EC 6.3.2.43 - [lysine-biosynthesis-protein LysW]—L-2-aminoadipate ligase

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IntEnz Enzyme Nomenclature
EC 6.3.2.43

Names

Accepted name:
[lysine-biosynthesis-protein LysW]—L-2-aminoadipate ligase
Other names:
AAA--LysW ligase
LysX [ambiguous]
α-aminoadipate-lysW ligase
lysX (gene name)
Systematic name:
[lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate:L-2-aminoadipate ligase (ADP-forming)

Reaction

Comments:

The enzymes from the thermophilic bacterium Thermus thermophilus and the thermophilic archaea Sulfolobus acidocaldarius and Sulfolobus tokodaii protect the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW. This reaction is part of the lysine biosynthesis pathway in these organisms. Formerly EC 6.3.2.n4.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Vassylyeva, M. N., Sakai, H., Matsuura, T., Sekine, S., Nishiyama, M., Terada, T., Shirouzu, M., Kuramitsu, S., Vassylyev, D. G., Yokoyama, S.
    Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8.
    Acta Crystallogr. D Biol. Crystallogr. 59: 1651-1652 (2003). [PMID: 12925802]
  2. Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T., Nishiyama, M.
    Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus.
    Nat. Chem. Biol. 5: 673-679 (2009). [PMID: 19620981]
  3. Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S. V., Kuzuyama, T., Nishiyama, M.
    Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
    Nat. Chem. Biol. 9: 277-283 (2013). [PMID: 23434852]

[EC 6.3.2.43 created 2014]