EC Number   |
General Information |
Reference |
|---|
  6.3.2.60 | evolution |
gene duplication events at different stages of evolution led to ArgX and LysX (EC 6.3.2.43) |
-, 754823 |
| 6.3.2.60 | evolution |
proposal of a mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities |
745351 |
| 6.3.2.60 | malfunction |
enzyme mutants Y175I, I185Y, N250G, and S251F exhibit an apparent substrate preference for glutamate, suggesting that Tyr at 185 compensates for the function of Tyr175 in the recognition of the gamma-carboxyl group of glutamate |
745351 |
| 6.3.2.60 | metabolism |
lysine and arginine biosyntheses are mediated by a common carrier protein in Sulfolobus acidocaldarius. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions |
-, 754823 |
| 6.3.2.60 | metabolism |
the enzyme is part of the lysine biosynthetic pathway in Thermococcus kodakarensis, overview. The lysine biosynthetic enzymes of Thermococcus kodakarensis convert AAA/Glu to lysine/ornithine |
745351 |
| 6.3.2.60 | more |
StArgX/ADP structrue analysis, and structure of substrate StLysW and recognition by enzyme StArgX, structural model of the phosphoryl intermediate in the StArgX reaction, overview. The alpha-amino group of the substrate glutmate molecule is to be ligated with the gamma-carboxyl group of Glu56 residue of StLysW. Interaction analysis of ArgX and LysW |
-, 754823 |
| 6.3.2.60 | 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 |
| 6.3.2.60 | physiological function |
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 |
| 6.3.2.60 | physiological function |
the hyperthermophilic archaeon Sulfolobus acidocaldarius not only biosynthesizes lysine through LysW-mediated protection of alpha-aminoadipate (AAA), but also uses the amino-group carrier protein LysW to protect the amino group of glutamate in arginine biosynthesis, cf. EC 6.3.2.43. ArgX is the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW |
-, 754823 |
