Inside Back Cover: Acid–Base Catalyst Discriminates between a Fructose 6‐Phosphate Aldolase and a Transaldolase (ChemCatChem 19/2015)

Publisher： John Wiley & Sons Inc

E-ISSN： 1867-3899|1867-3880|19|3186-3186

ISSN： 1867-3880

Source： CHEMCATCHEM (ELECTRONIC), Vol.1867-3880, Iss.19, 2015-10, pp. : 3186-3186

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Abstract

The Cover shows that a transaldolase scaffold can be used to generate an enzyme with fructose 6‐phosphate aldolase activity. In their Full Paper, A. K. Samland and co‐workers show that a considerable fructose 6‐phosphate aldolase activity was gained by replacing two residues involved in the binding of a catalytic water molecule in the active site of TalB by the corresponding residues in fructose 6‐phosphate aldolase. In addition, these replacements affect the protonation state of the essential lysine residue which was proven by experimental determination of its pKa‐value. More details can be found in the Full Paper by A. K. Samland et al. on page 3140 in Issue 19, 2015 (DOI: 10.1002/cctc.201500478).