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Aspartate kinase

Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.

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Aspartate kinase

Also known as Aspartate kinase (Aspartokinase).
Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.

Aspartate kinase Ask_Ect

Also known as Aspartate kinase Ask_Ect (Aspartokinase).
Involved in the biosynthesis of L-aspartate-beta-semialdehyde, which is an intermediate in the biosynthesis of ectoine, a highly soluble organic osmolyte, called compatible solute. Ectoine is used to avoid excessive water efflux, plasmolysis, molecular crowding of the cytoplasm, and cessation of growth in high salinity environments. Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.

Aspartate kinase Ask_LysC

Also known as Aspartate kinase Ask_LysC (Aspartokinase).
Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.

Aspartate kinase FUB3

Also known as Aspartate kinase FUB3 (Fusaric acid biosynthesis protein 3).
Aspartate kinase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 ().

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