Target type: molecularfunction
Catalysis of the reaction: 3R-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. [PMID:19571038, PMID:25203508]
(3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity catalyzes the reversible oxidation of (3R)-hydroxyacyl-CoA esters to the corresponding 3-ketoacyl-CoA esters, utilizing NAD+ as an electron acceptor. This enzyme is essential in the beta-oxidation pathway, a key metabolic process for breaking down fatty acids into energy. The enzyme specifically acts on the (3R) enantiomer of hydroxyacyl-CoA esters, demonstrating stereospecificity. The reaction proceeds in two steps: 1) the removal of a hydride ion from the C3 position of the (3R)-hydroxyacyl-CoA substrate, reducing NAD+ to NADH. 2) the removal of a proton from the hydroxyl group at the C3 position, resulting in the formation of a 3-ketoacyl-CoA ester. The catalytic mechanism involves a conserved tyrosine residue that acts as a general base, abstracting the proton from the hydroxyl group, and a histidine residue that acts as a general acid, donating a proton to the NAD+ cofactor. The enzyme exhibits a high degree of substrate specificity, preferentially utilizing medium-chain length acyl-CoA substrates. This activity plays a critical role in energy metabolism, providing essential building blocks for biosynthesis and contributing to the production of ATP. '
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Protein | Definition | Taxonomy |
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Peroxisomal multifunctional enzyme type 2 | A peroxisomal multifunctional enzyme type 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P51659] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
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N-(4,6-dimethyl-2-pyridinyl)-4-[5-(trifluoromethyl)-2-pyridinyl]-1-piperazinecarbothioamide | piperazines; pyridines |