Issue 12, 2011
From the journal:

Organic & Biomolecular Chemistry

Aldolase activity of serum albumins†

Fabio Benedetti,a   Federico Berti*a  and  Silvia Bidoggiaa  

* Corresponding authors

a Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via Giorgieri 1, (Italy)
E-mail: fberti@units.it
Fax: (+39) 040-558-2402

Abstract

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.

Graphical abstract: Aldolase activity of serum albumins

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Article information

DOI
https://doi.org/10.1039/C0OB01219J
Article type
Communication
Submitted
20 Dec 2010
Accepted
11 Apr 2011
First published
12 Apr 2011

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

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Aldolase activity of serum albumins

F. Benedetti, F. Berti and S. Bidoggia, Org. Biomol. Chem., 2011, 9, 4417 DOI: 10.1039/C0OB01219J

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