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KMID : 0578319970070050635
Molecules and Cells
1997 Volume.7 No. 5 p.635 ~ p.640
Peptide Mapping and amino Acid Sequencing of two Catechol 1,2-Dioxygenases (CD I1 and CD I2) from Acinetobacter lwoffii K24
Kim Seung-Il

Ha Kwon-Soo
Abstract
The partial amino acid sequences of two catechol 1,2-dioxygenases (CD I©ûand CD I©ü) from Acinetobacter lwoff6.u¡¥ K24 have been determined by analysis of peptides after cleavages with endopeptidase Lys-C, endopeptidase GIu-C, trypsin, and chemicals (cyanogen bromide and BNPS-skatole). They include 248 amino acid sequences ( 4 fragments) of CD I©ûand 211 anino acid sequences (5 fragments)of CD I©û. 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 regionk, suggesting that they have similar secondary structures.
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