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Information on EC 1.13.11.18 - persulfide dioxygenase
for references in articles please use BRENDA:EC1.13.11.18
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EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.11 With incorporation of two atoms of oxygen
1.13.11.18 persulfide dioxygenase
IUBMB Comments
An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically .
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
- 1.13.11.18
-
social
-
ethylmalonic
- encephalopathy
-
attitudes
-
authoritarianism
-
right-wing
-
prejudice
-
ideology
- thiosulfate
-
intergroup
-
petechia
-
acrocyanosis
-
political
- rhodanese
- polysulfides
-
sulfide:quinone
-
inequality
-
group-based
-
orthostatic
-
conservatism
-
lesbian
-
cross-lagged
-
endorsement
-
pseudaminobacter
- 1-hydroxy-2-naphthoate
-
ingroup
- medicine
Reaction Schemes
show+
+
=
+
+
2
Synonyms
sdo, ethe1, sulfur dioxygenase, persulfide dioxygenase, sulfur oxygenase, afe_0269, fe(ii)-containing persulfide dioxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BAE27_01805
ETHE1
ETHE1-like sulfur dioxygenase
PDO
SDO
SOR
sulfur dioxygenase
sulfur oxygenase
-
-
-
-
sulfur oxygenase/reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+
overall reaction
-
-
-
S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
(1a)
-
-
-
S-sulfinatoglutathione + H2O = glutathione + sulfite + H+
(1b), spontaneous
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
S-sulfanylglutathione:oxygen oxidoreductase
An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
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CAS REGISTRY NUMBER
COMMENTARY
37256-58-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bacillithiol persulfide + O2
bacillithiol + sulfite
Substrates: -
Products: -
Products: -
?
gamma-glutamyl-homocysteinyl-glycine + O2
gamma-glutamyl-homocysteinyl-SO2H + ?
Substrates: mechanism-based inhibitor, accepted as an alternative substrate and converted to glutamyl-homocysteinyl-SO2H
Products: -
Products: -
?
S-sulfanyl-L-cysteine + O2
L-cysteine + sulfite
Substrates: -
Products: -
Products: -
?
S-sulfanylglutathione + O2
glutathione + sulfite
Substrates: -
Products: -
Products: -
?
S-sulfanylglutathione + O2
sulfite + glutathione + H+
-
Substrates: -
Products: -
Products: -
?
sulfur + O2 + H2O
thiosulfate
-
Substrates: -
Products: in the presence of reduced glutathione and 2,2'-dipyridyl
Products: in the presence of reduced glutathione and 2,2'-dipyridyl
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
-
Substrates: -
Products: -
Products: -
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
-
Substrates: incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
Products: -
Products: -
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
-
Substrates: -
Products: -
Products: -
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
-
Substrates: incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
Products: -
Products: -
?
glutathione + sulfite + 2 H+
S-sulfanylglutathione + O2 + H2O
Substrates: -
Products: -
Products: -
r
glutathione + sulfite + 2 H+
S-sulfanylglutathione + O2 + H2O
-
Substrates: -
Products: -
Products: -
r
S-sulfanylglutathione + O2 + H2O
glutathione + sulfite + 2 H+
Substrates: -
Products: -
Products: -
r
S-sulfanylglutathione + O2 + H2O
glutathione + sulfite + 2 H+
Substrates: -
Products: -
Products: -
?
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: low amount of thiosulfate observed may result from a chemical reaction between sulfite and elemental sulfur
Products: low amount of thiosulfate observed may result from a chemical reaction between sulfite and elemental sulfur
ir
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: S2O32- may be formed through a secondary, non-enzymatic reaction
Products: S2O32- may be formed through a secondary, non-enzymatic reaction
ir
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: -
Products: -
?
sulfur + O2 + H2O
sulfite
-
Substrates: -
Products: S2O32- may be formed through a secondary, non-enzymatic reaction
Products: S2O32- may be formed through a secondary, non-enzymatic reaction
ir
additional information
?
