| Description | This entry describes a subclass of the aspartate kinases that are mostly Lys-sensitive and are not fused to homoserine dehydrogenase. The E. coli enzyme is a homodimer, while the Bacillus and Corynebacterium enzymes are alpha 2/beta 2 heterotetramers, where the beta subunit is translated from an in-phase alternative initiator at Met-246 [ , ]. The protein slr0657 from Synechocystis PCC6803 is extended by a duplication of the C-terminal region corresponding to the beta chain. Incorporation of a second copy of the C-terminal domain may be quite common in this subgroup of aspartokinases.Aspartate kinase catalyses the first step in the biosynthesis of Lys (via its precursor diaminopimelate), Met, and Thr. In Escherichia coli, a distinct isozyme is inhibited by each of these three amino acid end products [ ]. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenase, which catalyses the next step in the biosynthesis of these amino acids. In contrast, the Lys-sensitive form (III) is a monofunctional enzyme; homoserine dehydrogenase is not part of the Lys biosynthetic pathway. | Name | Aspartate kinase, monofunctional class |
| Short Name | Asp_kin_monofn | Type | Family |
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