CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Cysteine desulfurase

Enzyme Information

2.8.1.7
Cysteine desulfurase.
based on mapping to UniProt P77444
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
-!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
4.4.1.16
Selenocysteine lyase.
based on mapping to UniProt P77444
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.
-!- Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. -!- The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7).

UniProtKB Entries (1)

P77444
SUFS_ECOLI
Escherichia coli K-12
Cysteine desulfurase

PDB Structure

PDB 5DB5
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21
Arbing, M.A., Shin, A., Koo, C.W., Medrano-Soto, A., Eisenberg, D.
To Be Published