• Open Access

Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis


G. L. Holliday, EMBL-EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SD, UK
Fax: +44 1223 494496
Tel: +44 1223 492535
E-mail: gemma@ebi.ac.uk
Website: http://www.ebi.ac.uk/thornton-srv/databases/MACiE/


Enzymes are basically composed of 20 naturally occurring amino acids, yet they catalyse a dizzying array of chemical reactions, with regiospecificity and stereospecificity and under physiological conditions. In this review, we attempt to gain some understanding of these complex proteins, from the chemical versatility of the catalytic toolkit, including the use of cofactors (both metal ions and organic molecules), to the complex mapping of reactions to proteins (which is rarely one-to-one), and finally the structural complexity of enzymes and their active sites, often involving multidomain or multisubunit assemblies. This work highlights how the enzymes that we see today reflect millions of years of evolution, involving de novo design followed by exquisite regulation and modulation to create optimal fitness for life.