Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.

@article{Mihara1997CysteineSD,
  title={Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.},
  author={H. Mihara and T. Kurihara and T. Yoshimura and K. Soda and N. Esaki},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 36},
  pages={
          22417-24
        }
}
Selenocysteine lyase (EC 4.4.1.16) exclusively decomposes selenocysteine to alanine and elemental selenium, whereas cysteine desulfurase (NIFS protein) of Azotobacter vinelandii acts indiscriminately on both cysteine and selenocysteine to produce elemental sulfur and selenium respectively, and alanine. These proteins exhibit some sequence homology. The Escherichia coli genome contains three genes with sequence homology to nifS. We have cloned the gene mapped at 63.4 min in the chromosome and… Expand
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  • Proceedings of the National Academy of Sciences of the United States of America
  • 2002
TLDR
Evidence is reported that a strain lacking IscS is incapable of synthesizing 5-methylaminomethyl-2-selenouridine and its precursor 5- methylamine-3-thiouridine in tRNA, suggesting that the sulfur atom released from l-cysteine by the action of IscC is incorporated into mnm5s2U. Expand
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cDNA Cloning, Purification, and Characterization of Mouse Liver Selenocysteine Lyase
TLDR
Reverse transcriptase-polymerase chain reaction and Western blot analyses revealed that mSCL is cytosolic and predominantly exists in the liver, kidney, and testis, where mouse selenophosphate synthetase is also abundant, supporting the view that pyridoxal phosphate-dependent and highly specific tol-selenocysteine functions in cooperation with selenoprotein synthesis. Expand
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