desulfurase

de·sul·fur·ase

(dē-sŭl′fə-rās′, -rāz′)
n.
An enzyme that catalyzes the removal of sulfur, usually as hydrogen sulfide, from organic compounds. Also called desulfhydrase.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.
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The expression levels of cysteine desulfurase of variety KT30 and variety Defumm-8 first decreased and then increased with the increasing Se concentration; however, expression levels of Se were lower than the control, and expression levels of Se in leaves of variety Luobeiqi increased.
Many studies have proven that cysteine desulfurase (CysD), S-adenosyl-l-Met:l-Met S-methyltransferase (MMT) (Berken et al., 2002), serine acetyltransferase (SAT) (Van Hoewyk et al., 2008), and SeCys methyltransferase (SMT) were also the main genes for plant metabolism and Se accumulation (Berken et al., 2002).
Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities.
Cysteine desulfurase (CDS; EC 2.8.1.7) is an important enzyme for the assimilatory sulfur metabolism, where it performs the following desulfuration reaction [3, 6, 7] (Scheme 1):
Richhardt et al., "Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae," The Journal of Biological Chemistry, vol.
Dean, "Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis," Proceedings of the National Academy of Sciences of the United States of America, vol.
Altegoer et al., "Crystal structure of Bacillus subtilis cysteine desulfurase SufS and its dynamic interaction with frataxin and scaffold protein SufU," PLoS One, vol.
Bollinger Jr, "Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp.
Park, "Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration," The Journal of Biological Chemistry, vol.
Esaki, "Bacterial cysteine desulfurases: their function and mechanisms," Applied Microbiology and Biotechnology, vol.
This result built upon previous reports linking LYRM4 (also known as ISD11) as a binding partner to NFS1 cysteine desulfurase (NFS1), a sulfur donor in ISC biogenesis (Shi et al.
falciparum, the protein SufS and its partner SufE were found exclusively in the apicoplast and SufS was shown to have cysteine desulfurase activity in a complementation assay.