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