Summary: PLoS Biology | www.plosbiology.org 0663
From the bacterial colonies, each
with a unique cytochrome P450, they
randomly chose almost 1,000 for
detailed analysis. In about half of these,
the protein folded properly and bound
its heme group, despite differing from
the naturally occurring proteins at 70
out of about 460 amino acid positions
on average. Of those that folded
correctly, about three-quarters were
also functionally intact, able to catalyze
reactions similar to those of the native
proteins. Detailed analysis revealed the
contribution to catalytic activity of a
previously unappreciated amino acid
near the enzyme's active site. Some
of the mutants were more resistant to
heat degradation than the originals,
indicating the potential for creating

Source: Arnold, Frances H. - Division of Chemistry and Chemical Engineering, California Institute of Technology

Collections: Chemistry; Biology and Medicine