EC Number   |
General Information |
Reference |
|---|
    2.8.1.7 | malfunction |
deleting the enzyme renders the cells microaerophilic and hypersensitive to oxidative stress. Moreover, the deletion mutant shows impaired Fe-S cluster-dependent enzyme activity |
-, 737643 |
| 2.8.1.7 | malfunction |
enzyme mutation leads to a defect in Fe-S synthesis |
739016 |
| 2.8.1.7 | malfunction |
the disruption of the csd gene of Thermococcus kodakarensis, a facultative elemental sulfur-reducing hyperthermophilic archaeon, confers a growth defect evident only in the absence of sulfur. Growth can be restored by the addition of sulfur, but not sulfide |
728340 |
| 2.8.1.7 | metabolism |
SufS protein physically interacts with the Anabaena sulfur acceptor E protein. In the presence of the Anabaena sulfur acceptor E protein, the catalytic efficiency increases 10fold. For sulfur mobilization, the Anabaena sulfur acceptor E protein partners only SufS and not other cysteine desulfurases from Nostoc sp. The conserved cysteine of the SufS or the Anabaena sulfur acceptor E protein is essential for activity but not for their physical association |
760523 |
| 2.8.1.7 | metabolism |
the cysteine desulfurase Nfs1 is required for the increased protein Isu stability occurring after disruption of cluster formation on or transfer from protein Isu. Physical interaction between the Isu and Nfs1 proteins, not the enzymatic activity of Nfs1, is the important factor in increased stability |
726381 |
| 2.8.1.7 | metabolism |
the enzyme is the sulfur donor for M molybdenum cofactor biosynthesis. The enzyme is able to transfer sulfur to the C-terminal domain of MOCS3, a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation |
726333 |
| 2.8.1.7 | metabolism |
the enzyme plays an important role in environmental adaptation of the hyperthermophilic archaeon |
728340 |
| 2.8.1.7 | physiological function |
cysteine desulfurase (IscS, EC 2.8.1.7), not 3-MST, is the primary source of endogenous H2S in Escherichia coli under anaerobic conditions. A significant decrease in H2S production under anaerobic conditions is observed in Escherichia coli upon deletion of IscS, but not in 3-MST-deficient bacteria. The H2S-producing activity of recombinant IscS using L-cysteine as a substrate exhibits an approximately 2.6fold increase in the presence of dithiothreitol. The activity of IscS is regulated under the different redox conditions and the midpoint redox potential is -329 mV. H2S production from IscS is regulated under oxidative and reductive stress. A mutant strain lacking a chromosomal copy of the IscS-encoding gene iscS shows significant growth defects and low levels of ATP under both aerobic and anaerobic conditions |
-, 761145 |
| 2.8.1.7 | physiological function |
deletion of isoform causes a severe growth defect in the presence of 2% oxygen. The mutation delays colonization in a conventional mouse model of Clostridioides difficile infection and fails to colonize in a germfree model, which has higher intestinal oxygen levels |
-, 761245 |
| 2.8.1.7 | physiological function |
ferredoxins FDX1 and FDX2 in both their reduced and oxidized states interact with the protein complex responsible for mitochondrial iron-sulfur cluster assembly, which contains cysteine desulfurase (NFS1), ISD11 (LYRM4), and acyl carrier protein (Acp). Reduced FDX1 and FDX2 each donate electrons to the cysteine desulfurase complex in vitro and facilitate iron-sulfur cluster assembly. Ferredoxin Both FDX1 and FDX2 stimulate cysteine desulfurase activity. FDX2 binds more tightly to the cysteine desulfurase complex than FDX1 does. The reduced form of each ferredoxin becomes oxidized in the presence of the cysteine desulfurase complex when L-cysteine is added, leading to its conversion to L-alanine and the generation of sulfide |
760587 |
