Reaction participants Show >> << Hide
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Namehelp_outline
S-nitroso-L-cysteinyl-[SCAN]
Identifier
RHEA-COMP:19069
Reactive part
help_outline
- Name help_outline S-nitroso-L-cysteine residue Identifier CHEBI:149494 Charge 0 Formula C3H4N2O2S SMILEShelp_outline S(C[C@@H](C(*)=O)N*)N=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-cysteinyl-[protein]
Identifier
RHEA-COMP:10131
Reactive part
help_outline
- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 128 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-cysteinyl-[SCAN]
Identifier
RHEA-COMP:19068
Reactive part
help_outline
- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 128 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
S-nitroso-L-cysteinyl-[protein]
Identifier
RHEA-COMP:17091
Reactive part
help_outline
- Name help_outline S-nitroso-L-cysteine residue Identifier CHEBI:149494 Charge 0 Formula C3H4N2O2S SMILEShelp_outline S(C[C@@H](C(*)=O)N*)N=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:78387 | RHEA:78388 | RHEA:78389 | RHEA:78390 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Publications
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An enzyme that selectively S-nitrosylates proteins to regulate insulin signaling.
Zhou H.L., Grimmett Z.W., Venetos N.M., Stomberski C.T., Qian Z., McLaughlin P.J., Bansal P.K., Zhang R., Reynolds J.D., Premont R.T., Stamler J.S.
Acyl-coenzyme A (acyl-CoA) species are cofactors for numerous enzymes that acylate thousands of proteins. Here, we describe an enzyme that uses S-nitroso-CoA (SNO-CoA) as its cofactor to S-nitrosylate multiple proteins (SNO-CoA-assisted nitrosylase, SCAN). Separate domains in SCAN mediate SNO-CoA ... >> More
Acyl-coenzyme A (acyl-CoA) species are cofactors for numerous enzymes that acylate thousands of proteins. Here, we describe an enzyme that uses S-nitroso-CoA (SNO-CoA) as its cofactor to S-nitrosylate multiple proteins (SNO-CoA-assisted nitrosylase, SCAN). Separate domains in SCAN mediate SNO-CoA and substrate binding, allowing SCAN to selectively catalyze SNO transfer from SNO-CoA to SCAN to multiple protein targets, including the insulin receptor (INSR) and insulin receptor substrate 1 (IRS1). Insulin-stimulated S-nitrosylation of INSR/IRS1 by SCAN reduces insulin signaling physiologically, whereas increased SCAN activity in obesity causes INSR/IRS1 hypernitrosylation and insulin resistance. SCAN-deficient mice are thus protected from diabetes. In human skeletal muscle and adipose tissue, SCAN expression increases with body mass index and correlates with INSR S-nitrosylation. S-nitrosylation by SCAN/SNO-CoA thus defines a new enzyme class, a unique mode of receptor tyrosine kinase regulation, and a revised paradigm for NO function in physiology and disease. << Less
Cell 0:0-0(2023) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.