos taurus
Varandani, P.T.; Nafz, M.A.
Inhibition of glutathione-insulin transhydrogenase by metal ions and activation by histidine and other chelating agents
Biochim. Biophys. Acta
832
7-13
1985
Bos taurus
Chandler, M.L.; Varandani, P.T.
Kinetic analysis of the mechanism of insulin degradation by glutathione-insulin transhydrogenase (thiol: protein-disulfide oxidoreductase)
Biochemistry
14
2107-2115
1975
Bos taurus
Fabianek, R.A.; Hennecke, H.; Thony-Meyer, L.
Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
FEMS Microbiol. Rev.
24
303-316
2000
Escherichia coli, Pectobacterium carotovorum, Dickeya chrysanthemi, Haemophilus influenzae, Klebsiella sp., Yersinia pestis, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Enteritidis, Shigella flexneri, Vibrio cholerae serotype O1, Pseudomonas syringae (O52376), Pseudomonas aeruginosa (P0C2B2), Legionella pneumophila (P50024), Lelliottia amnigena (Q9XDP0), Yersinia pestis DsbA homologous, Dickeya chrysanthemi DsbA homologous, Vibrio cholerae serotype O1 DsbA homologous, Salmonella enterica subsp. enterica serovar Enteritidis DsbA homologous, Salmonella enterica subsp. enterica serovar Typhimurium DsbA homologous, Haemophilus influenzae DsbA homologous, Klebsiella sp. DsbA homologous, Pectobacterium carotovorum DsbA homologous, Legionella pneumophila DsbA homologous (P50024), Pseudomonas syringae DsbA homologous (O52376), Shigella flexneri DsbA homologous, Pseudomonas aeruginosa DsbA homologous (P0C2B2), Lelliottia amnigena DsbA homologous (Q9XDP0)
Biaglow, J.E.; Donahue, J.; Tuttle, S.; Held, K.; Chrestensen, C.; Mieyal, J.
A method for measuring disulfide reduction by cultured mammalian cells: relative contributions of glutathione-dependent and glutathione-independent mechanisms
Anal. Biochem.
281
77-86
2000
Cricetulus griseus, Homo sapiens
Loferer, H.; Hennecke, H.
Protein disulfide oxidoreductases in bacteria
Trends Biochem. Sci.
19
169-171
1994
Escherichia coli, Haemophilus influenzae, Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 DsbA homologous, Haemophilus influenzae DsbA homologous
Heuck, A.P.; Wolosiuk, R.A.
Di-fluoresceinthiocarbamyl-insulin: A fluorescent substrate for the assay of protein disulfide oxidoreductase activity
Anal. Biochem.
248
94-101
1997
Brassica napus
Moessner, E.; Iwai, H.; Glockshuber, R.
Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases
FEBS Lett.
477
21-26
2000
Escherichia coli
Tang, W.; Wang, C.C.
Zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ
Biochemistry
40
14985-14994
2001
Escherichia coli
Ishihara, T.; Tomita, H.; Hasegawa, Y.; Tsukagoshi, N.; Yamagata, H.; Udaka, S.
Cloning and characterization of the gene for a protein thiol-disulfide oxidoreductase in Bacillus brevis
J. Bacteriol.
177
745-749
1995
Brevibacillus brevis
Meima, R.; Eschevins, C.; Fillinger, S.; Bolhuis, A.; Hamoen, L.W.; Dorenbos, R.; Quax, W.J.; Van Dijl, J.M.; Provvedi, R.; Chen, I.; Dubnau, D.; Bron, S.
The bdbDC operon of Bacillus subtilis encodes thiol-disulfide oxidoreductases required for competence development
J. Biol. Chem.
277
6994-7001
2002
Bacillus subtilis
Van Straaten, M.; Missiakas, D.; Raina, S.; Darby, N.J.
The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli
FEBS Lett.
428
255-258
1998
Escherichia coli
Dorenbos, R.; Stein, T.; Kabel, J.; Bruand, C.; Bolhuis, A.; Bron, S.; Quax, W.J.; Van Dijl, J.M.
Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168
J. Biol. Chem.
277
16682-16688
2002
Bacillus subtilis
Kleemann, R.; Rorsman, H.; Rosengren, E.; Mischke, R.; Mai, N.T.; Bernhagen, J.
Dissection of the enzymatic and immunologic functions of macrophage migration inhibitory factor. Full immunologic activity of N-terminally truncated mutants
Eur. J. Biochem.
267
7183-7192
2000
Homo sapiens
Erlendsson, L.S.; Hederstedt, L.
Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells
J. Bacteriol.
184
1423-1429
2002
Bacillus subtilis
Erlendsson, L.S.; Moller, M.; Hederstedt, L.
