Literature DB >> 21562657

Aldolase activity of serum albumins.

Fabio Benedetti1, Federico Berti, Silvia Bidoggia.   

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.

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Year:  2011        PMID： 21562657     DOI： 10.1039/c0ob01219j

Source DB:  PubMed          Journal:  Org Biomol Chem        ISSN： 1477-0520            Impact factor:   3.876


  2 in total

1.  The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme.

Authors:  Joshua Schmidt; Clayton Ehasz; Michael Epperson; Kimberly Klas; Justin Wyatt; Mirko Hennig; Marcello Forconi
Journal:  Org Biomol Chem       Date:  2013-11-05       Impact factor: 3.876

2.  An albumin-derived peptide scaffold capable of binding and catalysis.

Authors:  Immacolata Luisi; Silvia Pavan; Giampaolo Fontanive; Alessandro Tossi; Fabio Benedetti; Adriano Savoini; Elisa Maurizio; Riccardo Sgarra; Daniele Sblattero; Federico Berti
Journal:  PLoS One       Date:  2013-02-22       Impact factor: 3.240
  2 in total

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