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

Gemma L. Holliday, Julia D. Fischer, John B. O. Mitchell, Janet M. Thornton

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3835-3845
Number of pages11
JournalFEBS Journal
Volume278
Issue number20
Early online date13 Jun 2011
DOIs
Publication statusPublished - Oct 2011

Keywords

  • active sites
  • catalysis
  • enzyme
  • evolution
  • MACiE
  • mechanism
  • specificity
  • structure
  • FUNGUS CURVULARIA-INAEQUALIS
  • ACTIVE-SITE
  • CATALYTIC-MECHANISM
  • ORGANIC COFACTORS
  • DATABASE
  • CHLOROPEROXIDASE
  • RESIDUES
  • CLASSIFICATION
  • MACIE
  • IDENTIFICATION

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