Enzymes
| UniProtKB help_outline | 110 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
L-lysyl-[lipoyl-carrier protein]
Identifier
RHEA-COMP:10500
Reactive part
help_outline
- Name help_outline L-lysine residue Identifier CHEBI:29969 Charge 1 Formula C6H13N2O SMILEShelp_outline C([C@@H](C(*)=O)N*)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 134 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
Identifier
RHEA-COMP:10494
Reactive part
help_outline
- Name help_outline N6-[(R)-lipoyl]-L-lysine residue Identifier CHEBI:83099 Charge 0 Formula C14H24N2O2S2 SMILEShelp_outline *-N[C@@H](CCCCNC(=O)CCCC[C@@H]1CCSS1)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-lysyl-[glycine-cleavage complex H protein]
Identifier
RHEA-COMP:10501
Reactive part
help_outline
- Name help_outline L-lysine residue Identifier CHEBI:29969 Charge 1 Formula C6H13N2O SMILEShelp_outline C([C@@H](C(*)=O)N*)CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 134 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein]
Identifier
RHEA-COMP:10502
Reactive part
help_outline
- Name help_outline N6-[(R)-lipoyl]-L-lysine residue Identifier CHEBI:83099 Charge 0 Formula C14H24N2O2S2 SMILEShelp_outline *-N[C@@H](CCCCNC(=O)CCCC[C@@H]1CCSS1)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:16413 | RHEA:16414 | RHEA:16415 | RHEA:16416 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| MetaCyc help_outline |
Publications
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A complex lipoate utilization pathway in Listeria monocytogenes.
Christensen Q.H., Hagar J.A., O'Riordan M.X., Cronan J.E.
Although a complete pathway of lipoic acid metabolism has been established in Escherichia coli, lipoic acid metabolism in other bacteria is more complex and incompletely understood. Listeria monocytogenes has been shown to utilize two lipoate-protein ligases for lipoic acid scavenging, whereas onl ... >> More
Although a complete pathway of lipoic acid metabolism has been established in Escherichia coli, lipoic acid metabolism in other bacteria is more complex and incompletely understood. Listeria monocytogenes has been shown to utilize two lipoate-protein ligases for lipoic acid scavenging, whereas only one of the ligases can function in utilization of host-derived lipoic acid-modified peptides. We report that lipoic acid scavenging requires not only ligation of lipoic acid but also a lipoyl relay pathway in which an amidotransferase transfers lipoyl groups to the enzyme complexes that require the cofactor for activity. In addition, we provide evidence for a new lipoamidase activity that could allow utilization of lipoyl peptides by lipoate-protein ligase. These data support a model of an expanded, three-enzyme pathway for lipoic acid scavenging that seems widespread in the Firmicutes phylum of bacteria. << Less