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evolution
the enzyme belongs to class II aspartate kinases
evolution
the enzyme belongs to class II aspartate kinases
evolution
the enzyme belongs to class III aspartate kinases
evolution
the enzyme from Corynebacterium pekinense belongs to the class II of aspartate kinases
evolution
the enzyme is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. The enzyme CaAK monomer from Clostridium acetobutylicum belongs to the class I type aspartate kinases which consists of one catalytic domain and two ACT domains
evolution
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
evolution
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the enzyme belongs to class II aspartate kinases
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malfunction
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A 2fold increase in lysine production is observed by cloning of the ASK gene in Corynebacterium glutamicum rather than in Escherichia coli, due to the presence of lysine exporter channel which facilitates lysine extraction
malfunction
four-week-old loss-of-function Arabidopsis thaliana mutants in the AK-HSDH2 gene have increased amounts of Asp and Asp-derived amino acids, especially Thr, in leaves, phenotype, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview
malfunction
the contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview
malfunction
the contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview
metabolism
aspartate kinase catalyzes the phosphorylation of aspartate to Asp-phosphate, the first step in the aspartate family biosynthesis pathway. The enzyme is feedback regulated
metabolism
aspartate kinase is the key enzyme in the biosynthesis of aspartate derived amino acids
metabolism
lysine biosynthesis in Corynebacterium glutamicum starts from aspartate and aspartate kinase is the principal enzyme involved in the lysine biosynthesis metabolic pathway, regulatory key role of aspartate kinase
metabolism
the enzyme catalyzes the first step in the aspartate-derived amino acid pathway. Synthesis of 4-phospho-L-aspartate from L-aspartate is an intermediate step at an important branch point where one path leads to the synthesis of lysine and the other to threonine, methionine and isoleucine. The aspartate kinase enzymes exhibit complex allosteric regulation
metabolism
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the enzyme catalyzes the first step of the biosynthesis of several amino acids, with L-isoleucine being the endproductof the pathway, overview. The enzyme is regulated by feedback inhibition, overview
metabolism
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
metabolism
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the enzyme is involved in the biosynthesis of 4-hydroxy-3-nitrosobenzamide
metabolism
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the enzyme catalyzes the first step of the biosynthesis of several amino acids, with L-isoleucine being the endproductof the pathway, overview. The enzyme is regulated by feedback inhibition, overview
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metabolism
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lysine biosynthesis in Corynebacterium glutamicum starts from aspartate and aspartate kinase is the principal enzyme involved in the lysine biosynthesis metabolic pathway, regulatory key role of aspartate kinase
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metabolism
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biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
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metabolism
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biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
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metabolism
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biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
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physiological function
aspartate kinase is a multimer and an allosteric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl phosphate. Allosteric regulation (feedback inhibition) of proteins controls the synthesis pathway of this enzyme
physiological function
biosynthesis of aspartate-derived amino acids lysine, methionine, threonine, and isoleucine involves monofunctional Asp kinases and dual-functional Asp kinase-homoserine dehydrogenases (AK-HSDHs). Isozymes AK2 and AK-HSDH1 are the major contributors to overall AK and HSDH activities, respectively
physiological function
the enzyme is tightly regulated through feedback control and responsible for the synthesis of 4-phospho-L-aspartate from L-aspartate. The aspartate kinase enzymes exhibit complex allosteric regulation
physiological function
aspartate kinase (AK) and homoserine dehydrogenase (HseDH, EC 1.1.1.3) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
physiological function
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aspartate kinase (AK) and homoserine dehydrogenase (HseDH, EC 1.1.1.3) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
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physiological function
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aspartate kinase (AK) and homoserine dehydrogenase (HseDH, EC 1.1.1.3) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
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physiological function
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aspartate kinase (AK) and homoserine dehydrogenase (HseDH, EC 1.1.1.3) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
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additional information
structure-function analysis, overview
additional information
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structure-function analysis, overview
additional information
catalytic residue Arg169 is an important residue in substrate binding, the catalytic domain, and in inhibitor binding. Arg169 forms a hydrogen bond with Glu92, which functions as the entrance gate. R169, S172, and G171 are key substrate binding residues. Three-dimensional structure analysis and structure homology modelling, overview
additional information
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catalytic residue Arg169 is an important residue in substrate binding, the catalytic domain, and in inhibitor binding. Arg169 forms a hydrogen bond with Glu92, which functions as the entrance gate. R169, S172, and G171 are key substrate binding residues. Three-dimensional structure analysis and structure homology modelling, overview