Engineered metalloregulation in enzymes

Trends Biochem Sci. 1992 Mar;17(3):100-4. doi: 10.1016/0968-0004(92)90245-5.

Abstract

Protein engineering of metal-dependent enzyme activity is now possible due to the wealth of information available about metalloproteins. The results emerging from these studies provide insight into our understanding of the chemistry of metals in macromolecular environments as well as the biology of metal-protein interactions.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Copper / chemistry
  • Histidine / chemistry
  • Metalloproteins / chemistry*
  • Metalloproteins / genetics
  • Molecular Sequence Data
  • Peptidyl-Dipeptidase A / chemistry*
  • Peptidyl-Dipeptidase A / genetics
  • Protein Engineering
  • Sequence Alignment
  • Structure-Activity Relationship
  • Trypsin / chemistry*
  • Trypsin / genetics
  • Zinc / chemistry

Substances

  • Metalloproteins
  • Histidine
  • Copper
  • Peptidyl-Dipeptidase A
  • Trypsin
  • Zinc