Cutinases are bacterial and fungal enzymes that catalyze the hydrolysis of natural cutin,
a three-dimensional inter-esterified polyester with epoxy-hydroxy fatty acids with chain lengths
between 16 and 18 carbon atoms. Due to their ability to accept long chain substrates, cutinases are also
effective in catalyzing in vitro both the degradation and synthesis of several synthetic polyesters and
polyamides. Here, we present a bioinformatics study that intends to correlate the structural features
of cutinases with their catalytic properties to provide rational basis for their effective exploitation,
particularly in polymer synthesis and biodegradation. The bioinformatics study used the BioGPS
method (Global Positioning System in Biological Space) that computed molecular descriptors based
on Molecular Interaction Fields (MIFs) described in the GRID force field. The information was
used to generate catalophores, spatial representations of the ability of each enzymatic active site
to establish hydrophobic and electrostatic interactions. These tools were exploited for comparing
cutinases to other serine-hydrolases enzymes, namely lipases, esterases, amidases and proteases,
and for highlighting differences and similarities that might guide rational engineering strategies.
Structural features of cutinases with their catalytic properties were correlated. The “catalophore” of
cutinases indicate shared features with lipases and esterases.
