Post translation modification

Chemical modification of protein after translation

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After translation Modification refers to protein After translation chemical modification 。 For most proteins, this is Protein Biosynthesis Later steps of.

Chinese name: Post translation modification
Foreign name: Post-translational modification

Alias: Post translational modification
Abbreviations: PTM

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The precursor protein is inactive, and a series of After translation Only by processing can they become functional mature proteins. The types of processing are various, generally divided into the following types: N-end fMet or Met removal Disulfide bond Formation chemical modification And cutting. When Synthetic protein 20 different amino acid Will combine into proteins. Protein translation Post protein Other biochemistry Functional groups (e.g Acetate 、 phosphate , different lipid and carbohydrate ）Will attach to the protein and change the protein chemical property Or cause structural changes (such as establishment Disulfide bond ）To expand the function of protein.

Furthermore, the enzyme can remove amino acids from the N-terminal end of the protein, or from the middle Peptide chain Cut. For example, insulin It is a peptide hormone, which will be cut twice after the establishment of disulfide bond, and the polypeptide precursor will be removed in the middle of the chain. The formed protein contains two disulfide bonds connected Polypeptide chain 。

Other decorations, like Phosphorylation It is part of the mechanism that controls protein activity. Protein activity can be to activate enzymes or passivation 。

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Post translation modifications include the following additions functional group Reaction of:

Acetylation ——Usually protein N end join acetyl 。

Alkylation ——Add such as methyl or ethyl etc. alkyl 。

Methylation ——A common type of alkylation Lysine 、 Arginine Waiting Side chain amino Add methyl group to it.

Biotinylation ——Use Biotin Additions Make the preserved lysine Acylation 。

Glutamization ——On glutamate And Angiosin And other proteins covalent bond 。

Glycinization ——In one to more than 40 kinds glycine Vasopressin C end Establish covalent bonds.

Saccharification ——Set Glycosyl join Asparagine 、 Hydroxylysine 、 serine or threonine , forming glycoprotein 。

Isoprene ——Join as Farnesol and Tetraisoprene etc. isoprene 。

Thiooctylation ——Attach Lipoic acid Functionality.

phosphoric acid Panthenoyl mercaptoethyl amination ——Like in fatty acids Polyketone 、 Nonribosome Peptide chain and Leucine Of biosynthesis From Acetyl CoA join 4 'phosphoric acid panthenoyl mercaptoethylamino 。

Phosphorylation ——Join Phosphate radical To serine Tyrosine , threonine or histidine 。

Sulfation ——Set Sulfate radical Add to tyrosine, Selenide C-terminal amidation 。

Other proteins or peptides

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interferon Activation of Genetization ——And Interferon activating gene 15 (ISG15) protein establishment covalent bond 。 Small ubiquitin related modification ——And Small ubiquitin related modifier protein Establish covalent bonds. Ubiquitination ——And ubiquitin Establish covalent bonds.

Chemical properties of amino acids

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melon ammonification ——Set Arginine Convert to Citrulline 。 Deamination ——Set glutamine Convert to glutamate Or will Asparagine Convert to Aspartate 。 Structural change Disulfide bond ——And two Cysteine Of amino acid establish covalent bond 。 Decompose protein - convert the Peptide bond Cut.

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