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A second aminoacid residue of mechanistic importance is Arg15, which is widely conserved among the known alpha class GSTs ( a value of the thiol group, and mutation of Arg15 to Ala or His decreases the steroid isomerase activity by two orders of magnitude, twice the effect of the Tyr9Phe mutation ( The mechanistic studies of human GST A1-1 were extended to human GST A3-3 following the discovery of the latter enzyme ( a value of 6.1 and Tyr9 phenol pK a of 7.9, somewhat lower than the corresponding pK a values of GST A1-1 ( cat value

Our model shows that the binding of heparin to the N domain of HGF I is coordinated by a cluster of positively charged residues, including Lys34, Arg35, Arg36, Lys60, Lys62, Arg73, Arg76, and Lys78 (Fig

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5, Additional file 1: Table S1)