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首页> 外文期刊>Current enzyme inhibition >Dextransucrase from Weissella cibaria JAG8 inhibited by lysine and cysteine specific inhibitors
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Dextransucrase from Weissella cibaria JAG8 inhibited by lysine and cysteine specific inhibitors

机译：赖氨酸和半胱氨酸特异性抑制剂抑制Weissella cibaria JAG8的右旋糖核酸酶

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摘要

Dextransucrase isolated from Weissella cibaria JAG8 was subjected to active site mapping analysis by using lysine specific inhibitor viz. pyridoxal-5’-phosphate (PLP) and 2,4,6-trinitrobenzenesulphonic acid (TNBS) gave 98.5% and 98.7% inhibition in enzyme activity at 25 mM concentration respectively. The ε-NH2 lysine derivative of enzymeinhibitor complex with PLP and TNBS gave absorbance maxima at 325 and 369 nm, respectively. PLP modified dextransucrase on reduction with sodium borohydride led to the formation of Nε-phosphopyridoxyl lysine complex showed fluorescence maxima at 397 nm indicating that one or more lysine residues present near or at the active site and are essential for enzyme activity. Sucrose, provided protection to the enzyme against inactivation by PLP. The enzyme inactivation caused by cysteine specific inhibitors, DTNB (10 mM) and iodoacetic acid (25 mM) was 98.7% and 98.9%, respectively. Enzyme-inhibitor complexes with DTNB (thio-nitrobenzoate) and iodoacetic acid (thio-acetate) were confirmed by appearance of absorbance maxima at 406 and 323 nm, respectively. These results showed that one or more cysteine residues present near or at the active site and are essential for enzyme activity. Essential cysteine residue at the active site is reported for the first time in dextransucrase.
机译：从Weissella cibaria JAG8分离的右旋糖核酸酶通过使用赖氨酸特异性抑制剂viz进行了活性位点作图分析。在25 mM浓度下，吡ido醛5'-磷酸（PLP）和2,4,6-三硝基苯磺酸（TNBS）分别具有98.5％和98.7％的酶活性抑制作用。与PLP和TNBS形成的酶抑制剂复合物的ε-NH2赖氨酸衍生物分别在325和369 nm处具有最大吸光度。用硼氢化钠还原后，PLP修饰的右旋糖核酸酶导致Nε-磷脂酰赖氨酸复合物的形成，在397 nm处显示出荧光最大值，表明一个或多个赖氨酸残基存在于活性位点附近或在活性位点，对于酶活性至关重要。蔗糖为酶提供了防止PLP灭活的保护。半胱氨酸特异性抑制剂DTNB（10 mM）和碘乙酸（25 mM）引起的酶失活分别为98.7％和98.9％。通过分别在406nm和323nm处出现最大吸光度来证实与DTNB（硫代硝基苯甲酸酯）和碘乙酸（硫代乙酸酯）的酶-抑制剂复合物。这些结果表明，一个或多个半胱氨酸残基存在于活性位点附近或在活性位点，对于酶活性是必不可少的。首次在葡聚糖转导酶中报道了活性位点的必需半胱氨酸残基。

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