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• W2080594259 abstract "Cys116, Lys240*, and Asp241* (asterisks indicate residues from the second subunit of the active dimer) at the active site of l-methionine γ-lyase of Pseudomonas putida (MGL_Pp) are highly conserved among heterologous MGLs. In a previous study, we found that substitution of Cys116 for His led to a drastic increase in activity toward l-cysteine and a decrease in that toward l-methionine. In this study, we examined some properties of the C116H mutant by kinetic analysis and 3D structural analysis. We assumed that substitution of Cys116 for His broke the original hydrogen-bond network and that this induced a significant effect of Tyr114 as a general acid catalyst, possibly due to the narrow space in the active site. The C116H mutant acquired a novel β-elimination activity and lead a drastic conformation change in the histidine residue at position 116 by binding the substrate, suggesting that this His residue affects the reaction specificity of C116H. Furthermore, we suggest that Lys240* is important for substrate recognition and structural stability and that Asp241* is also involved in substrate specificity in the elimination reaction. Based on this, we suggest that the hydrogen-bond network among Cys116, Lys240*, and Asp241* contributes to substrate specificity that is, to l-methionine recognition at the active site in MGL_Pp." @default.
• W2080594259 created "2016-06-24" @default.
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• W2080594259 date "2012-07-23" @default.
• W2080594259 modified "2023-10-01" @default.
• W2080594259 title "The Role of Amino Acid Residues in the Active Site of<scp>L</scp>-Methionine γ-lyase from<i>Pseudomonas putida</i>" @default.
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• W2080594259 doi "https://doi.org/10.1271/bbb.110906" @default.
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