Enzymes
UniProtKB help_outline | 986 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-ornithyl)-L-glutamate
Identifier
RHEA-COMP:13328
Reactive part
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- Name help_outline C-terminal-γ-(L-ornithyl)-L-glutamyl residue Identifier CHEBI:136763 Charge -1 Formula C10H17N3O5 SMILEShelp_outline N([C@H](C([O-])=O)CCC(N[C@@H](CCC[NH3+])C(=O)[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-ornithine Identifier CHEBI:46911 Charge 1 Formula C5H13N2O2 InChIKeyhelp_outline AHLPHDHHMVZTML-BYPYZUCNSA-O SMILEShelp_outline [NH3+]CCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 48 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:52676 | RHEA:52677 | RHEA:52678 | RHEA:52679 | |
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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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Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
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.
LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of α-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated pro ... >> More
LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of α-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection of AAA but also uses LysW to protect the amino group of glutamate in arginine biosynthesis. 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. The crystal structure of ArgX, the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW, was determined in complex with LysW. Structural comparison and enzymatic characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX identify the amino acid motif responsible for substrate discrimination between AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at different stages of evolution led to ArgX and LysX. << Less
Nat. Chem. Biol. 9:277-283(2013) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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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.