Activities | Families | Sequences | Fold types | References | Help
B6db references: 15952768

type Journal Article
authors Claus, M.T.; Zocher, G.E.; Maier, T.H.; Schulz, G.E.
title Structure of the O-Acetylserine Sulfhydrylase Isoenzyme CysM from Escherichia coli
journal Biochemistry
sel selected
ui 15952768
year (2005)
volume 44
number 24
pages 8620-6
keywords Adenosine Triphosphate
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.
last changed 2010/11/25 12:24

B6db references