-
Substrates: Arabidopsis ETHE1 catalyzes the glutathione persulfide-dependent consumption of oxygen
Products: -
Products: -
?
additional information
?
-
-
Substrates: BpPRF is a bifunctional enzyme that uses the rhodanese domain to preferentially catalyze sulfur transfer from thiosulfate to GSH to form sulfite and GSSH and uses the PDO domain to oxidize GSSH to sulfite
Products: -
Products: -
?
additional information
?
-
-
Substrates: cysteine persulfide and thiosulfate are no substrates
Products: -
Products: -
?
additional information
?
-
Substrates: coupled persulfide dioxygenase-persulfide transferase (cPDO-PT) activity assay producing thiosulfate as product preferentially from CoASSH and bacillithiol persulfide. CstB does not catalyze the formation of thiosulfate from reduced low molecular weight thiol, oxidized low molecular weight disulfide or Na2S. Cysteine persulfide (CSSH) and glutathione persulfide (GSSH) also serve as persulfide substrates for wild-type CstB but are poorer substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: coupled persulfide dioxygenase-persulfide transferase (cPDO-PT) activity assay producing thiosulfate as product preferentially from CoASSH and bacillithiol persulfide. CstB does not catalyze the formation of thiosulfate from reduced low molecular weight thiol, oxidized low molecular weight disulfide or Na2S. Cysteine persulfide (CSSH) and glutathione persulfide (GSSH) also serve as persulfide substrates for wild-type CstB but are poorer substrates
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-sulfanylglutathione + O2
sulfite + glutathione + H+
-
Substrates: -
Products: -
Products: -
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
-
Substrates: incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
Products: -
Products: -
?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
-
Substrates: incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
Products: -
Products: -
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
Products: further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
?
sulfur + O2 + H2O
sulfite
-
Substrates: incorporation of elemental sulfur
Products: -
Products: -
?
additional information
?
-
Substrates: Arabidopsis ETHE1 catalyzes the glutathione persulfide-dependent consumption of oxygen
Products: -
Products: -
?
additional information
?
-
-
Substrates: BpPRF is a bifunctional enzyme that uses the rhodanese domain to preferentially catalyze sulfur transfer from thiosulfate to GSH to form sulfite and GSSH and uses the PDO domain to oxidize GSSH to sulfite
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
non-heme iron
additional information
Fe2+
-
required, the PDO domain active site contains a mononuclear non-heme iron coordinated by His58, His114, and Asp133 comprising a 2His:1Asp facial triad. The remaining coordination sites are occupied by water molecules giving an octrahedral geometry around ferrous iron. The wild-type enzyme contains 0.60 mol iron per mol of enzyme, the mutant C314S 0.46 mol iron/mol enzyme
additional information
the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed
additional information
the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed
additional information
-
the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
gamma-glutamyl-homocysteinyl-glycine
mechanism-based inhibitor, accepted as an alternative substrate and converted to glutamyl-homocysteinyl-SO2H, which fails to undergo the final hydrolysis step in the catalytic cycle, leading to inhibition. Maximum inhibition to 30% of initial activity
-
H2O2
-
strong inhibition, reversible by subsequent addition of catalase and glutathione
sulfite
-
sulfite build up can potentially inhibit PDO activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-dipyridyl
-
stimulation at low concentrations e.g. 0.1 mM, may protect glutathione from destruction
ascorbate
-
addition of 2.5 mM ascorbate to the standard assay results in an 20% increase in the PDO-specific activity
glutathione
-
the enzyme activity shows a s trong positive correlation with GSH contents
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Intergroup contact, social dominance, and environmental concern: A test of the cognitive-liberalization hypothesis.
Adenomatous Polyposis Coli
ETHE1 overexpression promotes SIRT1 and PGC1? mediated aerobic glycolysis, oxidative phosphorylation, mitochondrial biogenesis and colorectal cancer.
Anemia, Hypochromic
The mitochondrial sulfur dioxygenase ETHE1 is required for amino acid catabolism during carbohydrate starvation and embryo development in Arabidopsis thaliana.
