the biosynthesis of l-isoleucine from pyruvate and ..

Molecular adaptation of alanine:glyoxylate aminotransferase targeting in primates.

Synthesis of Alanine Pyruvate AlanineTransamination from glutamate ..

Ignoring tyrosine (as it's immediate precursor is phenylalanine, an essentialamino acid), all of the nonessential amino acids (and we will include argininehere) are synthesized from intermediates of major metabolicpathways. Furthermore, the carbon skeletons of these amino acids are traceableto their corresponding ketoacids. Therefore, it could be possible tosynthesize any one of the nonessential amino acids directly by transaminatingits corresponding -ketoacid, if that ketoacid exists as a commonintermediate.

Molecular characterization of a gene for alanine aminotransferase from rice (Oryza sativa).

Amino acid synthesis - Wikipedia

Phenyl alanine is an α-amino acid with the formula HO2CCH(NH2)CH2C6H5. This essential amino acid is classified as nonpolar because of the hydrophobic nature of the benyl side chain. The codons for L-phenylalanine are UUU and UUC. It is a white, powdery solid. L-Phenylalanine (LPA) is an electrically-neutral amino acid, one of the twenty common amino acids used to biochemically form proteins, coded for by DNA.

Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular targeting.

Figure 2. Biosynthesis pathways of acetyl-CoA and NAD cofactors, and their involvement in chromatin-related processes. Acetyl-CoA is produced via two pathways to metabolize pyruvate, involving the key catalytic action of ACL or AceCS1. Acetyl-CoA is an essential metabolite required for the activity of HATs involved in creating an active chromatin conformation via the acetylation of histones. NAD is produced via the NAD salvage pathway. It is an essential cofactor for the PARP and SIRT enzymes, among other proteins. A link exists between the two pathways, as indicated by the dashed lines, by virtue that the NAD-using enzyme, SIRT1, activates the AceCS1 enzyme via protein deacetylation, which, in turn, produces the metabolite acetyl-CoA.

Alanine aminotransferase and glycine aminotransferase from maize (Zea mays L.) leaves.

Metabolism – Proteins | Biochemistry for Medics – …

The α-carbon atom of alanine is bound with a methyl group (-CH3), making it one of the simplest α-amino acids with respect to molecular structure and also resulting in alanine being classified as an aliphatic amino acid. The methyl group of alanine is non-reactive and is thus almost never directly involved in protein function.

KEGG PATHWAY: Metabolic pathways - Reference …

Alanine is most commonly produced by reductive amination of pyruvate. Because transamination reactions are readily reversible and pyruvate pervasive, alanine can be easily formed and thus has close links to metabolic pathways such as glycolysis, gluconeogenesis, and the citric acid cycle. It also arises together with lactate and generates glucose from protein via the alanine cycle.

Arabidopsis thaliana col L-alanine biosynthesis II

1. Doolittle RF (1989). "Redundancies in protein sequences" in Prediction of Protein Structures and the Principles of Protein Conformation. (Fasman GD, ed.), pp 599-623, Plenum Press, New York.
2. IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. . Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc.
3. Kendall, E. C.; McKenzie, B. F. “dl-Alanine” Organic Syntheses, Collected Volume 1, p.21 (1941).

Transamination of pyruvate by alanine …

As an essential amino acid, isoleucine is not synthesized in animals, hence it must be ingested, usually as a component of proteins. In plants and microorganisms, it is synthesized via several steps starting from pyruvic acid and alpha-ketoglutarate. Enzymes involved in this biosynthesis include:[1]


Alanine is an α-amino acid with the chemical formula HO2CCH(NH2)CH3. The L-isomer is one of the 20 proteinogenic amino acids, i.e. the building blocks of proteins. Its three letter code is ala, its one letter code is A, and its codons are GCU, GCC, GCA, and GCG.[1] It is classified as an nonpolar amino acid. L-alanine is second only to leucine, accounting for 7.8% of the primary structure in a sample of 1,150 proteins [1]. D-alanine occurs in bacterial cell walls and in some peptide antibiotics.