Sandbox341: Difference between revisions

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The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).

The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2).

'''STRUCTURE'''

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As stated above the enzyme requires metal co-factors in the active site; which consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)

IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)

Sandbox341: Difference between revisions

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-The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).
+The biological role of Isopentenyl diphosphate-dimethylallyl diphosphate Isomerase is to catalyze the interconversion of IPP and DMAPP(2).The mechanism of isomerization invovles an elecrophilic attack by a proton from the aqueous medium on the IPP double bond this produces a carbocation which is stabalized by the elimination of the C-2 pro-R hydrogen of IPP(1).The proposed model for this suggests the allyl moeity of IPP fits in a deeply buried cavity with E116 and C67 lying on opposite faces of the substrate within the active site, and closed by W161, Y104, and S36(2).
 '''STRUCTURE'''
 ----
-As stated above the enzyme requires metal co-factors in the active site; which consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)
+IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1)