PMID:15952768
| Citation |
Claus, MT, Zocher, GE, Maier, TH and Schulz, GE (2005) Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli. Biochemistry 44:8620-6 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1021/bi050485+ |
| Keywords |
Amino Acid Sequence; Crystallography, X-Ray; Cysteine Synthase/chemistry; Cysteine Synthase/isolation & purification; Cysteine Synthase/metabolism; Dimerization; Escherichia coli/enzymology; Isoenzymes/chemistry; Isoenzymes/isolation & purification; Isoenzymes/metabolism; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Weight; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Salmonella typhimurium/enzymology; Sequence Homology, Amino Acid |
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