Structural and Enzymatical Comparison of Lignostilbene-α,β-dioxygenase Isozymes, I, II, and III, fromPseudomonas paucimobilisTMY1009

1 January 1993

journal article
Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry

Vol. 57 (6) , 931-934
https://doi.org/10.1271/bbb.57.931

Abstract

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.

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