(July 3, 2015) A
research group at Umeå University has managed to capture and describe a protein
structure that, until now, has been impossible to study. The discovery lays the
base for developing designed enzymes as catalysts to new chemical reactions for
instance in biotechnological applications. The result of the study is published
in the journal Nature Communications.
Enzymes are extraordinary biocatalysts able to speed up the
cellular, chemical reactions several million times. This increase of speed is
completely necessary for all biological life, which would otherwise be limited
by the slow nature of vital chemical reactions. Now, a research group at the
Department of Chemistry has discovered a new aspect in enzymes that, in part,
explains how enzymes manage their tasks with unmatched efficiency and
selectivity.
So-called high-energy states in enzymes are regarded as
necessary for catalysing of chemical reactions. A high-energy level is a
protein structure only occurring temporarily and for a short period of time;
and these factors collaborate until its state becomes invisible to traditional
spectroscopic techniques. The Umeå researchers have managed to find a way to
maintain a high-energy state in the enzyme, adenylate kinase, by mutating the
protein.