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The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction).
67914 Ensembl ENSG00000088682 ENSMUSG00000031782 UniProt O75208 Q8K1Z0 RefSeq (mRNA) NM_020312 NM_026452 RefSeq (protein) NP_064708 NP_080728 Location (UCSC) Chr 16: 57.45 – 57.46 Mb Chr 8: 95.56 – 95.58 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Ubiquinone biosynthesis protein COQ9, mitochondrial, also known as coenzyme Q9 homolog (COQ9), is a protein that in humans is ...
In animal tissue, BCKDC catalyzes an irreversible step [2] in the catabolism of the branched-chain amino acids L-isoleucine, L-valine, and L-leucine, acting on their deaminated derivatives (L-alpha-keto-beta-methylvalerate, alpha-ketoisovalerate, and alpha-ketoisocaproate, respectively) and converting them [3] to α-Methylbutyryl-CoA, Isobutyryl-CoA and Isovaleryl-CoA respectively.
For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A – + B → A + B –. In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor).
These enzymes act by transferring an acetyl group from their substrate protein to the ADP-ribose moiety of NAD +; this cleaves the coenzyme and releases nicotinamide and O-acetyl-ADP-ribose. The sirtuins mainly seem to be involved in regulating transcription through deacetylating histones and altering nucleosome structure. [ 78 ]
Coenzymes Q is a coenzyme family that is ubiquitous in animals and many Pseudomonadota, [10] a group of gram-negative bacteria. The fact that the coenzyme is ubiquitous gives the origin of its other name, ubiquinone. [1] [2] [11] In humans, the most common form of coenzymes Q is coenzyme Q 10, also called CoQ 10 (/ ˌ k oʊ k j uː ˈ t ɛ n ...
Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. [ 1 ] [ 2 ] Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies .
Thiolases are a family of evolutionarily related enzymes.Two different types of thiolase [4] [5] [6] are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase (EC 2.3.1.9) and 3-ketoacyl-CoA thiolase (EC 2.3.1.16). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid ...