Isoleucine phenylalanine tryptophan tryptophan? Tyrosine-tyrosine

ASP- aspartic acid ASN- asparagine glutamic acid? Lysine lysine

Gln- glutamine? Methionine? Serine? Threonine?

Cysteine proline histidine arginine

Amino acid is a compound in which the hydrogen atom on the carbon atom of carboxylic acid is replaced by amino group, and the amino acid molecule contains two functional groups: amino group and carboxyl group. Similar to hydroxy acids, amino acids can be divided into α-,β-,γ-...w- amino acids according to the position of amino groups attached to the carbon chain, but the amino acids obtained by protein hydrolysis are all α-amino acids, with only twenty kinds, which are the basic units of protein.

Extended data:

The specific ways in which amino acids participate in metabolism are as follows:

1. oxidative deamination: step 1, dehydrogenation to produce imine; The second step is hydrolysis. The produced H2O2 is toxic. Under the catalysis of catalase, H2O and O2 are generated, which reduces the toxicity to cells.

2. Non-oxidative deamination: ① reductive deamination (under strict oxygen-free conditions); (2) water deamination; ③ Dehydration and deamination; (4) sulfhydryl deamination; ⑤ Redox deamination, in which two amino acids react with each other to produce organic acids, ketoacids and ammonia; ⑥ Deamidation.

3. Transamination. Transamination is an important way of deamination of amino acids. Except Gly, Lys, Thr and Pro, most amino acids can participate in transamination. Amino transfer occurs between α -amino acid and α -keto acid, and the result is that the original amino acid generates the corresponding keto acid, and the original keto acid generates the corresponding amino acid.

4. Combined deamination: Simple transamination can't finally deamination, and simple oxidation deamination can't meet the needs of deamination. With the help of combined deamination, organisms can deamination quickly;

1) combined deamination centered on glutamate dehydrogenase. The α-amino group of amino acid is firstly transferred to α-ketoglutarate to generate corresponding α-ketoacid and Glu, and then, under the catalysis of L-Glu deaminase, α-ketoglutarate deaminations and releases ammonia. 2) Combined deamination through purine nucleotide cycle. Skeletal muscle, heart muscle, liver and brain mainly circulate in the form of purine nucleotides.

References:

Baidu encyclopedia-amino acids