|Domain Trusted Cutoff||208.70|
|Domain Noise Cutoff||91.15|
|Mainrole Category||Amino acid biosynthesis|
|Subrole Category||Aspartate family|
|Entry Date||Dec 1 1999 10:45AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.
The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis.
DR EXPERIMENTAL; EGAD|9629|EC4024; monofunctional, Lys-sensitive homodimer
DR EXPERIMENTAL; EGAD|9487|EC0002; bifunctional, Thr-sensitive homotetramer
DR EXPERIMENTAL; EGAD|21696|EC3940; bifunctional, Met-sensistive homotetramer
DR EXPERIMENTAL; EGAD|52194|YER052C; mostly Thr-sensitive
DR EXPERIMENTAL; EGAD|75283|81007; bifunctional, chloroplast
|Genome Property||GenProp0160: aspartate semialdehyde biosynthesis from aspartate (HMM)|
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