Premium
The Mechanism of Class II, Metal‐Dependent Aldolases
Author(s) -
Fessner WolfDieter,
Schneider Achim,
Held Heike,
Sinerius Gudrun,
Walter Christiane,
Hixon Mark,
Schloss John V.
Publication year - 1996
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199622191
Subject(s) - chemistry , ligand (biochemistry) , stereochemistry , mechanism (biology) , chelation , dihydroxyacetone , mechanism of action , crystallography , combinatorial chemistry , biochemistry , organic chemistry , physics , receptor , quantum mechanics , glycerol , in vitro
Chelation of the cis‐enediolate form of dihydroxyacetone phosphate (see picture on the right) is the key step in the mechanism of action of Zn 2+ ‐dependent aldolases. This proposal is derived from inhibition studies with model compounds for both ground and transition states and from an X‐ray structure determination of a protein—ligand complex. The high degree of asymmetric induction occurring at both termini of the newly formed CC bond can now be explained.