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Literature summary for 2.8.4.3 extracted from
- Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB (2013), J. Biol. Chem., 288, 14200-14211.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AEI1 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | enzym MiaB physically interacts with monothiol glutaredoxin, GrxD, and the FeS carrier protein NfuA, with MiaB with affinities compatible with an in vivo function. NfuA is able to transfer its cluster in vitro to MiaB, whereas GrxD is unable to do so. Cells lacking both GrxD and NfuA display a severe defect in in vivo MiaB activity | Escherichia coli |
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