Reaction participants Show >> << Hide
- 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
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Namehelp_outline
N6-acetyl-L-lysyl-[protein]
Identifier
RHEA-COMP:10731
Reactive part
help_outline
- Name help_outline N6-acetyl-L-lysine residue Identifier CHEBI:61930 Charge 0 Formula C8H14N2O2 SMILEShelp_outline CC(=O)NCCCC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
(S)-2-amino-6-oxohexanoyl-[protein]
Identifier
RHEA-COMP:12448
Reactive part
help_outline
- Name help_outline (S)-2-amino-6-oxohexanoate residue Identifier CHEBI:131803 Charge 0 Formula C6H9NO2 SMILEShelp_outline [H]C(CCC[C@@H](C(*)=O)N*)=O 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
- Name help_outline acetamide Identifier CHEBI:27856 (Beilstein: 1071207; CAS: 60-35-5) help_outline Charge 0 Formula C2H5NO InChIKeyhelp_outline DLFVBJFMPXGRIB-UHFFFAOYSA-N SMILEShelp_outline CC(N)=O 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 H2O2 Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 426 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:51648 | RHEA:51649 | RHEA:51650 | RHEA:51651 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Publications
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Lysyl oxidase 3 is a dual-specificity enzyme involved in STAT3 deacetylation and deacetylimination modulation.
Ma L., Huang C., Wang X.J., Xin D.E., Wang L.S., Zou Q.C., Zhang Y.S., Tan M.D., Wang Y.M., Zhao T.C., Chatterjee D., Altura R.A., Wang C., Xu Y.S., Yang J.H., Fan Y.S., Han B.H., Si J., Zhang X., Cheng J., Chang Z., Chin Y.E.
In mammalian cells, histone deacetylase (HDAC) and Sirtuin (SIRT) are two families responsible for removing acetyl groups from acetylated proteins. Here, we describe protein deacetylation coupled with deacetylimination as a function of lysyl oxidase (LOX) family members. LOX-like 3 (Loxl3) associa ... >> More
In mammalian cells, histone deacetylase (HDAC) and Sirtuin (SIRT) are two families responsible for removing acetyl groups from acetylated proteins. Here, we describe protein deacetylation coupled with deacetylimination as a function of lysyl oxidase (LOX) family members. LOX-like 3 (Loxl3) associates with Stat3 in the nucleus to deacetylate and deacetyliminate Stat3 on multiple acetyl-lysine sites. Surprisingly, Loxl3 N-terminal scavenger receptor cysteine-rich (SRCR) repeats, rather than the C-terminal oxidase catalytic domain, represent the major deacetylase/deacetyliminase activity. Loxl3-mediated deacetylation/deacetylimination disrupts Stat3 dimerization, abolishes Stat3 transcription activity, and restricts cell proliferation. In Loxl3-/-mice, Stat3 is constitutively acetylated and naive CD4<sup>+</sup> T cells are potentiated in Th17/Treg cell differentiation. When overexpressed, the SRCR repeats from other LOX family members can catalyze protein deacetylation/deacetylimination. Thus, our findings delineate a hitherto-unknown mechanism of protein deacetylation and deacetylimination catalyzed by lysyl oxidases. << Less