Structural and enzymatical comparison of lignostilbene-alpha,beta-dioxygenase isozymes, I, II, and III, from Pseudomonas paucimobilis TMY1009.
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas paucimobilis TMY1009 were separated on QAE-Toyopearl chromatography. All active fractions were further chromatographed on DEAE-Toyopearl, Butyl-Toyopearl, and Sephacryl S-300 columns. Then the isozymes I, II, and III were purified homogeneously. All three isozymes consisted of two subunits with the same mol. mass. According to the N-terminal amino acid sequences up to 25 residues of these three isozymes and the reversed-phase HPLC patterns of peptidase-digested them, it was found that LSD-I, II, and III consisted of alpha alpha, alpha beta, and beta beta subunits, respectively. They showed different specificities for several substrates that are stilbene and styrene derivatives.
Kamoda
S
S
Department of Forest Products, Faculty of Agriculture, University of Tokyo, Japan.
Saburi
Y
Y
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D049308:Dioxygenases; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010105:Oxygenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
D007527:Isoenzymes; D010105:Oxygenases; D049308:Dioxygenases; C069684:lignostilbene-alpha,beta-dioxygenase