Sandbox Reserved 1694: Difference between revisions
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== Important amino acids== | == Important amino acids== | ||
[[Image:DPIDxT.png | thumb]] | [[Image:DPIDxT.png | thumb]] | ||
INPP1D54A does not have a catalytic triad though it has six important <scene name='89/892737/Catalytic_amino_acids/1'>catalytic amino acids</scene> (D54, E80, E79, D153, D317, T158) that promote catalysis in the reaction along with the metal ions that helped the protein function. These amino acids hold the metal ions in place and metal ions hold on to the water and substrate. Thr158 is a very important catalytic amino acid because it is going to do a nucleophilic attack on the water molecule (shown in the picture on the right) which will result in a cascade of other reactions to happen (series of bonds breaking and being made) eventually leading to a phosphate leaving group. Hence, why the function of the enzyme is to remove a phosphate group | INPP1D54A does not have a catalytic triad though it has six important <scene name='89/892737/Catalytic_amino_acids/1'>catalytic amino acids</scene> (D54, E80, E79, D153, D317, T158) that promote catalysis in the reaction along with the metal ions that helped the protein function. These amino acids hold the metal ions in place and metal ions hold on to the water and substrate. Thr158 is a very important catalytic amino acid because it is going to do a nucleophilic attack on the water molecule (shown in the picture on the right) which will result in a cascade of other reactions to happen (series of bonds breaking and being made) eventually leading to a phosphate leaving group. Hence, why the function of the enzyme is to remove a phosphate group. | ||
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In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (<scene name='89/892737/Alanine/1'>mutation in D54</scene>). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. <ref name="dollins" /> | In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (<scene name='89/892737/Alanine/1'>mutation in D54</scene>). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. <ref name="dollins" /> | ||
[[Image:Motif_Copy.png | thumb]] | |||
A six amino acid <scene name='89/892737/Motif/1'>motif</scene>, DPIDxT anchors the metal-binding sites in the protein that are likely involved in catalysis while the metal binds to the substrate. <ref name="dollins" /> The sixth amino acid, x, is not as important as the other five, however, it can be any amino acid depending on the related crystallized structure to INPP1D54A or to a similar protein. | A six amino acid <scene name='89/892737/Motif/1'>motif</scene>, DPIDxT anchors the metal-binding sites in the protein that are likely involved in catalysis while the metal binds to the substrate. <ref name="dollins" /> The sixth amino acid, x, is not as important as the other five, however, it can be any amino acid depending on the related crystallized structure to INPP1D54A or to a similar protein. Also, lithium is an uncompetitive inhibitor for this protein and when it binds to a metal site (metal site 3 in the lower image B) it causes the protein not to function properly. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references /> | <references /> | ||
