Enzymes
UniProtKB help_outline | 8,937 proteins |
Reaction participants Show >> << Hide
- Name help_outline a quinone Identifier CHEBI:132124 Charge 0 Formula C6O2R4 SMILEShelp_outline O=C1C(*)=C(*)C(=O)C(*)=C1* 2D coordinates Mol file for the small molecule Search links Involved in 127 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 6,148 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-methionyl-[protein]
Identifier
RHEA-COMP:12313
Reactive part
help_outline
- Name help_outline L-methionine residue Identifier CHEBI:16044 Charge 0 Formula C5H9NOS SMILEShelp_outline O=C(*)[C@@H](N*)CCSC 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a quinol Identifier CHEBI:24646 Charge 0 Formula C6H2O2R4 SMILEShelp_outline OC1=C(*)C(*)=C(O)C(*)=C1* 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-methionyl-(R)-S-oxide-[protein]
Identifier
RHEA-COMP:12314
Reactive part
help_outline
- Name help_outline L-methionine (R)-S-oxide residue Identifier CHEBI:45764 Charge 0 Formula C5H9NO2S SMILEShelp_outline C(*)(=O)[C@@H](N*)CC[S@](=O)C 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:51296 | RHEA:51297 | RHEA:51298 | RHEA:51299 | |
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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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Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons.
Gennaris A., Ezraty B., Henry C., Agrebi R., Vergnes A., Oheix E., Bos J., Leverrier P., Espinosa L., Szewczyk J., Vertommen D., Iranzo O., Collet J.F., Barras F.
The reactive species of oxygen and chlorine damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to methionine sulfoxide, which can cause a loss of biological activity. To rescue proteins with methionine sulfoxide resi ... >> More
The reactive species of oxygen and chlorine damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to methionine sulfoxide, which can cause a loss of biological activity. To rescue proteins with methionine sulfoxide residues, living cells express methionine sulfoxide reductases (Msrs) in most subcellular compartments, including the cytosol, mitochondria and chloroplasts. Here we report the identification of an enzymatic system, MsrPQ, repairing proteins containing methionine sulfoxide in the bacterial cell envelope, a compartment particularly exposed to the reactive species of oxygen and chlorine generated by the host defence mechanisms. MsrP, a molybdo-enzyme, and MsrQ, a haem-binding membrane protein, are widely conserved throughout Gram-negative bacteria, including major human pathogens. MsrPQ synthesis is induced by hypochlorous acid, a powerful antimicrobial released by neutrophils. Consistently, MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA. For this activity, MsrPQ uses electrons from the respiratory chain, which represents a novel mechanism to import reducing equivalents into the bacterial cell envelope. A remarkable feature of MsrPQ is its capacity to reduce both rectus (R-) and sinister (S-) diastereoisomers of methionine sulfoxide, making this oxidoreductase complex functionally different from previously identified Msrs. The discovery that a large class of bacteria contain a single, non-stereospecific enzymatic complex fully protecting methionine residues from oxidation should prompt a search for similar systems in eukaryotic subcellular oxidizing compartments, including the endoplasmic reticulum. << Less
Nature 528:409-412(2015) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.