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Ostensible Enzyme Promiscuity: Alkene Cleavage by Peroxidases
Author(s) -
Mutti Francesco G.,
Lara Miguel,
Kroutil Markus,
Kroutil Wolfgang
Publication year - 2010
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201002265
Subject(s) - moiety , hemin , chemistry , peroxidase , stereochemistry , enzyme , alkene , reactivity (psychology) , active site , catalysis , cleavage (geology) , heme , organic chemistry , biology , medicine , paleontology , alternative medicine , pathology , fracture (geology)
Enzyme promiscuity is generally accepted as the ability of an enzyme to catalyse alternate chemical reactions besides the ‘natural’ one. In this paper peroxidases were shown to catalyse the cleavage of a CC double bond adjacent to an aromatic moiety for selected substrates at the expense of molecular oxygen at an acidic pH. It was clearly shown that the reaction occurs due to the presence of the enzyme; furthermore, the reactivity was clearly linked to the hemin moiety of the peroxidase. Comparison of the transformations catalysed by peroxidase and by hemin chloride revealed that these two reactions proceed equally fast; additional experiments confirmed that the peptide backbone was not obligatory for the reaction and only a single functional group of the enzyme was required, namely in this case the prosthetic group (hemin). Consequently, we propose to define such a promiscuous activity as ‘ostensible enzyme promiscuity’. Thus, we call an activity that is catalysed by an enzyme ‘ostensible enzyme promiscuity’ if the reactivity can be tracked back to a single catalytic site, which on its own can already perform the reaction equally well in the absence of the peptide backbone.