| Description | Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In Bacillus subtilis, YclM is reported to be a single polypeptide of 50 kD. The B. subtilis 168 AKIII is induced by lysine and repressed by threonine, and it is synergistically inhibited by lysine and threonine [ , ].The bifunctional enzyme aspartokinase/homoserine dehydrogenase (AK-HSDH), found in bacteria and plant chloroplasts, catalyses the first and third steps of the aspartate pathway. Homoserine dehydrogenase ( ) catalyses the conversion of L-homoserine to L-aspartate-4-semialdehyde using NAD(P), while aspartate kinase ( ) catalyses the phosphorylation of L-aspartate to 4-phospho-L-aspartate. There are two genes encoding different isoforms of this bifunctional enzymes; one isoform is threonine-sensitive, while the other is methionine-sensitive [ ].This superfamily represents the N-terminal catalytic domain found in aspartokinase and in the bifunctional enzyme aspartokinase/homoserine dehydrogenase. It has a key role in amino acid binding. | Name | Aspartokinase/Bifunctional aspartokinase/homoserine dehydrogenase, catalytic domain |
| Short Name | AsparK_Bifunc_asparK/hSer_DH | Type | Homologous_superfamily |
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