| Name | cysteine desulfurase |
|---|---|
| Synonyms | Cysteine desulfurase; HUSSY 08; IscS; NFS 1; NFS1; NFS1 nitrogen fixation 1 (S. cerevisiae); NFS1 nitrogen fixation 1 homolog (S. cerevisiae); NFS1 nitrogen fixation 1 isoform a variant… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19946146 | Zhang W, Urban A, Mihara H, Leimkuhler S, Kurihara T, Esaki N: IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of in Escherichia coli. J Biol Chem. 2010 Jan 22;285(4):2302-8. Epub 2009 Nov 29. |
169(2,2,3,4) | Details |
| 20213443 | Cartini F, Remelli W, Dos Santos PC, Papenbrock J, Pagani S, Forlani F: Mobilization of sulfane sulfur from desulfurases to the Azotobacter vinelandii sulfurtransferase RhdA. Amino Acids. 2010 Mar 7. Mobilization of the L: - sulfur for the persulfuration of the rhodanese of Azotobacter vinelandii, RhdA, can be mediated by the A. vinelandii desulfurases, IscS and NifS. |
81(1,1,1,1) | Details |
| 19722697 | Liu Y, Cowan JA: -sulfur cluster biosynthesis: characterization of a molten globule domain in human NFU. Biochemistry. 2009 Aug 11;48(31):7512-8. This C-terminal domain contains a pair of redox active cysteines and demonstrates thioredoxin-like activity by both binding to and mediating persulfide bond cleavage of sulfur-loaded IscS, the sulfide donor for [2Fe-2S] cluster assembly on ISU-type scaffold proteins. |
31(0,1,1,1) | Details |
| 19454487 | Shi Y, Ghosh MC, Tong WH, Rouault TA: Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum Mol Genet. 2009 Aug 15;18(16):3014-25. Epub 2009 May 18. Here, we have cloned and characterized human ISD11 and shown that human ISD11 forms a stable complex in vivo with the human cysteine desulfurase (ISCS), which generates the inorganic sulfur needed for Fe-S protein biogenesis. |
31(0,1,1,1) | Details |
| 19968861 | Poliak P, Van Hoewyk D, Obornik M, Zikova A, Stuart KD, Tachezy J, Pilon M, Lukes J: Functions and cellular localization of cysteine desulfurase and selenocysteine lyase in Trypanosoma brucei. FEBS J. 2010 Jan;277(2):383-93. Epub 2009 Dec 7. Nfs-like proteins have cysteine desulfurase (CysD) activity, which removes sulfur (S) from and provides S for iron-sulfur cluster assembly and the thiolation of tRNAs. |
7(0,0,1,2) | Details |
| 19720832 | Naamati A, Regev-Rudzki N, Galperin S, Lill R, Pines O: Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J Biol Chem. 2009 Oct 30;284(44):30200-8. Epub 2009 Aug 31. Nfs1 is a highly conserved mitochondrial cysteine desulfurase that participates in iron-sulfur cluster assembly as a sulfur donor. |
6(0,0,1,1) | Details |
| 20064440 | Hoff KG, Culler SJ, Nguyen PQ, McGuire RM, Silberg JJ, Smolke CD: In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2. . Chem Biol. 2009 Dec 24;16(12):1299-308. In addition, we find that maximal fluorescence in the cytosol of mammalian cells requires the iron-sulfur cluster assembly proteins ISCU and NFS1. |
6(0,0,1,1) | Details |
| 20054882 | Trotter V, Vinella D, Loiseau L, Ollagnier de Choudens S, Fontecave M, Barras F: The CsdA desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol. 2009 Dec;74(6):1527-42. Escherichia coli contains three such enzymes, IscS, SufS and CsdA. |
2(0,0,0,2) | Details |
| 19883076 | Behshad E, Bollinger JM Jr: Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. Biochemistry. 2009 Dec 22;48(50):12014-23. |
2(0,0,0,2) | Details |
| 20097860 | Albrecht AG, Netz DJ, Miethke M, Pierik AJ, Burghaus O, Peuckert F, Lill R, Marahiel MA: SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis. J Bacteriol. 2010 Mar;192(6):1643-51. Epub 2010 Jan 22. Further, we show that apo-SufU is an activator of the cysteine desulfurase SufS by enhancing its activity about 40-fold in vitro. Bacteria use three distinct systems for iron-sulfur (Fe/S) cluster biogenesis: the ISC, SUF, and NIF machineries. |
2(0,0,0,2) | Details |
| 19798741 | Hanzelmann P, Dahl JU, Kuper J, Urban A, Muller-Theissen U, Leimkuhler S, Schindelin H: Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains. Protein Sci. 2009 Dec;18(12):2480-91. Rhodaneses/sulfurtransferases are ubiquitous enzymes that catalyze the transfer of sulfane sulfur from a donor molecule to a thiophilic acceptor via an active site that is modified to a persulfide during the reaction. In vitro YnjE can be efficiently persulfurated by the cysteine desulfurase IscS. |
1(0,0,0,1) | Details |