Burd W, Yourkevich O, Voskoboev A J, van Pée K H
Kupala Grodno State University, Grodno, Belarus.
FEMS Microbiol Lett. 1995 Jun 15;129(2-3):255-60. doi: 10.1111/j.1574-6968.1995.tb07589.x.
A non-haem chloroperoxidase was isolated from the enteric bacterium Serratia marcescens. The enzyme was purified to homogeneity by heat treatment, ammonium sulfate precipitation, ion exchange chromatography, gel filtration and dye-ligand affinity chromatography. Native chloroperoxidase has a molecular mass of 58 kDa and consists of two identical subunits of 29 kDa. Whereas chloroperoxidase catalyses only the bromination of monochlorodimedone, indole is chlorinated by this enzyme. Chloroperoxidase also catalyses the oxidation of amino to nitro groups. The enzyme is thermostable and does not lose any activity when incubated at 65 degrees C for 2 h. Comparison of the first 15 amino-terminal amino acids showed a sequence identity of 80% to the chloroperoxidases from Streptomyces lividans and Pseudomonas pyrrocinia. However, no precipitation band was obtained in the Ouchterlony agar diffusion assay with antibodies raised against the chloroperoxidases from Pseudomonas pyrrocinia and Streptomyces aureofaciens Tü24.
从肠道细菌粘质沙雷氏菌中分离出一种非血红素氯过氧化物酶。通过热处理、硫酸铵沉淀、离子交换色谱、凝胶过滤和染料配体亲和色谱将该酶纯化至同质。天然氯过氧化物酶的分子量为58 kDa，由两个相同的29 kDa亚基组成。虽然氯过氧化物酶仅催化一氯二甲基酮的溴化反应，但吲哚可被该酶氯化。氯过氧化物酶还催化氨基向硝基的氧化反应。该酶具有热稳定性，在65℃孵育2小时不会丧失任何活性。前15个氨基末端氨基酸的序列比较显示，与来自淡紫链霉菌和吡咯菌素假单胞菌的氯过氧化物酶的序列同一性为80%。然而，在用针对吡咯菌素假单胞菌和金色链霉菌Tü24的氯过氧化物酶产生的抗体进行的免疫双扩散试验中未获得沉淀带。
