Enzymes
UniProtKB help_outline | 1,397 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
[amino-group carrier protein]-C-terminal-γ-(L-lysyl)-L-glutamate
Identifier
RHEA-COMP:9715
Reactive part
help_outline
- Name help_outline C-terminal-γ-L-glutamyl-L-lysine group Identifier CHEBI:78526 Charge -1 Formula C11H19N3O5 SMILEShelp_outline [NH3+]CCCC[C@H](NC(=O)CC[C@H](N-*)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[amino-group carrier protein]-C-terminal-L-glutamate
Identifier
RHEA-COMP:9693
Reactive part
help_outline
- Name help_outline C-terminal-L-glutamyl residue Identifier CHEBI:78525 Charge -2 Formula C5H6NO4 SMILEShelp_outline [O-]C(=O)CC[C@H](N-*)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-lysine Identifier CHEBI:32551 Charge 1 Formula C6H15N2O2 InChIKeyhelp_outline KDXKERNSBIXSRK-YFKPBYRVSA-O SMILEShelp_outline [NH3+]CCCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 65 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:48684 | RHEA:48685 | RHEA:48686 | RHEA:48687 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Characterization of a lysK gene as an argE homolog in Thermus thermophilus HB27.
Miyazaki J., Kobashi N., Fujii T., Nishiyama M., Yamane H.
We conducted a chromosome walk to obtain a DNA fragment downstream of lysJ and found an argE homolog in a putative operon composed of lysJ-orfC-orfD-argE homologs. A knockout mutant of the argE homolog showed significantly slow growth on a minimal medium, and the growth was markedly improved by ad ... >> More
We conducted a chromosome walk to obtain a DNA fragment downstream of lysJ and found an argE homolog in a putative operon composed of lysJ-orfC-orfD-argE homologs. A knockout mutant of the argE homolog showed significantly slow growth on a minimal medium, and the growth was markedly improved by addition of lysine. We therefore termed this gene lysK. Purified LysK protein has deacetylating activities for both N(2)-acetyllysine and N(2)-acetylornithine at almost equal efficiency. These results suggest that lysK which may share an ancestor with argE functions not only for the lysine biosynthesis, but also for arginine biosynthesis in Thermus thermophilus. << Less
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Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus.
Horie A., Tomita T., Saiki A., Kono H., Taka H., Mineki R., Fujimura T., Nishiyama C., Kuzuyama T., Nishiyama M.
Although the latter portion of lysine biosynthesis, the conversion of alpha-aminoadipate (AAA) to lysine, in Thermus thermophilus is similar to the latter portion of arginine biosynthesis, enzymes homologous to ArgA and ArgJ are absent from the lysine pathway. Because ArgA and ArgJ are known to mo ... >> More
Although the latter portion of lysine biosynthesis, the conversion of alpha-aminoadipate (AAA) to lysine, in Thermus thermophilus is similar to the latter portion of arginine biosynthesis, enzymes homologous to ArgA and ArgJ are absent from the lysine pathway. Because ArgA and ArgJ are known to modify the amino group of glutamate to avoid intramolecular cyclization of intermediates, their absence suggests that the pathway includes an alternative N-modification system. We reconstituted the conversion of AAA to lysine and found that the amino group of AAA is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW; that the side chain of AAA is converted to the lysyl side chain while still attached to LysW; and that lysine is subsequently liberated from the LysW-lysine fusion. The fact that biosynthetic enzymes recognize the acidic globular domain of LysW indicates that LysW acts as a carrier protein or protein scaffold for the biosynthetic enzymes. This study thus reveals the previously unknown function of a small protein in primary metabolism. << Less
Nat. Chem. Biol. 5:673-679(2009) [PubMed] [EuropePMC]
This publication is cited by 9 other entries.