EC Number   |
General Information |
Reference |
|---|
   6.3.2.43 | evolution |
proposal of a mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities |
745351 |
| 6.3.2.43 | malfunction |
no growth of deletion mutant without L-lysine. Growth is possible with lysine supplementation. A 0.05-mM concentration of lysine is most effective to support the growth of the deletion mutant, but a higher concentration of lysine decreases the growth rate |
-, 726025 |
| 6.3.2.43 | metabolism |
the enzyme is part of the lysine biosynthetic pathway in Thermococcus kodakarensis, overview. The gene cluster for lysine biosynthetic genes through AAA produces lysine with a LysW-mediated system. In this cluster, TK0279, TK0278, TK0276, TK0277, TK0275, and TK0274 are expected to be responsible for the conversion process from AAA to lysine through the LysW system as LysW-gamma-AAA synthetase, LysW-gamma-AAA kinase, LysW-gamma-AAA semialdehyde dehydrogenase, LysW-gamma-lysine aminotransferase, and LysW-gamma-lysine carboxypeptidase, respectively. LysW-gamma-AAA thus synthesized is transferred to subsequent biosynthetic enzymes to be converted to LysW-gamma-lysine by phosphorylation, reduction, and amination steps. In the final step, LysW-gamma-lysine is recognized by LysK, a carboxypeptidase, resulting in the release of lysine. The lysine biosynthetic enzymes of Thermococcus kodakarensis convert AAA/Glu to lysine/ornithine |
745351 |
| 6.3.2.43 | more |
the modification by TK0278 and successive phosphorylation by TK0276 occurr at the C-terminus of TkLysW. Residue Tyr175 in TkLysX/ArgX plays a critical role in the recognition of glutamate. Residues Thr196, Asn250, and Ala251 are involved in the recognition of the delta-carboxyl group of AAA. The Tyr residue at strand beta10, the Tyr residue at strand beta11, and the Thr residue at the large loop as the additional key residues that define substrate specificity in LysX family proteins |
745351 |
| 6.3.2.43 | physiological function |
enzyme LysX recognizes alpha-aminoadipate (AAA) as a substrate, structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis. Purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. Proposal of a mechanism for substrate recognition |
-, 745351 |
| 6.3.2.43 | physiological function |
in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression |
-, 746544 |
| 6.3.2.43 | physiological function |
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW |
-, 726025 |
| 6.3.2.43 | physiological function |
the enzyme is involved in biosynthesis of lysine in Thermus thermophilus |
726024 |
| 6.3.2.43 | physiological function |
the enzyme is involved in the biosynthesis of lysine through the L-2-aminoadipate pathway |
-, 725697 |
| 6.3.2.43 | physiological function |
Thermococcus kodakarensis has the potential to biosynthesize lysine and ornithine using the carrier protein LysW-mediated system with a single set of bifunctional enzymes |
-, 745351 |
