Crystallization (Comment) | Organism |
---|---|
solution structures of oxidized and reduced mycoredoxin-1 reveal a thioredoxin fold with a putative mycothiol-binding site | Mycolicibacterium smegmatis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | isoform mycoredoxin-1 gets S-mycothiolated on its N-terminal nucleophilic cysteine residue | Mycolicibacterium smegmatis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | isoform mycoredoxin-1 acts as an oxidoreductase exclusively linked to the mycothiol electron transfer pathway and can reduce S-mycothiolated mixed disulfides. Mycoredoxin-1 has a redox potential of -218 mV and hydrogen bonding with neighbouring residues lowers the pKa of its N-terminal nucleophilic cysteine | Mycolicibacterium smegmatis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
mycoredoxin-1 | - |
Mycolicibacterium smegmatis |
General Information | Comment | Organism |
---|---|---|
physiological function | a mycoredoxin-1 deletion strain is more sensitive to oxidative stress than wild-type | Mycolicibacterium smegmatis |