1.8.5.8: eukaryotic sulfide quinone oxidoreductase
This is an abbreviated version!
For detailed information about eukaryotic sulfide quinone oxidoreductase, go to the full flat file.
Reaction
Synonyms
glutathione:CoQ reductase, HMT2, ScSQR, SQOR, SQR, Sqrdl, sulfide : quinone oxidoreductase, sulfide quinone oxidoreductase, sulfide:quinone oxidoreductase
ECTree
1.8.5.8 eukaryotic sulfide quinone oxidoreductaseAdvanced search results
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Inhibitors
Inhibitors on EC 1.8.5.8 - eukaryotic sulfide quinone oxidoreductase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
cyanide
cyanide treatment destabilized human SQOR and leads to its inactivation with concomitant loss of the bridging sulfane sulfur. Addition of sulfide to inactive cyanide treated enzyme leads to recovery of active SQOR, indicating that the oxidation state of the active site cysteines is preserved upon cyanide treatment. Crystallization of SQOR with cyanide led to the capture of a 379Cys N-(201Cys-disulfanyl)-methanimido thioate intermediate. Spectral and kinetic characterization of cyanolysis-induced dismantling followed by sulfide-dependent rebuilding of the trisulfide cofactor, proposed mechanism for cyanolysis and cysteine trisulfide rebuilding in SQOR, overview
H2S
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the enzyme activity decreases when the ambient sulfide concentration exceeds 0.3 mM
2-ethoxy-4-(4-fluorophenyl)-5H-indeno[1,2-b]pyridine-3-carbonitrile
HTS12441
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2-ethoxy-4-(4-fluorophenyl)-5H-indeno[1,2-b]pyridine-3-carbonitrile
HTS12441
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2-ethoxy-4-(4-fluorophenyl)-5H-indeno[1,2-b]pyridine-3-carbonitrile
HTS12441
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2-methoxy-4-phenyl-5H-indeno[1,2-b]pyridine-3-carbonitrile
RH00520
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4-(2-chlorophenyl)-2-methoxy-5H-indeno[1,2-b]pyridine-3-carbonitrile
HTS12442
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4-(2-chlorophenyl)-2-methoxy-5H-indeno[1,2-b]pyridine-3-carbonitrile
HTS12442
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4-(2-chlorophenyl)-2-methoxy-5H-indeno[1,2-b]pyridine-3-carbonitrile
HTS12442
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4-(4-aminophenyl)-6-methoxy-3'-methyl[2,2'-bipyridine]-5-carbonitrile
STI1, SQOR-targeted inhibitor 1, STI1 is a potent and highly selective inhibitor of SQOR. The first-in-class inhibitor of sulfide:quinone oxidoreductase binds to the CoQ-binding pocket in human SQOR and protects against adverse cardiac remodeling and heart failure. Ability of STI1 to protect against pathological remodelling of the left ventricle and the progression to heart failure patients with reduced ejection fraction (HFrEF). Docking of STI1 to ligand-free SQOR (PDB ID 6M06) and modeling of the SQOR-STI1 complex
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4-(4-aminophenyl)-6-methoxy-3'-methyl[2,2'-bipyridine]-5-carbonitrile
STI1, SQOR-targeted inhibitor 1, STI1 is a potent and highly selective inhibitor of SQOR. The first-in-class inhibitor of sulfide:quinone oxidoreductase binds to the CoQ-binding pocket in SQOR and protects against adverse cardiac remodeling and heart failure
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4-(4-aminophenyl)-6-methoxy-3'-methyl[2,2'-bipyridine]-5-carbonitrile
STI1, SQOR-targeted inhibitor 1, STI1 is a potent and highly selective inhibitor of SQOR. STI1 is a competitive inhibitor that binds with high selectivity to the coenzyme Q-binding pocket in SQOR. STI1 exhibits very low cytotoxicity and attenuats the hypertrophic response of neonatal rat ventricular cardiomyocytes and H9c2 cells induced by neurohormonal stressors
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additional information
inhibitor identification by high-throughput screening of a small-molecule library, followed by focused medicinal chemistry optimization and structure-based design. The coenzyme Q-binding pocket in human SQOR is a druggable target. Discovery of over 500 compounds that inhibit SQOR with IC50 below 0.02 mM, and discovery of a potent series (class A/A') of SQOR inhibitors, which block substrate access to the CoQ-binding site leading to competitive inhibition
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additional information
inhibitor identification by high-throughput screening of a small-molecule library, followed by focused medicinal chemistry optimization and structure-based design. The coenzyme Q-binding pocket in human SQOR is a druggable target. Discovery of over 500 compounds that inhibit SQOR with IC50 below 0.02 mM, and discovery of a potent series (class A/A') of SQOR inhibitors, which block substrate access to the CoQ-binding site leading to competitive inhibition
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additional information
inhibitor identification by high-throughput screening of a small-molecule library, followed by focused medicinal chemistry optimization and structure-based design. STI1 is able to inhibit hypertrophic growth of neonatal rat ventricular cardiomyocytes (NRVMs) and H9c2 cells induced by various agonists, e.g. angiotensin II
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