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evolution
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the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening
evolution
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the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening
malfunction
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
malfunction
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enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
malfunction
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the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
malfunction
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enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview
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malfunction
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the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine
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malfunction
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deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid
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metabolism
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aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
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aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
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aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
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aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway
metabolism
the enzyme lies at the first branch point in the biosynthetic pathway of important amino acids including lysine and methionine and the cell-wall component diaminopimelate
metabolism
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Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
metabolism
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aspartate-beta-semialdehyde dehydrogenase lies at the first branch point in the aspartate metabolic pathway which leads to the biosynthesis of several essential amino acids and some important metabolites. This pathway is crucial for many metabolic processes in plants and microbes like bacteria and fungi, but is absent in mammals
metabolism
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aspartate-beta-semialdehyde dehydrogenase lies at the first branch point in the aspartate metabolic pathway which leads to the biosynthesis of several essential amino acids and some important metabolites. This pathway is crucial for many metabolic processes in plants and microbes like bacteria and fungi, but is absent in mammals
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
metabolism
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
metabolism
the enzyme has a rate-limiting key function in the biosynthesis of amino acids L-threonine, L-lysine, and L-isoleucine from L-aspartate via L-homoserine
metabolism
mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview
metabolism
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aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
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metabolism
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the enzyme lies at the first branch point in the biosynthetic pathway of important amino acids including lysine and methionine and the cell-wall component diaminopimelate
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metabolism
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mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview
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metabolism
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aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway
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metabolism
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mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview
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metabolism
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Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate
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physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
physiological function
the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
physiological function
aspartate beta-semialdehyde dehydrogenase (ASADH) catalyzes the conversion of phosphoaspartate to aspartate beta-semialdehyde (L-ASA) via reductive dephosphorylation using NADPH as a cofactor
physiological function
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the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
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physiological function
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aspartate beta-semialdehyde dehydrogenase (ASADH) catalyzes the conversion of phosphoaspartate to aspartate beta-semialdehyde (L-ASA) via reductive dephosphorylation using NADPH as a cofactor
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physiological function
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the enzyme catalyzes the NADPH-dependent reductive dephosphorylation of 4-aspartyl phosphate to produce the key intermediate aspartate semialdehyde
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additional information
active site structure analysis and comparison, detailed overview
additional information
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active site structure analysis and comparison, detailed overview
additional information
The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
additional information
active site of FtASADH and NADP+ binding, structure analysis, overview
additional information
the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
additional information
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the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
additional information
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The structure of CnASADH belongs to the Rossmann-fold superfamily of pyridine-linked dehydrogenases and shares the same overall monomeric structural features as the other ASADHs for which structures are determined
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additional information
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active site of FtASADH and NADP+ binding, structure analysis, overview
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additional information
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active site structure analysis and comparison, detailed overview
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additional information
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the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
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additional information
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the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle
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