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The Mechanism of Class II, Metal‐Dependent Aldolases

1996; Wiley; Volume: 35; Issue: 19 Linguagem: Inglês

10.1002/anie.199622191

1521-3773

Wolf‐Dieter Fessner, Achim Schneider, Heike A. Held, Gudrun Sinerius, Christiane Walter, Mark S. Hixon, John V. Schloss,

Hemoglobin structure and function

Chelation of the cis-enediolate form of dihydroxyacetone phosphate (see picture on the right) is the key step in the mechanism of action of Zn2+-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 CC bond can now be explained.