Papa's got a brand new tag: advances in identification of proteases and their substrates

Trends Biotechnol. 2005 Feb;23(2):59-64. doi: 10.1016/j.tibtech.2004.12.010.

Abstract

Characterization of proteolytic enzymes and their substrates presents a formidable challenge in the context of biological systems. Despite the fact that an estimated 2% of the human genome codes for proteases, only a small fraction of these enzymes have well-characterized functions. Much of the difficulty in understanding protease biology is a direct result of the complexity of regulation, localization and activation exhibited by this class of enzymes. Here, we focus on several recently developed techniques representing crucial advances toward identification of proteases and their natural substrates.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Electrophoresis, Gel, Two-Dimensional
  • Fluorescent Dyes / chemistry
  • Humans
  • Isotope Labeling
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / metabolism*
  • Proteome / analysis
  • Substrate Specificity

Substances

  • Fluorescent Dyes
  • Proteome
  • Peptide Hydrolases