A novel enzyme catalyzing the phosphorylationofproteins was isolated from the brain.The protein contains 100aminoacids and a pI value of 7 (neutral). It can form a homodimerwhensecreted from the cell. The protein was then producedbyrecombinant DNA technology and purified to homogeneity.Thepurified protein has the same size but not charge when comparedtothe native protein, and does not have catalytic activity.However,when the protein is expressed in plant, the purifiedprotein hasfull enzymatic activity.
1. What aminoacids are likely to be presentin the protein?
~~Is it only that the 5charged amino acids(histidine, arginine, lysine, aspartate,glutamate) likely to bepresent in the protein?
2. Briefly explainwhy the protein purifiedfrom plant but not bacteria, has enzymaticactivity
~~Can someone suggest whatcan be the answer of thisquestion. Can this be due to posttranslational modification?
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