Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline D-histidine Identifier CHEBI:142967 Charge 0 Formula C6H9N3O2 InChIKeyhelp_outline HNDVDQJCIGZPNO-RXMQYKEDSA-N SMILEShelp_outline C=1(N=CNC1)C[C@H](C(=O)[O-])[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 868 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate Identifier CHEBI:141808 Charge 0 Formula C10H16N4O4 InChIKeyhelp_outline PQUPEWJRDBYFHU-JGVFFNPUSA-N SMILEShelp_outline N=1C(=CNC1)C[C@@H]([NH2+]CC[C@H]([NH3+])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 H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-methyl-5'-thioadenosine Identifier CHEBI:17509 (Beilstein: 42420; CAS: 2457-80-9) help_outline Charge 0 Formula C11H15N5O3S InChIKeyhelp_outline WUUGFSXJNOTRMR-IOSLPCCCSA-N SMILEShelp_outline CSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 34 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59088 | RHEA:59089 | RHEA:59090 | RHEA:59091 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus.
Ghssein G., Brutesco C., Ouerdane L., Fojcik C., Izaute A., Wang S., Hajjar C., Lobinski R., Lemaire D., Richaud P., Voulhoux R., Espaillat A., Cava F., Pignol D., Borezee-Durant E., Arnoux P.
Metal acquisition is a vital microbial process in metal-scarce environments, such as inside a host. Using metabolomic exploration, targeted mutagenesis, and biochemical analysis, we discovered an operon in Staphylococcus aureus that encodes the different functions required for the biosynthesis and ... >> More
Metal acquisition is a vital microbial process in metal-scarce environments, such as inside a host. Using metabolomic exploration, targeted mutagenesis, and biochemical analysis, we discovered an operon in Staphylococcus aureus that encodes the different functions required for the biosynthesis and trafficking of a broad-spectrum metallophore related to plant nicotianamine (here called staphylopine). The biosynthesis of staphylopine reveals the association of three enzyme activities: a histidine racemase, an enzyme distantly related to nicotianamine synthase, and a staphylopine dehydrogenase belonging to the DUF2338 family. Staphylopine is involved in nickel, cobalt, zinc, copper, and iron acquisition, depending on the growth conditions. This biosynthetic pathway is conserved across other pathogens, thus underscoring the importance of this metal acquisition strategy in infection. << Less
Science 352:1105-1109(2016) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.