|
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 |
Activity |
2.5.1.47 |
Family |
2.5.1.47 |
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 |
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