Contribution of the amino acid residues located near the active site metal to the metal–specific activity of Porphyromonas gingivalis SOD induced by a double mutation of Leu 72 Trp and Leu 76 Phe
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The role of superoxide dismutase (SOD) as a radical scavenger in Porphyromonas gingivalis is well documented. P. gingivalis SOD (Pg SOD), which is characterized by a metal–tolerant activity, can use either iron or manganese as a cofactor. Leu ₇2 and Leu ₇6, located near the active–site metal, are characteristic amino acid sequences of Pg SOD proteins, although they are substituted to Trp in the ₇2 position and Phe in the ₇6 position in most iron–containing SOD (Fe–SOD) proteins. In the present study, we constructed a mutant of the enzyme with changes from Leu ₇2 to Trp and Leu ₇6 to Phe. This mutant SOD was examined with respect to its metal–dependent activity and structural characterization. We herein conclude the integrity of Leu ₇2 and Leu ₇6 is a necessary requisite for the metal–tolerant activity of Pg SOD.
Contribution of the amino acid residues located near the active site metal to the metal–specific activity of Porphyromonas gingivalis SOD induced by a double mutation of Leu 72 Trp and Leu 76 Phe
