Aldolase activity of serum albumins

Fabio Benedetti; Federico Berti; Silvia Bidoggia

doi:10.1039/C0OB01219J

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Organic & Biomolecular Chemistry

Issue 12, 2011

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Aldolase activity of serum albumins

Fabio Benedetti , Federico Berti and Silvia Bidoggia

Org. Biomol. Chem., 2011,9, 4417-4420

DOI: 10.1039/C0OB01219J
Received 20 Dec 2010, Accepted 11 Apr 2011
First published on the web 12 Apr 2011

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Abstract
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Bovine and human serum albumins catalyze the aldol reaction of aromatic aldehyedes and acetone, with saturation kinetics and moderate and opposite enantioselectivity. The reaction occurs at the binding site in domain IIa, and is inhibited by warfarin. Kinetic data are consistent with an enamine mechanism. The activity is conserved in a 103 aminoacid peptide derived from the albumin sequence.