Disease relevance of Syringaldazine

• The encoded gene product was expressed in Escherichia coli and showed laccase-like activity, oxidising 2,2'-azino-bis(3-ethylbenz-thiazoline-6-sulfonic acid), 2,6-dimethoxyphenol and syringaldazine (SGZ) [1].

High impact information on Syringaldazine

• Specific activities of MtL mutants toward 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) and syringaldazine indicate that substrate specificity was not changed by the introduced mutations [2].
• Peroxidase activity (EC 1.11.1.7) towards phenolic substrates, i.e. pyrogallol, syringaldazine and guaiacol, and ascorbate peroxidase activity (EC 1.11.1.11) were analyzed in embryo axes of Lupinus luteus L. cv. Polo cultured on Heller medium for 96h after inoculation with the necrotrophic fungus Fusarium oxysporum f.sp [3].
• The pH optimum of Lbh1 with SGZ is 7.5-8 (at 45 degrees C) and the laccase activity is stimulated rather than inhibited by chloride [1].
• AIMS: Enzyme kinetics of purified laccases from six different Pleurotus ostreatus strains were determined in the oxidation of syringaldazine, guaiacol and ABTS [4].
• This result, coupled with the fact that syringaldazine served as the substrate for the insoluble enzyme, confirmed that cuticular phenoloxidase is of the "laccase" type [5].

Anatomical context of Syringaldazine

• Infection of lupin seedlings with Fusarium culmorum results in the increase in peroxidase activity with syringaldazine as a substrate, mostly in microsomes and cell walls, in the latter fraction somewhat later than in microsomes and cytosol [6].

References