non-proteinogenic
nonproteinogenic

All three are non-proteinogenic amino acids, not being found in proteins.

This non-proteinogenic amino acid is classified as a polar base.

Many important proteinogenic and non-proteinogenic amino acids also play critical non-protein roles within the body.

In cells, especially autotrophs, several non-proteinogenic amino acids are found as metabolic intermediates.

It also focuses on an expanded genetic code and the incorporation of non-proteinogenic amino acids into proteins.

Several non-proteinogenic amino acids are noteworthy because they are:

Naturally-occurring cyanotoxins can also include non-proteinogenic amino acids.

Perhaps the most abundant azitidine containing natural product is azetidine-2-carboxylic acid, a non-proteinogenic homolog of proline.

Enduracididine is an α-amino acid that is non-proteinogenic.

Cycloleucine is a non-proteinogenic amino acid.

-(+)-(S)-Canavanine is a non-proteinogenic amino acid found in certain leguminous plants.

Caramboxin is a non-proteinogenic amino acid that stimulates the glutamate receptors in neurons.

Non-proteinogenic BCAAs include norvaline and 2-aminoisobutyric acid.

It is not one of the proteinogenic amino acids and rather rare in nature (cf. Non-proteinogenic amino acids).

Aside from the 22 proteinogenic amino acids, there are many other amino acids that are called non-proteinogenic.

It belongs to peptaibol peptides which contain the non-proteinogenic amino acid residue Aib (2-aminoisobutyric acid).

Ethionine is a non-proteinogenic amino acid structurally related to methionine, with an ethyl group in place of the methyl group.

The peptide has several unusual features, including four -amino acids, a methylated phenylalanine, and the non-proteinogenic amino acid enduracididine.

Non-proteinogenic amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis.

Another example is the possibility of using the promiscuous activities of cysteine synthase (cysM) towards nucleophiles to produce non-proteinogenic amino acids.

Several non-proteinogenic amino acids are toxic due to their ability to mimic certain properties of proteinogenic amino acids, such as thialysine.

Proteusins, also called polytheonamides, were originally presumed to be nonribosomal natural products due to the presence of many D-amino acids and other non-proteinogenic amino acids.

The non-proteinogenic amino acid L-homoarginine is a growth inhibitor of S. aureus, as well as Candida albicans.

In biochemistry, non-coded, non-proteinogenic, or "unnatural" amino acids are those not naturally encoded or found in the genetic code of any organisms.

Peptaibols are biologically active peptides containing between seven and twenty amino acid residues, some of which are non-proteinogenic amino acids.

Thus, nonproteinogenic amino acids would have been excluded by the contingent evolutionary success of nucleotide-based life forms.

-Isoglutamine, the derivative of the nonproteinogenic -glutamic acid, has R configuration.

Nonproteinogenic amino acids are incorporated in nonribosomal peptides, which are not produced by the ribosome during translation.

In all, six of the seven total amino acids of the teicoplanin backbone are composed of nonproteinogenic or modified amino acids.

Analysis indicated tyrosine and three types of nonproteinogenic amino acids, (S)-4-hydroxyphenylglycine, 3,5-dihydroxyphenylglycine, and β-hydroxytyrosine as the building blocks of the teicoplanin group of glycopeptides.

Two nonproteinogenic amino acids exist in the lipopeptide, the unusual amino acid L-kynurenine (Kyn), only known to daptomycin, and L-3-methylglutamic acid (mGlu).

These and other novel genes (dptI, dptJ) are believed to be involved in supplying the nonproteinogenic amino acids L-3-methylglutamic acid and Kyn; they are located next to the NRPS genes.