Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activity.

@article{Kessler2004Slr0077OS,
  title={Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activity.},
  author={Dorothea Kessler},
  journal={Biochemical and biophysical research communications},
  year={2004},
  volume={320 2},
  pages={
          571-7
        }
}
  • D. Kessler
  • Published 23 July 2004
  • Biology, Medicine
  • Biochemical and biophysical research communications
NifS-like proteins activate sulfur for a variety of biosynthetic purposes. The genome of the cyanobacterium Synechocystis contains 4 nifS-related sequences of which only the slr0077 gene seems to be essential. In this report the heterologous production of the Slr0077 protein, its purification, and catalytic properties are described. Slr0077 produces alanine as well as pyruvate from cyst(e)ine as substrate; the product ratio depends on the redox conditions. Alanine is the typical product of… 
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References

SHOWING 1-10 OF 33 REFERENCES
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
TLDR
It is shown that NIFS is a pyridoxal phosphate-containing homodimer that catalyzes the formation of L-alanine and elemental sulfur by using L-cysteine as substrate, and it is proposed that an enzyme-bound cysteinyl persulfide that requires the release of the sulfur from the substrate L- Cysteine for its formation ultimately provides the inorganic sulfide required for nitrogenase metallocluster formation.
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.
TLDR
Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound Persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly.
Role of a NifS-like protein from the cyanobacterium Synechocystis PCC 6803 in the maturation of FeS proteins.
TLDR
In the presence of Fe(2+), cysteine, and a reductant, the NifS-like protein was able to produce holoferredoxin from apof deferredoxin, and the implications of two different activities for FeS center biosynthesis in Synechocystis are discussed.
Gene Cloning, Purification, and Characterization of Two Cyanobacterial NifS Homologs Driving Iron-Sulfur Cluster Formation
TLDR
The results suggest that SsCsd1 and SSCsd2 facilitate the iron-sulfur cluster assembly by producing inorganic sulfur from L-cysteine, which probably proceeds through a mechanism that is different from that in A. vinelandii.
Assembly of Iron-Sulfur Clusters
TLDR
A very strong selective pressure against the maintenance of A. vinelandii iscS or hscA knock-out mutations is revealed and it is suggested that such mutations are either lethal or highly deleterious.
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product.
TLDR
The nifS gene product is a pyridoxal phosphate binding enzyme that catalyzes the desulfurization of L-cysteine to yield L-alanine and sulfur in Azotobacter vinelandii and it is suggested that NIFS participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation.
Cysteine Sulfinate Desulfinase, a NIFS-like Protein ofEscherichia coli with Selenocysteine Lyase and Cysteine Desulfurase Activities
TLDR
The Escherichia coli genome contains three genes with sequence homology to nifS, and a new enzyme catalyzes the removal of elemental sulfur and selenium atoms froml-cysteine, l-cystine,l-selenocysteine; and l-alanine, which is distinct from A. vinelandii NIFS in this respect.
Snapshots of the Cystine Lyase C-DES during Catalysis
TLDR
The combined results allow a catalytic mechanism to be proposed involving interactions between cystine and the active site residues Arg-360, Arg-369, and Trp-251*; these residues reorient during the β-elimination reaction, leading to the formation of a hydrophobic pocket that stabilizes the enolimine tautomer of the aminoacrylate and the cysteine persulfide product.
A Novel l-Cysteine/Cystine C-S-Lyase Directing [2Fe-2S] Cluster Formation of SynechocystisFerredoxin*
TLDR
A function-based identification of a cysteine/cystine C-S-lyase as a participant in ferredoxin Fe-S cluster formation is provided and an increased reactivity was found with cystine instead of Cysteine, which should yield cysteined persulfide as the primary product.
Bacterial cysteine desulfurases: their function and mechanisms
TLDR
Enzymes capable of providing a variety of biosynthetic pathways for sulfur/selenium-containing biomolecules are probably applicable to the production of cofactors and the bioconversion of useful compounds.
...
1
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