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In E. coli citrate synthase, the enzyme involved in the condensation reaction initiating the Citric Acid Cycle is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP. [2] This is one of the initial regulations of the α-ketoglutarate family of amino acid synthesis.
Ribosomes translate the codons to their respective amino acids. [1] In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle. [2] Essential amino acids must be consumed and are made in other organisms. The amino acids are joined by peptide bonds making a polypeptide chain.
Deaminated amino acids that are ketogenic, such as leucine, also feed TCA cycle, forming acetoacetate & ACoA and thereby produce ketones. [1] Besides its role in the synthesis of ketone bodies, HMG-CoA is also an intermediate in the synthesis of cholesterol, but the steps are compartmentalised. [1] [2] Ketogenesis occurs in the mitochondria ...
Phosphagen system (ATP-PCr) and purine nucleotide cycle (PNC) [1] The Purine Nucleotide Cycle is a metabolic pathway in protein metabolism requiring the amino acids aspartate and glutamate. The cycle is used to regulate the levels of adenine nucleotides, in which ammonia and fumarate are generated. [2] AMP converts into IMP and the byproduct ...
The amino acid glycine contributes all its carbon (2) and nitrogen (1) atoms, with additional nitrogen atoms from glutamine (2) and aspartic acid (1), and additional carbon atoms from formyl groups (2), which are transferred from the coenzyme tetrahydrofolate as 10-formyltetrahydrofolate, and a carbon atom from bicarbonate (1). Formyl groups ...
The generation of reducing equivalents, in the form of NADPH, used in reductive biosynthesis reactions within cells (e.g. fatty acid synthesis). Production of ribose 5-phosphate (R5P), used in the synthesis of nucleotides and nucleic acids. Production of erythrose 4-phosphate (E4P) used in the synthesis of aromatic amino acids.
For a protein containing n amino acids, the number of high-energy phosphate bonds required to translate it is 4n-1. [9] The rate of translation varies; it is significantly higher in prokaryotic cells (up to 17–21 amino acid residues per second) than in eukaryotic cells (up to 6–9 amino acid residues per second). [10]
The conversion of the amino acid glutamine to α-ketoglutarate takes place in two reaction steps: Conversion of glutamine to α-ketoglutarate. 1. Hydrolysis of the amino group of glutamine yielding glutamate and ammonium. Catalyzing enzyme: glutaminase (EC 3.5.1.2) 2. Glutamate can be excreted or can be further metabolized to α-ketoglutarate.