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=Introduction= | =Introduction= | ||
| - | :Mevalonate diphosphate decarboxylase (MDD) is an important enzyme required for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi <ref name = "Byres"> 17583736 </ref>. MDD is a member of the GHMP (Galactokinase, Homoserine kinase, mevalonate kinase and phosphomevalonate kinase) enzyme family, and is responsible for the conversion of mevalonate diphosphate to isopentenyl pyrophosphate with the help of 1 ATP molecule<ref name = "Byres"/> <ref name = "Voynova"> 18823933 </ref>. | + | :Mevalonate diphosphate decarboxylase (MDD) is an important enzyme required for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi <ref name = "Byres"> 17583736 </ref>. MDD is a member of the GHMP (Galactokinase, Homoserine kinase, mevalonate kinase and phosphomevalonate kinase) enzyme family, and is responsible for the conversion of mevalonate diphosphate to isopentenyl pyrophosphate with the help of 1 ATP molecule<ref name = "Byres"/> <ref name = "Voynova"> 18823933 </ref>.The kinases in the GHMP family share a characteristic alpha/beta fold and similar sequences <ref name = "Byres"/>, even though they differ in quaternary structures, and can bind a wide variety of substrates <ref name = "ByresMartin"> 16511101 </ref>. Some GHMP kinases exist as dimers, some as tetramers and some as monomers <ref name = "Byres"/>. The amino acid residues in MDD are highly conserved across all species, indicating the specific important activity of the enzyme <ref name = "Byres"/>. |
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<scene name='Sandbox_Reserved_333/Fig2/1'>gggggg</scene> | <scene name='Sandbox_Reserved_333/Fig2/1'>gggggg</scene> | ||
Revision as of 07:00, 11 March 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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Introduction
- Mevalonate diphosphate decarboxylase (MDD) is an important enzyme required for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi [1]. MDD is a member of the GHMP (Galactokinase, Homoserine kinase, mevalonate kinase and phosphomevalonate kinase) enzyme family, and is responsible for the conversion of mevalonate diphosphate to isopentenyl pyrophosphate with the help of 1 ATP molecule[1] [2].The kinases in the GHMP family share a characteristic alpha/beta fold and similar sequences [1], even though they differ in quaternary structures, and can bind a wide variety of substrates [3]. Some GHMP kinases exist as dimers, some as tetramers and some as monomers [1]. The amino acid residues in MDD are highly conserved across all species, indicating the specific important activity of the enzyme [1].
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Image:Trial 1.png
Caption 1
