in Escherichia coli, the major enzymes with N-succinyl-L,L-diaminopimelate aminotransferase (SDAP-AT) activity in lysine synthesis are ArgD, AstC, and SerC. Lysine availability does not regulate synthesis of the major SDAP-ATs. Complementation analysis of mutants lacking aminotransferases shows that the SDAP-ATs and alanine aminotransferases are exceptionally redundant, and this redundancy may ensure peptidoglycan synthesis
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diffration to 2.0 A resolution. The orthorhombic crystals contain one functional dimer in the asymmetric unit. The homodimer displays the typical S-shape of class I pyridoxal 5'-phosphate-binding proteins. The two active sites of the dimer both feature an internal aldimine with the co-factor pyridoxal 5'-phosphate covalently bound to the Lys232, although neither substrate nor cofactor has been added during protein production, purification and crystallization. Nine water molecules are conserved in the active site and form an intricate hydrogen-bonding network with the co-factor and the surrounding amino acid residues
Azotobacter vinelandii, Klebsiella aerogenes, Alcaligenes faecalis, Escherichia coli, Lactiplantibacillus plantarum, Micrococcus luteus, no activity in Brewer's yeast, no activity in Lactobacillus casei, no activity in Sus scrofa, no activity in Streptococcus sp., Desmonostoc muscorum, Rhodobacter sphaeroides