Enzymes
| UniProtKB help_outline | 1,804 proteins |
| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline (R)-noradrenaline Identifier CHEBI:72587 Charge 1 Formula C8H12NO3 InChIKeyhelp_outline SFLSHLFXELFNJZ-QMMMGPOBSA-O SMILEShelp_outline C=1(C=CC(=CC1O)[C@H](C[NH3+])O)O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-glutaminyl-[protein]
Identifier
RHEA-COMP:10207
Reactive part
help_outline
- Name help_outline L-glutamine residue Identifier CHEBI:30011 Charge 0 Formula C5H8N2O2 SMILEShelp_outline O=C(*)[C@@H](N*)CCC(=O)N 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
5-(R)-noradrenalinyl-L-glutamyl-[protein]
Identifier
RHEA-COMP:17054
Reactive part
help_outline
- Name help_outline 5-glutamyl noradrenaline residue Identifier CHEBI:167178 Charge 0 Formula C13H16N2O5 SMILEShelp_outline O=C(*)[C@@H](N*)CCC(=O)NC[C@@H](C1=CC(=C(C=C1)O)O)O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 518 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:66560 | RHEA:66561 | RHEA:66562 | RHEA:66563 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| Gene Ontology help_outline |
Publications
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Histaminylation of fibrinogen by tissue transglutaminase-2 (TGM-2): potential role in modulating inflammation.
Lai T.S., Greenberg C.S.
Plasma fibrinogen plays an important role in hemostasis and inflammation. Fibrinogen is converted to fibrin to impede blood loss and serves as the provisional matrix that aids wound healing. Fibrinogen also binds to cytokine activated endothelial cells and promotes the binding and migration of leu ... >> More
Plasma fibrinogen plays an important role in hemostasis and inflammation. Fibrinogen is converted to fibrin to impede blood loss and serves as the provisional matrix that aids wound healing. Fibrinogen also binds to cytokine activated endothelial cells and promotes the binding and migration of leukocytes into tissues during inflammation. Tissue transglutaminase (TGM-2) released from injured cells could cross-link fibrinogen to form multivalent complexes that could promote adhesion of platelets and vascular cells to endothelium. Histamine released by mast cells is a potent biogenic amine that promotes inflammation. The covalent attachment of histamine to proteins (histaminylation) by TGM-2 could modify local inflammatory reactions. We investigated TGM-2 crosslinking of several biogenic amines (serotonin, histamine, dopamine and noradrenaline) to fibrinogen. We identified histaminylation of fibrinogen by TGM-2 as a preferred reaction in solid and solution phase transglutaminase assays. Histamine caused a concentration-dependent inhibition of fibrinogen cross-linking by TGM-2. Fibrinogen that was not TGM-2 crosslinked bound to unactivated endothelial cells with low affinity. However, the binding was increased by sevenfold when fibrinogen was cross-linked by TGM-2. Histaminylation of fibrinogen also inhibited TGM-2 crosslinking of fibrinogen and the binding to un-activated HUVEC cells by 75–90 %. In summary, the histaminylation of fibrinogen by TGM-2 could play a role in modifying inflammation by sequestering free histamine and by inhibiting TGM-2 crosslinking of fibrinogen. << Less
Amino Acids 45:857-864(2013) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Transglutaminase-mediated transamidation of serotonin, dopamine and noradrenaline to fibronectin: evidence for a general mechanism of monoaminylation.
Hummerich R., Thumfart J.O., Findeisen P., Bartsch D., Schloss P.
The activity of some small GTPases is regulated by covalent transamidation of serotonin (5-hydropxytryptamien) to glutamine residues of the enzymes. This process is mediated by transglutaminase (TGase) and is termed "serotonylation". In addition, serotonylation of neural proteins and proteins of t ... >> More
The activity of some small GTPases is regulated by covalent transamidation of serotonin (5-hydropxytryptamien) to glutamine residues of the enzymes. This process is mediated by transglutaminase (TGase) and is termed "serotonylation". In addition, serotonylation of neural proteins and proteins of the extracellular matrix such as fibronectin has been demonstrated. Here we show that the catecholamines dopamine (DA) and noradrenaline (NA) inhibit serotonylation of fibronectin and that DA and NA themselves can be selectively transamidated into fibronectin by TGase. All three biogenic monoamines also block TGase-mediated transamidation of another monoamine, monodansylacadaverine, into fibronectin, suggesting a general mechanism of TGase-mediated "monoaminylation". << Less
FEBS Lett. 586:3421-3428(2012) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.