This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Birrer Sandbox 2
From Proteopedia
| Line 1: | Line 1: | ||
==Alcohol Dehydrogenase== | ==Alcohol Dehydrogenase== | ||
| - | Alcohol dehydrogenase (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. In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The mechanism of the reaction is below: | + | Alcohol dehydrogenase (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. {{STRUCTURE_1htb | PDB=1htb | SCENE= }} |
| - | CH3CH2OH + NAD+ → CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) | + | In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The mechanism of the reaction is below: |
| + | CH3CH2OH + NAD+ → CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) (citation needed) | ||
| + | The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase. | ||
Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load | Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load | ||
and display another structure. | and display another structure. | ||
| - | |||
| - | {{STRUCTURE_1htb | PDB=1htb | SCENE= }} | ||
Revision as of 17:15, 1 March 2010
Alcohol Dehydrogenase
Alcohol dehydrogenase (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.
| |||||||||
| 1htb, resolution 2.40Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||||
| Gene: | HUMAN BETA3 CDNA (Homo sapiens) | ||||||||
| Activity: | Alcohol dehydrogenase, with EC number 1.1.1.1 | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The mechanism of the reaction is below:
CH3CH2OH + NAD+ → CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) (citation needed) The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase.
Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
and display another structure.
