Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1

Annu Rev Microbiol. 2004:58:555-85. doi: 10.1146/annurev.micro.57.030502.090927.

Abstract

The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

Publication types

  • Review

MeSH terms

  • Acinetobacter / enzymology
  • Amino Acid Sequence
  • Catechols / metabolism*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Point Mutation
  • Protein Conformation
  • Protocatechuate-3,4-Dioxygenase / chemistry*
  • Protocatechuate-3,4-Dioxygenase / genetics
  • Protocatechuate-3,4-Dioxygenase / metabolism
  • Pseudomonas / enzymology
  • Sequence Alignment

Substances

  • Catechols
  • Protocatechuate-3,4-Dioxygenase