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==Introduction==

:Mevalonate diphosphate decarboxylase (MDD) is an important enzyme required by every cell for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi <ref name = "Byres">PMID: 17583736 </ref> <ref name = "Text" > Nelson, D.L. and Cox, M.M. 2008. Lehninger Principles of Biochemistry, Fifth ed. W.H. Freeman and Company. pp 831 </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 (IPP) with the help of 1 ATP molecule<ref name = "Byres"/> <ref name = "Voynova"> PMID: 18823933 </ref>. Even though the kinases in the GHMP family differ in quaternary structure and ability to bind a wide variety of substrates, they share a characteristic alpha/beta fold and similar sequences <ref name = "Byres"/> <ref name = "ByresMartin"> PMID: 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"/>.

:'''Mevalonate diphosphate decarboxylase''' (MDD) is an important enzyme required by every cell for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi <ref name = "Byres">PMID: 17583736 </ref> <ref name = "Text" > Nelson, D.L. and Cox, M.M. 2008. Lehninger Principles of Biochemistry, Fifth ed. W.H. Freeman and Company. pp 831 </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 (IPP) with the help of 1 ATP molecule<ref name = "Byres"/> <ref name = "Voynova"> PMID: 18823933 </ref>. Even though the kinases in the GHMP family differ in quaternary structure and ability to bind a wide variety of substrates, they share a characteristic alpha/beta fold and similar sequences <ref name = "Byres"/> <ref name = "ByresMartin"> PMID: 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"/>.

Sandbox Reserved 333: Difference between revisions

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 <Structure load='2hk3' size='400' frame='true' align='right' caption='Fig 1 Mevalonate diphosphate decarboxylase in the homodimeric form' scene='Insert optional scene name here' />
 ==Introduction==
-:Mevalonate diphosphate decarboxylase (MDD) is an important enzyme required by every cell for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi <ref name = "Byres">PMID: 17583736 </ref> <ref name =  "Text" > Nelson, D.L. and Cox, M.M. 2008. Lehninger Principles of Biochemistry, Fifth ed. W.H. Freeman and Company. pp 831 </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 (IPP) with the help of 1 ATP molecule<ref name = "Byres"/> <ref name = "Voynova"> PMID: 18823933 </ref>.  Even though the kinases in the GHMP family differ in quaternary structure and ability to bind a wide variety of substrates, they share a characteristic alpha/beta fold and similar sequences <ref name = "Byres"/> <ref name = "ByresMartin"> PMID: 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"/>.
+:'''Mevalonate diphosphate decarboxylase''' (MDD) is an important enzyme required by every cell for the biosynthesis of cholesterol and other isoprenoids in mammals, bacteria, yeast and fungi <ref name = "Byres">PMID: 17583736 </ref> <ref name =  "Text" > Nelson, D.L. and Cox, M.M. 2008. Lehninger Principles of Biochemistry, Fifth ed. W.H. Freeman and Company. pp 831 </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 (IPP) with the help of 1 ATP molecule<ref name = "Byres"/> <ref name = "Voynova"> PMID: 18823933 </ref>.  Even though the kinases in the GHMP family differ in quaternary structure and ability to bind a wide variety of substrates, they share a characteristic alpha/beta fold and similar sequences <ref name = "Byres"/> <ref name = "ByresMartin"> PMID: 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"/>.
+See also [[Mevalonate pathway]]
 ==Structure==