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首页> 外文期刊>Journal of Toxicology-Toxin Reviews >EVOLUTIONARY REDUCTION OF ENZYMATIC ACTIVITIES OF SNAKE VENOM PHOSPHOLIPASES A_2
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EVOLUTIONARY REDUCTION OF ENZYMATIC ACTIVITIES OF SNAKE VENOM PHOSPHOLIPASES A_2

机译:蛇毒磷酸化酶A_2的酶活性的进化还原

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摘要

The reaction mechanism of the 14 kDa secreted phospholipases A_2 (PLAs) and examples of venom PLAs with diminished catalytic activities are reviewed. Evolutionary strategies to reduce the venom PLA catalytic power and new function gains are discussed. Down-regulations of the enzymatic activities appear to be due to: 1) retention of interfacial binding, but with selective alternation of active site residues in basic PLAs; 2) mutations at both the interfacial binding sites and catalytic sites of strong anticoagulating PLAs which bind to the coagulation factor; and 3) either substitution or truncation of the interface binding sites in acidic subunits of heterodimeric PLA-neurotoxins to generate chaperon like molecules.
机译:综述了14 kDa分泌的磷脂酶A_2(PLA)的反应机理以及催化活性减弱的毒PLA的实例。讨论了减少毒液PLA催化能力和获得新功能的进化策略。酶活性的下调似乎是由于:1)保留了界面结合,但是在碱性PLA中有活性位点残基的选择性改变。 2)与凝血因子结合的强抗凝PLA的界面结合位点和催化位点处的突变; 3)异源二聚PLA-神经毒素的酸性亚基中的界面结合位点的取代或截短,以产生伴侣分子。

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