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Fructose 1,6‐Bisphosphate Aldolase from Staphylococcus carnosus : Overexpression, Structure Prediction, Stereoselectivity, and Application in the Synthesis of Bicyclic Sugars
Author(s) -
Zannetti Maria Teresa,
Walter Christiane,
Knorst Marion,
Fessner WolfDieter
Publication year - 1999
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/(sici)1521-3765(19990604)5:6<1882::aid-chem1882>3.0.co;2-c
Subject(s) - aldolase a , bicyclic molecule , stereoselectivity , fructose bisphosphate aldolase , stereochemistry , enzyme , chemistry , fructose , biochemistry , catalysis
The unusually stable fructose 1,6‐bisphosphate aldolase from Staphylococcus carnosus (FruA sca ) was overproduced in E. coli . An α = β ‐barrel structure and highly conserved active site was inferred from sequence analysis in comparison to known class I aldolases. A preparative study with generic aliphatic and hydroxylated aldehydes confirmed a high level of stereoselectivity, and thus a functional equivalence of the Staphylococcus enzyme to the commercial rabbit muscle aldolase for asymmetric synthesis. Despite their high enzyme cross‐linking reactivity, glutardialdehyde derivatives could be converted by the Staphylococcus aldolase to give novel bicyclic sugars.