Brain Diseases
Acute and Chronic Management in an Atypical Case of Ethylmalonic Encephalopathy.
Brain Diseases
Acute Strokelike Presentation and Long-term Evolution of Diffusion Restriction Pattern in Ethylmalonic Encephalopathy.
Brain Diseases
Arabidopsis ETHE1 Encodes a Sulfur Dioxygenase That Is Essential for Embryo and Endosperm Development.
Brain Diseases
Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism.
Brain Diseases
Chronic Exposure to Sulfide causes Accelerated Degradation of Cytochrome c oxidase in Ethylmalonic Encephalopathy.
Brain Diseases
Combined treatment with oral metronidazole and N-acetylcysteine is effective in ethylmalonic encephalopathy.
Brain Diseases
Compromised therapeutic value of pediatric liver transplantation in ethylmalonic encephalopathy: A case report.
Brain Diseases
Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.
Brain Diseases
Deficiency of the mitochondrial sulfide regulator ETHE1 disturbs cell growth, glutathione level and causes proteome alterations outside mitochondria.
Brain Diseases
Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria.
Brain Diseases
ETHE1 overexpression promotes SIRT1 and PGC1? mediated aerobic glycolysis, oxidative phosphorylation, mitochondrial biogenesis and colorectal cancer.
Brain Diseases
Ethylmalonic encephalopathy ETHE1 p. D165H mutation alters the mitochondrial function in human skeletal muscle proteome.
Brain Diseases
Ethylmalonic encephalopathy ETHE1 R163W/R163Q mutations alter protein stability and redox properties of the iron centre.
Brain Diseases
Ethylmalonic encephalopathy is caused by mutations in ETHE1, a gene encoding a mitochondrial matrix protein.
Brain Diseases
Ethylmalonic encephalopathy: Clinical course and therapy response in an uncommon mild case with a severe ETHE1 mutation.
Brain Diseases
Expression of abiotic stress inducible ETHE1-like protein from rice is higher in roots and is regulated by calcium.
Brain Diseases
Expression of abiotic stress inducible ETHE1?like protein from rice is higher in roots and is regulated by calcium
Brain Diseases
Identification of a novel homozygous nonsense variant in a Chinese patient with ethylmalonic encephalopathy and a genotype-phenotype spectrum review.
Brain Diseases
Identification of new mutations in the ETHE1 gene in a cohort of 14 patients presenting with ethylmalonic encephalopathy.
Brain Diseases
Improved clinical outcome following liver transplant in patients with ethylmalonic encephalopathy.
Brain Diseases
Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy.
Brain Diseases
Mitochondrial diseases caused by toxic compound accumulation: from etiopathology to therapeutic approaches.
Brain Diseases
Mitochondrial Dysfunction and Redox Homeostasis Impairment as Pathomechanisms of Brain Damage in Ethylmalonic Encephalopathy: Insights from Animal and Human Studies.
Brain Diseases
Multiple sources of metabolic disturbance in ETHE1-related ethylmalonic encephalopathy.
Brain Diseases
Novel Compound Heterozygous Variants of ETHE1 Causing Ethylmalonic Encephalopathy in a Chinese Patient: A Case Report.
Brain Diseases
Novel ETHE1 mutation in a carrier couple having prior offspring affected with ethylmalonic encephalopathy: Genetic analysis, clinical management and reproductive outcome.
Brain Diseases
Protein polysulfidation-dependent persulfide dioxygenase activity of ethylmalonic encephalopathy protein 1.
Brain Diseases
Proteomics Reveals that Redox Regulation Is Disrupted in Patients with Ethylmalonic Encephalopathy.
Brain Diseases
Quantitative proteomics suggests metabolic reprogramming during ETHE1 deficiency.
Brain Diseases
Response to medical and a novel dietary treatment in newborn screen identified patients with ethylmalonic encephalopathy.
