Cysteine desulfurase

Attaches to apoNifK2D2 to assist FeMoco insertion in Klebsiella pneumoniae-, Em equivalent protein inAzotobacter vinelandii is y Cysteine desulfurase... 

Tantalean JC, MA Araya. CP Saavedra, DE Fuementes, JM Perez, IL Calderon, P Youderian, CC Vasquez (2003) The Geobacillus stearothermophilus V iscS gene, encoding cysteine desulfurase, confers resistance to potassium tellurite in Escherichia coli. J Bacteriol 185 5831-5837. 

Another enzyme, cysteine desulfurase, converts L-cysteine to L-alanine and a sulfane sulfur - a chain of divalent sulfur atoms. A protein-bound cysteine persulfide is formed on a conserved cysteine residue. Such enzymes have important roles in the biosynthesis of Fe-S clusters and sulfur-containing cofactors.9... 

Schwartz CJ, Djaman O, Imlay JA, Kiley PJ. 2000. The cysteine desulfurase, IscS, has a major role in in vivo Ee-S cluster formation in Escherichia coli. Proc Natl Acad Sci USA 97 9009-14. 

The current model for FeS cluster formation is based mainly on studies of Saccharomyces and human cells (reviewed in bill and Muhlenhoff 2006 Rouault and Tong 2005 Tachezy and Dolezal 2007). The pyridoxal phosphate-dependent cysteine desulfurase (IscS) is a central component catalyzing the production of sulfur from -cysteine (Ii et al. 1999 Schwartz et al. 2000). The released sulfur is transferred to IscU which constitutes a scaffold for the formation of a transient FeS cluster (Agar et al. 2000). Subsequently, the FeS cluster is transferred to mitochondrial apoproteins with the assistance of the... 

Emelyanov VV (2003) Phylogenetic affinity of a Giardia lamblia cysteine desulfurase conforms to canonical pattern of mitochondrial ancestry. FEMS Microbiol Lett 226 257-266... 

Yet another enzyme able to release or transfer sulfur in the S° oxidation state is the PLP-dependent cysteine desulfurase that is encoded by the nifS gene of the nitrogenase gene cluster shown in Fig. 24-4. 

Fig. 4.13). The active form of MoCo requires a third sulfur hgand, which, in the case of nitrate reductase (NR) and sulfite oxidase (SO), is supplied by a cysteine residue of the apo-protein. For xanthine dehydrogenase (XDH), and aldehyde oxidase (AO), the third sulfur ligand is derived from cysteine and is generated as a persulfide by a PLP-dependent cysteine desulfurase, analogous to that found in Fe—S cluster formation. This is then transferred to MoCo, and occupies a similar position to the terminal sulfur in NR and SO. ° It is interesting to note that the formation of active Mo-enzymes depends not only on the availability of Mo, but also requires both Fe and Cu. 

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