Bacillus subtilis StoA Is a thiol-disulfide oxidoreductase important for spore cortex synthesis
J. Bacteriol.
186
6230-6238
2004
Bacillus subtilis
Philipps, B.; Glockshuber, R.
Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli
J. Biol. Chem.
277
43050-43057
2002
Escherichia coli
Erlendsson, L.S.; Acheson, R.M.; Hederstedt, L.; Le Brun, N.E.
Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis
J. Biol. Chem.
278
17852-17858
2003
Bacillus subtilis
Frickel, E.M.; Frei, P.; Bouvier, M.; Stafford, W.F.; Helenius, A.; Glockshuber, R.; Ellgaard, L.
ERp57 is a multifunctional thiol-disulfide oxidoreductase
J. Biol. Chem.
279
18277-18287
2004
Homo sapiens
Tanaka, R.; Mizukami, M.; Ishibashi, M.; Tokunaga, H.; Tokunaga, M.
Cloning and expression of the ccdA-associated thiol-disulfide oxidoreductase (catA) gene from Brevibacillus choshinensis: stimulation of human epidermal growth factor production
J. Biotechnol.
103
1-10
2003
Brevibacillus choshinensis
Crow, A.; Le Brun, N.E.; Oubrie, A.
The role of ResA in type II cytochrome c maturation
Biochem. Soc. Trans.
33
149-151
2005
Bacillus subtilis
Zhang, X.; Hu, Y.; Guo, X.; Lescop, E.; Li, Y.; Xia, B.; Jin, C.
The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity
J. Biol. Chem.
281
8296-8304
2006
Bacillus subtilis
Colbert, C.L.; Wu, Q.; Erbel, P.J.; Gardner, K.H.; Deisenhofer, J.
Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation
Proc. Natl. Acad. Sci. USA
103
4410-4415
2006
Bacillus subtilis
Garg, S.K.; Suhail Alam, M.; Soni, V.; Radha Kishan, K.V.; Agrawal, P.
Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase
Protein Expr. Purif.
52
422-432
2007
Mycobacterium tuberculosis
Tanaka, R.; Mizukami, M.; Tokunaga, M.
Novel processing and localization of catA, ccdA associated thiol-disulfide oxidoreductase, in protein hyper-producing bacterium Brevibacillus choshinensis
Protein Pept. Lett.
12
95-98
2005
Brevibacillus choshinensis
Osipova, S.; Permyakov, A.; Mitrofanova, T.; Trufanov, V.; Ermakova, M.; Chistyakova, A.; Pshenichnikova, T.
GSH-dependent protein disulfide oxidoreductase of wheat grain: activity in maturing wheat kernels, and relationship with rheological properties of dough
Cereal Res. Commun.
35
1477-1486
2007
Triticum aestivum
-
Garcin, E.B.; Bornet, O.; Elantak, L.; Vita, N.; Pieulle, L.; Guerlesquin, F.; Sebban-Kreuzer, C.
Structural and mechanistic insights into unusual thiol disulfide oxidoreductase
J. Biol. Chem.
287
1688-1697
2012
Desulfovibrio vulgaris
Davey, L.; Ng, C.K.; Halperin, S.A.; Lee, S.F.
Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii
J. Biol. Chem.
288
16416-16429
2013
Streptococcus gordonii
D'Ambrosio, K.; De Simone, G.; Pedone, E.; Rossi, M.; Bartolucci, S.; Pedone, C.
Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1
Acta Crystallogr. Sect. F
61
335-336
2005
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Chauhan, N.; Hoti, S.L.
Role of cysteine-58 and cysteine-95 residues in the thiol di-sulfide oxidoreductase activity of macrophage migration inhibitory factor-2 of Wuchereria bancrofti
Acta Trop.
153
14-20
2016
Wuchereria bancrofti (A0A088FMA5)
Roszczenko, P.; Grzeszczuk, M.; Kobierecka, P.; Wywial, E.; Urbanowicz, P.; Wincek, P.; Nowak, E.; Jagusztyn-Krynicka, E.
Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231
BMC Microbiol.
15
135
2015
Helicobacter pylori (O25017), Helicobacter pylori ATCC 700392 (O25017)
Davey, L.; Halperin, S.; Lee, S.
Mutation of the thiol-disulfide oxidoreductase SdbA activates the CiaRH two-component system, leading to bacteriocin expression shutdown in Streptococcus gordonii
J. Bacteriol.
198
321-331
2016
Streptococcus gordonii, Streptococcus gordonii SecCR1
Luong, T.; Reardon-Robinson, M.; D.Siegel, S.; Ton-That, H.
Reoxidation of the thiol-disulfide oxidoreductase MdbA by a bacterial vitamin K epoxide reductase in the biofilm-forming actinobacterium Actinomyces oris
J. Bacteriol.
199
e00817
2017
Actinomyces oris (A0A0M3KL32), Actinomyces oris
Reardon-Robinson, M.E.; Osipiuk, J.; Jooya, N.; Chang, C.; Joachimiak, A.; Das, A.; Ton-That, H.
A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence
Mol. Microbiol.
98
1037-1050
2015
Corynebacterium diphtheriae (Q6NFK7), Corynebacterium diphtheriae ATCC 700971 (Q6NFK7)
Grabowska, A.D.; Wywial, E.; Dunin-Horkawicz, S.; Lasica, A.M.; Woesten, M.M.; Nagy-Staron, A.; Godlewska, R.; Bocian-Ostrzycka, K.; Pienkowska, K.; Laniewski, P.; Bujnicki, J.M.; van Putten, J.P.; Jagusztyn-Krynicka, E.K.
Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA
PLoS ONE
9
e106247
2014
Campylobacter jejuni subsp. jejuni
Luong, T.T.; Reardon-Robinson, M.E.; Siegel, S.D.; Ton-That, H.
Reoxidation of the thiol-disulfide oxidoreductase MdbA by a bacterial vitamin K epoxide reductase in the biofilm-forming actinobacterium actinomyces oris
J. Bacteriol.
199
e00817-16
2017
Actinomyces oris (A0A0M3KL32), Actinomyces oris
Zaffagnini, M.; Bedhomme, M.; Marchand, C.H.; Couturier, J.; Gao, X.-H.; Rouhier, N.; Trost, P.; Lemaire, S.D.
Glutaredoxin s12 unique properties for redox signaling
Antioxid. Redox Signal.
16
17-32
2012
Populus sp.
Gao, X.-H.; Zaffagnini, M.; Bedhomme, M.; Michelet, L.; Cassier-Chauvat, C.; Decottignies, P.; Lemaire, S.D.
Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii kinetics and specificity in deglutathionylation reactions
FEBS Lett.
584
2242-2248
2010
Chlamydomonas reinhardtii (A8HN52), Chlamydomonas reinhardtii (A8I7Q4), Chlamydomonas reinhardtii (A8IYH1), Chlamydomonas reinhardtii (A8JHA9)
Zaffagnini, M.; Michelet, L.; Massot, V.; Trost, P.; Lemaire, S.D.
Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin
J. Biol. Chem.
283
8868-8876
2008
Chlamydomonas reinhardtii (A8JH05), Chlamydomonas reinhardtii (A8JHA9)
Soma, S.; Morgada, M.N.; Naik, M.T.; Boulet, A.; Roesler, A.A.; Dziuba, N.; Ghosh, A.; Yu, Q.; Lindahl, P.A.; Ames, J.B.; Leary, S.C.; Vila, A.J.; Gohil, V.M.
COA6 is structurally tuned to function as a thiol-disulfide oxidoreductase in copper delivery to mitochondrial cytochrome c oxidase
Cell Rep.
29
4114-4126.e5
2019
Saccharomyces cerevisiae (Q3E846), Homo sapiens (Q5JTJ3), Saccharomyces cerevisiae ATCC 204508 (Q3E846)
Onder, O.; Verissimo, A.F.; Khalfaoui-Hassani, B.; Peters, A.; Koch, H.G.; Daldal, F.
Absence of thiol-disulfide oxidoreductase DsbA impairs cbb3-type cytochrome c oxidase biogenesis in Rhodobacter capsulatus
Front. Microbiol.
8
2576
2017
Rhodobacter capsulatus (D5AU49), Rhodobacter capsulatus NBRC 16581 (D5AU49), Rhodobacter capsulatus ATCC BAA-309 (D5AU49), Rhodobacter capsulatus SB1003 (D5AU49)
Luong, T.T.; Tirgar, R.; Reardon-Robinson, M.E.; Joachimiak, A.; Osipiuk, J.; Ton-That, H.
Structural basis of a thiol-disulfide oxidoreductase in the hedgehog-forming actinobacterium Corynebacterium matruchotii
J. Bacteriol.
200
e00783-17
2018
Corynebacterium matruchotii, Corynebacterium matruchotii ATCC 14266
Jalal, N.A.; Davey, L.; Halperin, S.A.; Lee, S.F.
Identification of redox partners of the thiol-disulfide oxidoreductase SdbA in Streptococcus gordonii
J. Bacteriol.
201
e00030-19
2019
Streptococcus gordonii (A8AZP5), Streptococcus gordonii Challis (A8AZP5), Streptococcus gordonii ATCC 35105 (A8AZP5), Streptococcus gordonii DL1 (A8AZP5), Streptococcus gordonii V288 (A8AZP5), Streptococcus gordonii BCRC 15272 (A8AZP5), Streptococcus gordonii CH1 (A8AZP5)
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