Birrer Sandbox 2: Difference between revisions
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==Alcohol Dehydrogenase== {{STRUCTURE_1htb | PDB=1htb | SCENE= }} | ==Alcohol Dehydrogenase== {{STRUCTURE_1htb | PDB=1htb | SCENE= }} | ||
==Overview== | ==Overview== | ||
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==Reaction and Mechanism== | ==Reaction and Mechanism== | ||
In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. In its reaction, alcohol dehydrogenase uses zinc and NAD to facilitate the reaction. The function of zinc is to position the –OH group on the ethanol in a conformation that allows for the oxidation to occur. NAD then acts as a cosubstrate and performs the oxidation. A second scene shows the whole molecule of ADH complexed with just Zn and EtOH (<scene name='Birrer_Sandbox_2/Adh_plus_zn_and_ethanol/1'>ADH+ZN,ETOH Whole Structure</scene>). A second scene (<scene name='Birrer_Sandbox_2/Ligand_and_3_residues/1'>Ligand + 3 Residues</scene>) shows a picture of this interaction, with two ethanol molecules attached to the active sites. In the picture Zinc is positioned between Cys46, Cys174, and His67, all polar side chains. Ethanol, then, binds to the zinc which is next to the NAD cosubstrate. <ref>''Alcohol Dehydrogenase''. [[Protein Data Bank]]. 2010. RCSB. 1 March 2010 <http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb13_3.html> </ref> | In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. In its reaction, alcohol dehydrogenase uses zinc and NAD to facilitate the reaction. The function of zinc is to position the –OH group on the ethanol in a conformation that allows for the oxidation to occur. NAD then acts as a cosubstrate and performs the oxidation. A second scene shows the whole molecule of ADH complexed with just Zn and EtOH (<scene name='Birrer_Sandbox_2/Adh_plus_zn_and_ethanol/1'>ADH+ZN,ETOH Whole Structure</scene>). A second scene (<scene name='Birrer_Sandbox_2/Ligand_and_3_residues/1'>Ligand + 3 Residues</scene>) shows a picture of this interaction, with two ethanol molecules attached to the active sites. In the picture Zinc is positioned between Cys46, Cys174, and His67, all polar side chains. Ethanol, then, binds to the zinc which is next to the NAD cosubstrate. <ref>''Alcohol Dehydrogenase''. [[Protein Data Bank]]. 2010. RCSB. 1 March 2010 <http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb13_3.html> </ref> | ||
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==Kinetics and Regulation== | |||
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==References== | ==References== | ||
<references /> | <references /> | ||