Sandbox Reserved 164

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 6: Line 6:
== Superoxide Dismutase 1 (SOD1) ==
== Superoxide Dismutase 1 (SOD1) ==
-
SOD1 is an oxidoreductase enzyme that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals. 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>.
+
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 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 18: Line 18:
<references />
<references />
-
1. McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100
 
2. McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736
2. McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736
3. 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
3. 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

Revision as of 02:56, 29 March 2011

This Sandbox is Reserved from March 9, 2011, through May 30, 2011 for use by the course Biochemistry at Reinhardt University, Waleska, USA, taught by Irma Santoro. This reservation includes Sandbox Reserved 162 through Sandbox Reserved 168.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert a 3D applet Jmol scene window.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

SOD 1 protein NMR

Drag the structure with the mouse to rotate


Contents

Superoxide Dismutase 1 (SOD1)

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 [1]. 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 [2].


Structure

The SOD 1 protein has an amino acid sequence of 154 AA.

ALS

References

  1. ↑ McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100
  2. ↑ SOD 1. Genetics Home Reference. U.S. National Library of Medicine; 2010


2. McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736

3. 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

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_164"
Personal tools