Peptide mapping and amino acid sequencing of two catechol 1,2-dioxygenases (CD I1 and CD I2) from Acinetobacter lwoffii K24

Mol Cells. 1997 Oct 31;7(5):635-40.

Abstract

The partial amino acid sequences of two catechol 1,2-dioxygenases (CD I1 and CD I2) from Acinetobacter lwoffii K24 have been determined by analysis of peptides after cleavages with endopeptidase Lys-C, endopeptidase Glu-C, trypsin, and chemicals (cyanogen bromide and BNPS-skatole). They include 248 amino acid sequences (4 fragments) of CD I1 and 211 amino acid sequences (5 fragments) of CD I2. Two enzymes have more than 50% sequence homology with type I catechol 1,2-dioxygenases and less than 30% sequence homology with type II catechol 1,2-dioxygenases. Two enzymes have similar hydropathy profiles in the N-terminal region, suggesting that they have similar secondary structures.

Publication types

  • Comparative Study

MeSH terms

  • Acinetobacter / enzymology*
  • Amino Acid Sequence*
  • Amino Acids / analysis
  • Catechol 1,2-Dioxygenase
  • Dioxygenases*
  • Isoenzymes / chemistry*
  • Molecular Sequence Data
  • Oxygenases / chemistry*
  • Peptide Mapping* / methods
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Amino Acids
  • Isoenzymes
  • Oxygenases
  • Dioxygenases
  • Catechol 1,2-Dioxygenase