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SOD1 is one of three oxidoreductase enzymes that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals and transforming them into oxygen and hydrogen peroxide. <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref> This occurs in a quick two step mechanism:

M(n+1)+-SOD + O2− → Mn+-SOD + O2

Cu(2+)SOD + O2− → Cu(+)SOD + O2

Mn+-SOD + O2− + 2H+ → M(n+1)+-SOD + H2O2<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.

Cu(+)SOD + O2− + 2H+ → Cu(2+)SOD + H2O2<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.

This protein is coded for by the SOD 1 gene located on chromosome 21 at position 21q22.1 from base pairs 33,031,934 to 33,041,243. <ref name="Sod1">SOD 1. Genetics Home Reference. U.S. National Library of Medicine; 2010</ref>

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== ALS ==

Mutations to the SOD 1 protein have been linked to the development of familial amyotrophic lateral sclerosis. <ref name="Al-Chalabi">Al-Chalabi A, Leigh PN (August 2000). "Recent advances in amyotrophic lateral sclerosis". Curr. Opin. Neurol. 13 (4): 397–405. PMID 10970056.</ref> These mutations cause a conformational change that leads to motor neuron death through toxic radical build up, promotion of apoptosis, aggregate formation of misfolded proteins, or over stimulation of the cells.<ref name="Sod1">SOD 1. Genetics Home Reference. U.S. National Library of Medicine; 2010</ref>

Mutations to the SOD 1 protein have been linked to the development of familial amyotrophic lateral sclerosis (Lou Gehrig's Disease). <ref name="Al-Chalabi">Al-Chalabi A, Leigh PN (August 2000). "Recent advances in amyotrophic lateral sclerosis". Curr. Opin. Neurol. 13 (4): 397–405. PMID 10970056.</ref> These mutations cause a conformational change that leads to motor neuron death through toxic radical build up, promotion of apoptosis, aggregate formation of misfolded proteins, or over stimulation of the cells.<ref name="Sod1">SOD 1. Genetics Home Reference. U.S. National Library of Medicine; 2010</ref> In the United States, one of the most common SOD 1 protein mutations is the A4V mutation, where a point mutation causes the alanine at the 4th amino acid position to change to a valine; <ref name="Rosen">Rosen DR, Bowling AC, Patterson D, Usdin TB, Sapp P, Mezey E, McKenna-Yasek D, O'Regan J, Rahmani Z, Ferrante RJ (June 1994). "A frequent ala 4 to val superoxide dismutase-1 mutation is associated with a rapidly progressive familial amyotrophic lateral sclerosis". Hum. Mol. Genet. 3 (6): 981–7. PMID 7951249</ref> however, over 100 different mutations have been found in association with the onset of ALS.

== References ==

Sandbox Reserved 164: Difference between revisions

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 <Structure load='3ECU' size='500' frame='true' align='right' caption='Crystal Structure of SOD 1 protein, PDB ID: 3ECU' scene='Insert optional scene name here' />
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 SOD1 is one of three oxidoreductase enzymes that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals and transforming them into oxygen and hydrogen peroxide. <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref>  This occurs in a quick two step mechanism:
-M(n+1)+-SOD + O2− → Mn+-SOD + O2
+Cu(2+)SOD + O2− → Cu(+)SOD + O2
-Mn+-SOD + O2− + 2H+ → M(n+1)+-SOD + H2O2<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.
+Cu(+)SOD + O2− + 2H+ → Cu(2+)SOD + H2O2<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.
 This protein is coded for by the SOD 1 gene located on chromosome 21 at position 21q22.1 from base pairs 33,031,934 to 33,041,243. <ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref>
@@ Line 17: / Line 17: @@
 == ALS ==
-Mutations to the SOD 1 protein have been linked to the development of familial amyotrophic lateral sclerosis. <ref name="Al-Chalabi">Al-Chalabi A, Leigh PN (August 2000). "Recent advances in amyotrophic lateral sclerosis". Curr. Opin. Neurol. 13 (4): 397–405. PMID 10970056.</ref>   These mutations cause a conformational change that leads to motor neuron death through toxic radical build up, promotion of apoptosis, aggregate formation of misfolded proteins, or over stimulation of the cells.<ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref>
+Mutations to the SOD 1 protein have been linked to the development of familial amyotrophic lateral sclerosis (Lou Gehrig's Disease). <ref name="Al-Chalabi">Al-Chalabi A, Leigh PN (August 2000). "Recent advances in amyotrophic lateral sclerosis". Curr. Opin. Neurol. 13 (4): 397–405. PMID 10970056.</ref>   These mutations cause a conformational change that leads to motor neuron death through toxic radical build up, promotion of apoptosis, aggregate formation of misfolded proteins, or over stimulation of the cells.<ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref> In the United States, one of the most common SOD 1 protein mutations is the A4V mutation, where a point mutation causes the alanine at the 4th amino acid position to change to a valine; <ref name="Rosen">Rosen DR, Bowling AC, Patterson D, Usdin TB, Sapp P, Mezey E, McKenna-Yasek D, O'Regan J, Rahmani Z, Ferrante RJ (June 1994). "A frequent ala 4 to val superoxide dismutase-1 mutation is associated with a rapidly progressive familial amyotrophic lateral sclerosis". Hum. Mol. Genet. 3 (6): 981–7. PMID 7951249</ref> however, over 100 different mutations have been found in association with the onset of ALS.
 == References ==
 <references />