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Int J Biol Macromol 2019 Nov 01;140:998-1005. doi: 10.1016/j.ijbiomac.2019.08.089.
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A novel, kinetically stable copper, zinc superoxide dismutase from Psychropotes longicauda.

Li Y , Zhang H .

Superoxide dismutases (SODs) are one of the most important antioxidant enzymes against oxidative damage. In the present study, we cloned and expressed a novel and stable Cu, Zn-SOD from a hadal sea cucumber Psychropotes longicauda (i.e., Pl-Cu, Zn-SOD). The purified recombinant enzyme was intracellular, dimeric with the Mr. of approximately 38 kDa, with the expressed activity from 0 °C to 60 °C at an optimal temperature of 20 °C and 30 °C and maximum activity at the pH of 8.0. The Km and Vmax values of Pl-Cu, Zn-SOD were 0.041 ± 0.004 mM and 1450.275 ± 36.621 U/mg, respectively. At tested conditions, Pl-Cu, Zn-SOD was relatively stable in chemicals, such as β-ME, EDTA, Tween 20, Triton X-100, and Chaps, especially in urea and guanidine hydrochloride, which can resist protease hydrolysis and tolerate high hydrostatic pressure of 100 MPa and 2 M NaCl. All these properties make Pl-Cu, Zn-SOD a candidate in the biopharmaceutical and nutraceutical fields, and help us better understand the adaptation mechanism of hadal area.

PubMed ID: 31408658
Article link: Int J Biol Macromol

Genes referenced: LOC100887844 LOC752081 LOC756768 sod1