Peptide mapping and amino acid sequencing of two catechol 1,2-dioxygenases (CD I1 and CD I2) from Acinetobacter lwoffii K24.
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.
Kim
S I
SI
Biomolecule Research Group, Korea Basic Science Institute, Taejon.
Ha
K S
KS
D000150:Acinetobacter / Q000201:enzymology*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D050548:Catechol 1,2-Dioxygenase; D049308:Dioxygenases; D007527:Isoenzymes / Q000737:chemistry*; D008969:Molecular Sequence Data; D010105:Oxygenases / Q000737:chemistry*; D010449:Peptide Mapping / Q000379:methods; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D000596:Amino Acids; D007527:Isoenzymes; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase