Enzymes
UniProtKB help_outline | 324 proteins |
Reaction participants Show >> << Hide
- 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hypobromite Identifier CHEBI:29250 (CAS: 14380-62-2) help_outline Charge -1 Formula BrO InChIKeyhelp_outline JGJLWPGRMCADHB-UHFFFAOYSA-N SMILEShelp_outline [O-]Br 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
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Namehelp_outline
L-tyrosyl-[protein]
Identifier
RHEA-COMP:10136
Reactive part
help_outline
- Name help_outline L-tyrosine residue Identifier CHEBI:46858 Charge 0 Formula C9H9NO2 SMILEShelp_outline O=C(*)[C@@H](N*)CC=1C=CC(=CC1)O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
3-bromo-L-tyrosyl-[protein]
Identifier
RHEA-COMP:17686
Reactive part
help_outline
- Name help_outline 3-bromo-L-tyrosine residue Identifier CHEBI:183512 Charge 0 Formula C9H8BrNO2 SMILEShelp_outline OC1=CC=C(C[C@H](N-*)C(-*)=O)C=C1Br 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
Cross-references
RHEA:69356 | RHEA:69357 | RHEA:69358 | RHEA:69359 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Publications
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Peroxidasin-mediated bromine enrichment of basement membranes.
He C., Song W., Weston T.A., Tran C., Kurtz I., Zuckerman J.E., Guagliardo P., Miner J.H., Ivanov S.V., Bougoure J., Hudson B.G., Colon S., Voziyan P.A., Bhave G., Fong L.G., Young S.G., Jiang H.
Bromine and peroxidasin (an extracellular peroxidase) are essential for generating sulfilimine cross-links between a methionine and a hydroxylysine within collagen IV, a basement membrane protein. The sulfilimine cross-links increase the structural integrity of basement membranes. The formation of ... >> More
Bromine and peroxidasin (an extracellular peroxidase) are essential for generating sulfilimine cross-links between a methionine and a hydroxylysine within collagen IV, a basement membrane protein. The sulfilimine cross-links increase the structural integrity of basement membranes. The formation of sulfilimine cross-links depends on the ability of peroxidasin to use bromide and hydrogen peroxide substrates to produce hypobromous acid (HOBr). Once a sulfilimine cross-link is created, bromide is released into the extracellular space and becomes available for reutilization. Whether the HOBr generated by peroxidasin is used very selectively for creating sulfilimine cross-links or whether it also causes oxidative damage to bystander molecules (e.g., generating bromotyrosine residues in basement membrane proteins) is unclear. To examine this issue, we used nanoscale secondary ion mass spectrometry (NanoSIMS) imaging to define the distribution of bromine in mammalian tissues. We observed striking enrichment of bromine (<sup>79</sup>Br, <sup>81</sup>Br) in basement membranes of normal human and mouse kidneys. In peroxidasin knockout mice, bromine enrichment of basement membranes of kidneys was reduced by ∼85%. Proteomic studies revealed bromination of tyrosine-1485 in the NC1 domain of α2 collagen IV from kidneys of wild-type mice; the same tyrosine was brominated in collagen IV from human kidney. Bromination of tyrosine-1485 was reduced by >90% in kidneys of peroxidasin knockout mice. Thus, in addition to promoting sulfilimine cross-links in collagen IV, peroxidasin can also brominate a bystander tyrosine. Also, the fact that bromine enrichment is largely confined to basement membranes implies that peroxidasin activity is largely restricted to basement membranes in mammalian tissues. << Less
Proc. Natl. Acad. Sci. U.S.A. 117:15827-15836(2020) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
RHEA:69356 part of RHEA:69360 This reaction can occur spontaneously.