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2.8.1.7 |
Description |
Cysteine desulfurase |
Alternative names |
IscS; NifS; SufS; cysteine desulfurylase. |
Catalyzed reaction |
L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine |
Cofactor |
Pyridoxal-phosphate. |
Comments |
The reaction shown is the first part of a catalytic process, which is completed by passing on the protein-bound sulfur to other acceptors. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) and functions by mobilizing sulfur. |
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Cysteine desulfurases are phylogenetically and functionally related to enzymes such as selenocystine lyases (C-DES type). They are also phylogenetically related to selenocysteine lyases (EC 4.4.1.16), and often show some selenocysteine lyase activity.
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Diseases |
Classical xanthinuria type II |
PDB |
1ECX; 1P3W; 6M4J; |
Organisms |
-Eubacteria -Archea -Plants -Metazoa -Human |
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Links |
Enzyme (activities) 2.8.1.7
BRENDA (activities) 2.8.1.7
KEGG (pathways) 2.8.1.7
PLPMDB (PLP mutants) 2.8.1.7
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References |
Articles on 2.8.1.7 |
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last changed |
2020/05/08 01:58 |
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