Search results
Results from the WOW.Com Content Network
This reaction is essential for the subsequent steps in beta oxidation that lead to the production of acetyl-CoA, NADH, and FADH2, which are important for generating ATP, the energy currency of the cell. Long-chain hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency is a condition that affects mitochondrial function due to enzyme impairments.
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group , which may be in the form of FAD or flavin mononucleotide (FMN).
The electron transport chain oxidizes coenzymes NADH and FADH2. Protein synthesis makes use of mitochondrial DNA, RNA, and tRNA. [5] Regulation of processes makes use of ions (Ca 2+ /K + /Mg +). [6] Additional metabolites present in the matrix are CO 2, H 2 O, O 2, ATP, ADP, and P i. [1]
The following reaction is the oxidation of the fatty acid by FAD to afford an α,β-unsaturated fatty acid thioester of coenzyme A: ACADs can be categorized into three distinct groups based on their specificity for short-, medium-, or long-chain fatty acid acyl-CoA substrates.
Long-chain acyl-CoA esters are substrates for a number of important enzymatic reactions and play a central role in the regulation of metabolism as allosteric regulators of several enzymes. To participate in specific metabolic processes, fatty acids must first be activated by being joined in thioester linkage (R-CO-SCoA) to the -SH group of ...
The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid [13] Phenylacrylic acid decarboxylase (EC 4.1.1.102), an enzyme which confers resistance to cinnamic acid in yeast [14] Phototropin and cryptochrome, light-sensing proteins [15]
This specificity reflects the distinct metabolic roles of the respective coenzymes, and is the result of distinct sets of amino acid residues in the two types of coenzyme-binding pocket. For instance, in the active site of NADP-dependent enzymes, an ionic bond is formed between a basic amino acid side-chain and the acidic phosphate group of NADP +.
a long-chain acyl-CoA + electron-transfer flavoprotein a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein This enzyme contains FAD as prosthetic group and participates in fatty acid metabolism and PPAR signaling pathway. [ 6 ]