1.8.4.15: protein dithiol oxidoreductase (disulfide-forming)
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For detailed information about protein dithiol oxidoreductase (disulfide-forming), go to the full flat file.
Reaction
Synonyms
C. trachomatis disulfide bond protein A, CtDsbA, disulfide oxidoreductase, DsbA, More, MSH-dependent thiol-disulfide reductase, mycothiol-dependent thiol-disulfide reductase, ncgl2478, protein dithiol oxidoreductase, SdbA, Streptococcus disulfide bond protein A, TDOR, thiol-disulfide oxidoreductase
ECTree
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Reference on EC 1.8.4.15 - protein dithiol oxidoreductase (disulfide-forming)
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ireland, P.; McMahon, R.; Marshall, L.; Halili, M.; Furlong, E.; Tay, S.; Martin, J.; Sarkar-Tyson, M.
Disarming Burkholderia pseudomallei Structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo
Antioxid. Redox Signal.
20
606-617
2014
Burkholderia pseudomallei
Zapun, A.; Creighton, T.; Bardwell, J.
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
Biochemistry
32
5083-5092
1993
Escherichia coli
Bardwell, J.; McGovern, K.; Beckwith, J.
Identification of a protein required for disulfide bond formation in vivo
Cell
67
581-589
1991
Escherichia coli
Akiyama, Y.; Kamitani, S.; Kusukawa, N.; Ito, K.
In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product
J. Biol. Chem.
267
22440-22445
1992
Escherichia coli
Bader, M.; Muse, W.; Zander, T.; Bardwell, J.
Reconstitution of a protein disulfide catalytic system
J. Biol. Chem.
273
10302-10307
1998
Escherichia coli
Davey, L.; Ng, C.; Halperin, S.; Lee, S.
Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii
J. Biol. Chem.
288
16416-16429
2013
Streptococcus gordonii, Streptococcus gordonii SecCR1
Christensen, S.; Halili, M.; Strange, N.; Petit, G.; Huston, W.; Martin, J.; McMahon, R.
Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development
PLoS ONE
14
e0222595
2019
Chlamydia trachomatis (G4NNC6), Chlamydia trachomatis, Chlamydia trachomatis A2497 (G4NNC6)
Guddat, L.; Bardwell, J.; Martin, J.
Crystal structures of reduced and oxidized DsbA Investigation of domain motion and thiolate stabilization
Structure
6
757-767
1998
Escherichia coli (P0AEG4)
Liu, Y.; Li, X.; Luo, J.; Su, T.; Si, M.; Chen, C.
A novel mycothiol-dependent thiol-disulfide reductase in Corynebacterium glutamicum involving oxidative stress resistance
3 Biotech
11
372
2021
Corynebacterium glutamicum (Q8NMK6), Corynebacterium glutamicum, Corynebacterium glutamicum LMG 3730 (Q8NMK6), Corynebacterium glutamicum BCRC 11384 (Q8NMK6), Corynebacterium glutamicum ATCC 13032 (Q8NMK6), Corynebacterium glutamicum JCM 1318 (Q8NMK6), Corynebacterium glutamicum NCIMB 10025 (Q8NMK6), Corynebacterium glutamicum DSM 20300 (Q8NMK6)
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