The isolation and properties of a tabtoxin-hydrolysing aminopeptidase from the periplasm of Pseudomonas syringae pv. tabaci
作者： C. Levi , R.D. Durbin
DOI: 10.1016/S0048-4059(86)80076-5
关键词: Enzyme 、 Periplasmic space 、 Pseudomonadales 、 Biology 、 Biochemistry 、 Tabtoxin 、 Aminopeptidase 、 Microbiology 、 Pseudomonadaceae 、 Pseudomonas syringae 、 Divalent
摘要: A tabtoxin-hydrolysing enzyme was partially purified from the periplasm of several strains Pseudomonas syringae pv. tabaci . It is an aminopeptidase with a broad pH optimum. The obtained by osmotic shock and then ammonium sulphate precipitation; it became unstable further purificiation (Bio-Gel, DEAE-Sephadex Phenyl-Sepharose chromatography). Its activity sensitive to EDTA but not n -ethylmaleimide or phenylmethyl-sulphonyl fluoride. Although, tabtoxin hydrolysis absolutely requires zinc for in vivo , other divalent cations are effective restoring EDTA-treated preparation. Bacterial which could be activated hydrolyse did have zinc-activatable peptidase their periplasm. This appears responsible conversion bacterium biologically active form, tabtoxinine- β -lactam. may also function as part mechanism self-protection against
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