1.8.4.16	a [protein] carrying a disulfide bond + thioredoxin	overall reaction	Escherichia coli	a [protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454236	
1.8.4.16	a [protein] carrying a disulfide bond + thioredoxin	overall reaction	Escherichia coli	a [protein] with reduced L-cysteine residues + thioredoxin disulfide	?	-	454236	
1.8.4.16	a [protein] carrying a disulfide bond + thioredoxin-1	overall reaction	Escherichia coli	a [protein] with reduced L-cysteine residues + thioredoxin-1 disulfide	-	?	454235	
1.8.4.16	a [protein] with reduced L-cysteine residues + thioredoxin disulfide	overall reaction	Escherichia coli	a [protein] carrying a disulfide bond + thioredoxin	-	?	454237	
1.8.4.16	a [protein] with reduced L-cysteine residues + thioredoxin disulfide	overall reaction	Rhodobacter capsulatus	a [protein] carrying a disulfide bond + thioredoxin	-	?	454237	
1.8.4.16	a [protein] with reduced L-cysteine residues + thioredoxin disulfide	overall reaction	Neisseria gonorrhoeae	a [protein] carrying a disulfide bond + thioredoxin	-	?	454237	
1.8.4.16	CQQGFDGTQNSCK peptide containing amide-coupled tetraazacyclododecane-1,4,7,10-tetraacetic acid + GSSG	-	Neisseria gonorrhoeae	?	-	?	455483	
1.8.4.16	human insulin + reduced dithiothreitol	-	Neisseria gonorrhoeae	?	-	?	455775	
1.8.4.16	insulin + dithiothreitol	-	Escherichia coli	reduced insulin + oxidized dithiothreitol	-	?	455792	
1.8.4.16	additional information	electron transfer by the enzyme involves sequential reduction and oxidation of its three structural domains, in which reducing potential is transferred from cytoplasmic thioredoxin to the beta domain, then successively to gamma and alpha, and thence to periplasmic substrates. Formation of a disulfide bond between cysteines 163 and 285 of the beta domain is part of the mechanism of the transmembrane electron transfer by the enzyme	Escherichia coli	?	-	-	89	
1.8.4.16	additional information	the enzyme does not catalyze the reduction of the disulfide of the thioredoxin-like oxidant DsbA	Escherichia coli	?	-	-	89	
1.8.4.16	additional information	the enzyme includes three domains, each containing a pair of cysteine residues that perform a series of disulfide exchange reactions. In the first step, the transmembrane domain accepts electrons from thioredoxin in the cytoplasm; these are then transferred to the periplasmic C-terminal domain and finally to the N-terminal domain, which is also located in the periplasm	Escherichia coli	?	-	-	89	
1.8.4.16	additional information	the enzyme is composed of three domains, each containing two redox-active cysteines. All six of these cysteines are required for enzyme activity. The N-terminal periplasmic domain DsbDalpha directly reduces DsbC. DsbDalpha is then itself reduced by the C-terminal periplasmic domain, DsbDgamma, a thioredoxin-like polypeptide. The resulting oxidized DsbDgamma is reduced by the membrane-embedded DsbDbeta domain that contains eight transmembrane segments. Electrons passed from cytoplasmic thioredoxin 1 restore DsbDbeta to the reduced form, thus allowing it to continue to transfer electrons to DsbDgamma	Escherichia coli	?	-	-	89	
1.8.4.16	additional information	the enzyme transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment	Escherichia coli	?	-	-	89	
1.8.4.16	additional information	the enzyme transports electrons without using a metabolite or a cofactor	Escherichia coli	?	-	-	89	
1.8.4.16	additional information	the periplasmic protein TrbB relies on the enzyme from Escherichia coli for maintenance of its C-X-X-C redox active site motif which is responsible for its enzymatic activity	Escherichia coli	?	-	-	89	
1.8.4.16	[CcmG protein] carrying a disulfide bond + thioredoxin	-	Escherichia coli	[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454698	
1.8.4.16	[CcmG protein] carrying a disulfide bond + thioredoxin	-	Neisseria gonorrhoeae	[CcmG protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454698	
1.8.4.16	[DsbC protein] carrying a disulfide bond + thioredoxin	-	Escherichia coli	[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454709	
1.8.4.16	[DsbC protein] carrying a disulfide bond + thioredoxin	-	Neisseria gonorrhoeae	[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454709	
1.8.4.16	[DsbC protein] carrying a disulfide bond + thioredoxin	-	Escherichia coli	[DsbC] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454710	
1.8.4.16	[DsbC protein] with reduced L-cysteine residues + thioredoxin disulfide	-	Escherichia coli	[DsbC protein] carrying a disulfide bond + thioredoxin	-	?	454711	
1.8.4.16	[DsbE protein] carrying a disulfide bond + thioredoxin	-	Escherichia coli	[DsbE protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454712	
1.8.4.16	[DsbG protein] carrying a disulfide bond + thioredoxin	-	Escherichia coli	[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454713	
1.8.4.16	[DsbG protein] carrying a disulfide bond + thioredoxin	-	Neisseria gonorrhoeae	[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454713	
1.8.4.16	[DsbG protein] with reduced L-cysteine residues + thioredoxin disulfide	-	Escherichia coli	[DsbG protein] carrying a disulfide bond + thioredoxin	-	?	454714	
1.8.4.16	[HelX protein] carrying a disulfide bond + thioredoxin	-	Rhodobacter capsulatus	[HelX protein] with reduced L-cysteine residues + thioredoxin disulfide	-	?	454717	
1.8.4.16	[protein DsbC] carrying a disulfide bond + thioredoxin	-	Neisseria meningitidis	[protein DsbC] with reduced L-cysteine residues + thioredoxin disulfide	-	-	454732	
1.8.4.16	[protein DsbE] carrying a disulfide bond + thioredoxin	-	Neisseria meningitidis	[protein DsbE] with reduced L-cysteine residues + thioredoxin disulfide	-	-	454733	
1.8.4.16	[protein DsbG] carrying a disulfide bond + thioredoxin	-	Neisseria meningitidis	[protein DsbG] with reduced L-cysteine residues + thioredoxin disulfide	-	-	454734