N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase from Entamoeba histolytica: metal alters catalytic rates but not substrate affinity |
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Authors: | Ashraf Mohammad Yadav Bhawna Perinthottathil Sreejith Kumar Kokila Sree Vats Divya Muthuswami Rohini Komath Sneha Sudha |
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Institution: | School of Life Sciences, Jawaharlal Nehru University, New Delhi 110 067, India. |
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Abstract: | PIG-L/GPI12 proteins are endoplasmic reticulum-resident membrane proteins involved in the second step of glycosylphosphatidylinositol anchor biosynthesis in eukaryotes. We show that the Entamoeba histolytica PIG-L protein is optimally active in the acidic pH range. The enzyme has an intrinsic low level of de-N-acetylase activity in the absence of metal and is significantly stimulated by divalent cations. Metal binding induces a large conformational change in the protein that appears to improve catalytic rates while not altering the affinity of the enzyme for its substrate. |
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