Structural highlights
Function
[CYSM_ECOLI] Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The enzyme O-acetylserine sulfhydrylase participates in the biosynthesis of l-cysteine in bacteria and plants. The structure of isoenzyme B (CysM) from Escherichia coli was established in a hexagonal crystal form at 2.7 A resolution (wild-type) and in a merohedrally twinned tetragonal crystal form at 2.1 A resolution (surface mutant). Structural superpositions revealed the variations with respect to isoenzyme A (CysK) and explained the different substrate specificities. A geometric model of the reaction catalyzed by CysM is proposed. Both isoenzymes are used for the production of l-amino acid derivatives as building blocks for the synthesis of peptides and peptidomimetic drugs. Since the structure of CysM revealed a remarkable main chain variation at the active center, it constitutes a further starting point for engineering mutants with novel substrate specificities.
Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli.,Claus MT, Zocher GE, Maier TH, Schulz GE Biochemistry. 2005 Jun 21;44(24):8620-6. PMID:15952768[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Claus MT, Zocher GE, Maier TH, Schulz GE. Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli. Biochemistry. 2005 Jun 21;44(24):8620-6. PMID:15952768 doi:10.1021/bi050485+
