Methyl parathion hydrolase (MPH) can catalyze the hydrolysis of P-O, P-F, P-CN and P-S bonds in organophosphorus compounds such as methyl parathion. In this study, the effect of K+ on the catalytic activity of MPH was investigated, and the residues interacting with K+ on the activity of MPH were also analyzed. Enzymatic activity analysis showed that the activity of MPH increased rapidly with the increase in ion concentration of potassium. The catalytic activity of MPH in 3 mol/L K+ solution was 13.39 times higher than that in the absence of K+. Based on the molecular dynamic analysis of MPH, the prediction method of K+ distribution in the vicinity of amino acid residues of MPH was established. The predicted results showed that K+ tends to distribute near Asp, Glu, Gln and Asn residues of MPH, and reduced the flexibility of A85-T95 and V323-N329 regions. The most flexible residues E94 and N329 in these two regions were mutated into Ala, which reduced the relative activity of MPH (1 mol/L K+/ 0 mol/L K+) by 26% and 33% respectively and mutating both the residues into Ala reduced the relative activity by 53%. These results indicated that K+ regulated MPH reaction by interacting with E94 and N329, which provides target residues for molecular modification to enhance MPH activity.
SHI Cheng
,
LIU Song
,
DU Guocheng
. Regulation of catalytic efficiency of methyl parathion hydrolase by K+[J]. Food and Fermentation Industries, 2020
, 46(6)
: 8
-12
.
DOI: 10.13995/j.cnki.11-1802/ts.022552
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