EC Number |
Title |
Organism |
---|
1.8.5.9 | Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation |
Bacteroides fragilis |
1.8.5.9 | Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation |
Escherichia coli |
1.8.5.9 | Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation |
Mycobacterium tuberculosis |
1.8.5.9 | Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation |
Mycobacterium tuberculosis H37Rv |
1.8.5.9 | Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation |
Bacteroides fragilis NCTC9343 |
1.8.5.9 | Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB |
Escherichia coli |
1.8.5.9 | DsbA-DsbB interaction through their active site cysteines Evidence from an odd cysteine mutant of DsbA |
Escherichia coli |
1.8.5.9 | Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB |
Escherichia coli |
1.8.5.9 | Entropy-driven mechanisms between disulfide-bond formation protein A (DsbA) and B (DsbB) in Escherichia coli |
Escherichia coli |
1.8.5.9 | Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA |
Escherichia coli |