Cysteine desulfurase: Difference between revisions
Content deleted Content added
m →References: Journal cites (journal names):, using AWB (8060) |
|||
| Line 26: | Line 26: | ||
* {{cite journal | author = Mihara H, Esaki N | date = 2002 | title = Bacterial cysteine desulfurases: their function and mechanisms | journal = Appl. Microbiol. Biotechnol. | volume = 60 | pages = 12–23 | pmid = 12382038 | doi = 10.1007/s00253-002-1107-4 | issue = 1-2 }} |
* {{cite journal | author = Mihara H, Esaki N | date = 2002 | title = Bacterial cysteine desulfurases: their function and mechanisms | journal = Appl. Microbiol. Biotechnol. | volume = 60 | pages = 12–23 | pmid = 12382038 | doi = 10.1007/s00253-002-1107-4 | issue = 1-2 }} |
||
* {{cite journal | author = Frazzon J, Dean DR | date = 2003 | title = Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry | journal = Curr. Opin. Chem. Biol. | volume = 7 | pages = 166–73 | pmid = 12714048 | doi = 10.1016/S1367-5931(03)00021-8 | issue = 2 }} |
* {{cite journal | author = Frazzon J, Dean DR | date = 2003 | title = Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry | journal = Curr. Opin. Chem. Biol. | volume = 7 | pages = 166–73 | pmid = 12714048 | doi = 10.1016/S1367-5931(03)00021-8 | issue = 2 }} |
||
{{Sulfur-containing group transferases}} |
|||
{{transferase-stub}} |
{{transferase-stub}} |
||
Revision as of 03:14, 9 January 2016
| cysteine desulfurase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.8.1.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a cysteine desulfurase (EC 2.8.1.7) is an enzyme that catalyzes the chemical reaction
- L-cysteine + [enzyme]-cysteine L-alanine + [enzyme]-S-sulfanylcysteine
Thus, the two substrates of this enzyme are L-cysteine and [[[enzyme]-cysteine]], whereas its two products are L-alanine and [[[enzyme]-S-sulfanylcysteine]].
This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include IscS, NIFS, NifS, SufS, and cysteine desulfurylase. This enzyme participates in thiamine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T3I.
References
- Zheng L, White RH, Cash VL, Jack RF, Dean DR (1993). "Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 90 (7): 2754–8. doi:10.1073/pnas.90.7.2754. PMC 46174. PMID 8464885.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Mihara H, Esaki N (2002). "Bacterial cysteine desulfurases: their function and mechanisms". Appl. Microbiol. Biotechnol. 60 (1–2): 12–23. doi:10.1007/s00253-002-1107-4. PMID 12382038.
- Frazzon J, Dean DR (2003). "Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry". Curr. Opin. Chem. Biol. 7 (2): 166–73. doi:10.1016/S1367-5931(03)00021-8. PMID 12714048.