Birrer Sandbox 2: Difference between revisions

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Alcohol dehydrogenase (PDB id [[1htb]]), or ADH, is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen. The initial scene (<scene name='Birrer_Sandbox_2/Whole_adh_molecule/1'>Alcohol Dehydrogenase Overview</scene>) shows an overview of the molecule, allowing for a general look at the tertiary structure of alcohol dehydrogenase. As far as structure is concerned, alcohol dehydrogenase exists as a tetramer with a zinc molecule complexed in each of the subunits.<ref>Vallee, Bert. L & Hoch, Frederic L. (1955) ''Proc. Natl. Acad. Sci. U.S.A. 41'',327-338. </ref> It has a SCOP catagory of an alpha and beta protein. It does contain at the N-terminal a domain that is all beta; however, the C-Terminal domain is alpha and beta, so the catagory is alpha and beta. The C-Terminal core has 3 layers of alpha/beta/alpha and parallel beta sheets of 6 strands.<ref>''Protein: Alcohol dehydrogenase from Human (Homo sapiens), different isozymes''. SCOP. 2009. 1 March 2010 < http://scop.berkeley.edu/data/scop.b.d.c.b.b.c.html></ref>

Alcohol dehydrogenase (PDB id [[1htb]]), or ADH, is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen. The initial scene (<scene name='Birrer_Sandbox_2/Whole_adh_molecule/1'>Alcohol Dehydrogenase Overview</scene>) shows an overview of the molecule, allowing for a general look at the tertiary structure of alcohol dehydrogenase (it is complexed with cl, pyz, nad, and zn). As far as structure is concerned, alcohol dehydrogenase exists as a tetramer with a zinc molecule complexed in each of the subunits.<ref>Vallee, Bert. L & Hoch, Frederic L. (1955) ''Proc. Natl. Acad. Sci. U.S.A. 41'',327-338. </ref> It has a SCOP catagory of an alpha and beta protein. It does contain at the N-terminal a domain that is all beta; however, the C-Terminal domain is alpha and beta, so the catagory is alpha and beta. The C-Terminal core has 3 layers of alpha/beta/alpha and parallel beta sheets of 6 strands.<ref>''Protein: Alcohol dehydrogenase from Human (Homo sapiens), different isozymes''. SCOP. 2009. 1 March 2010 < http://scop.berkeley.edu/data/scop.b.d.c.b.b.c.html></ref>

Birrer Sandbox 2: Difference between revisions

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Revision as of 01:28, 24 March 2010 view source David Birrer (talk \| contribs) 81 edits No edit summary ← Older edit		Revision as of 01:47, 24 March 2010 view source David Birrer (talk \| contribs) 81 edits No edit summary Newer edit →
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	Alcohol dehydrogenase (PDB id [[1htb]]), or ADH, is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen. The initial scene (<scene name='Birrer_Sandbox_2/Whole_adh_molecule/1'>Alcohol Dehydrogenase Overview</scene>) shows an overview of the molecule, allowing for a general look at the tertiary structure of alcohol dehydrogenase. As far as structure is concerned, alcohol dehydrogenase exists as a tetramer with a zinc molecule complexed in each of the subunits.<ref>Vallee, Bert. L & Hoch, Frederic L. (1955) ''Proc. Natl. Acad. Sci. U.S.A. 41'',327-338. </ref> It has a SCOP catagory of an alpha and beta protein. It does contain at the N-terminal a domain that is all beta; however, the C-Terminal domain is alpha and beta, so the catagory is alpha and beta. The C-Terminal core has 3 layers of alpha/beta/alpha and parallel beta sheets of 6 strands.<ref>''Protein: Alcohol dehydrogenase from Human (Homo sapiens), different isozymes''. SCOP. 2009. 1 March 2010 < http://scop.berkeley.edu/data/scop.b.d.c.b.b.c.html></ref>		Alcohol dehydrogenase (PDB id [[1htb]]), or ADH, is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen. The initial scene (<scene name='Birrer_Sandbox_2/Whole_adh_molecule/1'>Alcohol Dehydrogenase Overview</scene>) shows an overview of the molecule, allowing for a general look at the tertiary structure of alcohol dehydrogenase (it is complexed with cl, pyz, nad, and zn). As far as structure is concerned, alcohol dehydrogenase exists as a tetramer with a zinc molecule complexed in each of the subunits.<ref>Vallee, Bert. L & Hoch, Frederic L. (1955) ''Proc. Natl. Acad. Sci. U.S.A. 41'',327-338. </ref> It has a SCOP catagory of an alpha and beta protein. It does contain at the N-terminal a domain that is all beta; however, the C-Terminal domain is alpha and beta, so the catagory is alpha and beta. The C-Terminal core has 3 layers of alpha/beta/alpha and parallel beta sheets of 6 strands.<ref>''Protein: Alcohol dehydrogenase from Human (Homo sapiens), different isozymes''. SCOP. 2009. 1 March 2010 < http://scop.berkeley.edu/data/scop.b.d.c.b.b.c.html></ref>