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These amino acids are absorbed into the bloodstream to be transported to the liver and onward to the rest of the body. Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. [3] They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in ...
The amino acid glutamate is used to neutralize the ammonia produced when AMP is converted into IMP. Another amino acid, aspartate , is used along with IMP to produce S-AMP in the cycle. Skeletal muscle contains amino acids for use in catabolism, known as the free amino acid pool; however, inadequate carbohydrate supply and/or strenuous exercise ...
Surface-based chemical metabolism of amino acids and very small compounds may have led to the build-up of amino acids, coenzymes and phosphate-based small carbon molecules. [ 119 ] [ additional citation(s) needed ] Amino acids and similar building blocks could have been elaborated into proto- peptides , with peptides being considered key ...
Aromatic amino acids, in turn, are precursors for many biosynthetic pathways, including the lignin in wood. [citation needed] Dietary pentose sugars derived from the digestion of nucleic acids may be metabolized through the pentose phosphate pathway, and the carbon skeletons of dietary carbohydrates may be converted into glycolytic ...
The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in the industrial synthesis of L-cysteine for example.
Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids.This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism).
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 +.
Because skeletal muscle is unable to utilize the urea cycle to safely dispose of ammonium ions generated in the breakdown of branch chain amino acids, it must get rid of it in a different way. To do so, the ammonium is combined with free α-ketoglutarate via a transamination reaction in the cell, yielding glutamate and α-keto acid.
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