Brain Diseases
Staphylococcus aureus CstB Is a Novel Multidomain Persulfide Dioxygenase-Sulfurtransferase Involved in Hydrogen Sulfide Detoxification.
Brain Diseases
Stress response of OsETHE1 is altered in response to light and dark conditions.
Brain Diseases
Untargeted Metabolomics Analysis Reveals a Link between ETHE1-Mediated Disruptive Redox State and Altered Metabolic Regulation.
Brain Diseases
[Clinical and genetic analysis of a case with atypical ethyl malonate encephalopathy].
Carcinogenesis
ETHE1 overexpression promotes SIRT1 and PGC1? mediated aerobic glycolysis, oxidative phosphorylation, mitochondrial biogenesis and colorectal cancer.
Colorectal Neoplasms
ETHE1 overexpression promotes SIRT1 and PGC1? mediated aerobic glycolysis, oxidative phosphorylation, mitochondrial biogenesis and colorectal cancer.
Colorectal Neoplasms
Systems Biomedicine of Primary and Metastatic Colorectal Cancer Reveals Potential Therapeutic Targets.
Congenital Abnormalities
Total hip arthroplasty requiring subtrochanteric osteotomy for developmental hip dysplasia 5- to 14-year results.
COVID-19
U.S. public support for COVID-19 vaccine donation to low- and middle-income countries during the COVID-19 pandemic.
Craniocerebral Trauma
Increased Risks of Suicide Attempt and Suicidal Drug Overdose Following Admission for Head Injury in Patients with Depression.
Craniocerebral Trauma
Increasing Risks of Suicide Attempt and Suicidal Drug Overdose After Head Trauma in Patients With Sleep-Disordered Breathing: A Population-Based Study.
Craniosynostoses
Piezosurgical Suturectomy and Sutural Distraction Osteogenesis for the Treatment of Unilateral Coronal Synostosis.
Cytochrome-c Oxidase Deficiency
Chronic Exposure to Sulfide causes Accelerated Degradation of Cytochrome c oxidase in Ethylmalonic Encephalopathy.
Diabetic Nephropathies
Evaluating Pharmacological Effects of Two Major Components of Shuangdan Oral Liquid: Role of Danshensu and Paeonol in Diabetic Nephropathy Rat.
Enteritis
[Epidemiological impact of RV gastroenteritis in the Abruzzo Region: SDO analysis]
Epilepsy
Differences in Incidence and Risks of Suicide Attempt and Suicidal Drug Overdose between Patients with Epilepsy with and without Comorbid Depression.
Gastroenteritis
[Epidemiological impact of RV gastroenteritis in the Abruzzo Region: SDO analysis]
Hyperlipidemias
Metabolomics analysis of the therapeutic mechanism of Semen Descurainiae Oil on hyperlipidemia rats using 1 H-NMR and LC-MS.
Hypospadias
Hypospadias prevalence in the Emilia Romagna Region registry: Increasing or methodology?
Infections
The role of short-chain dehydrogenase/oxidoreductase, induced by salt stress, on host interaction of B. pseudomallei.
Melanoma
Second Diagnostic Opinion by Experienced Dermatopathologists in the Setting of a Referral Regional Melanoma Unit Significantly Improves the Clinical Management of Patients With Cutaneous Melanoma.
Melioidosis
Altered proteome of a Burkholderia pseudomallei mutant defective in short-chain dehydrogenase affects cell adhesion, biofilm formation and heat stress tolerance.
Metabolic Syndrome
Lipogenesis is decreased by grape seed proanthocyanidins according to liver proteomics of rats fed a high fat diet.
Mitochondrial Diseases
Acute Strokelike Presentation and Long-term Evolution of Diffusion Restriction Pattern in Ethylmalonic Encephalopathy.
Mitochondrial Diseases
Improved clinical outcome following liver transplant in patients with ethylmalonic encephalopathy.
Mitochondrial Diseases
Mitochondrial diseases caused by toxic compound accumulation: from etiopathology to therapeutic approaches.
Neoplasms
[Extending traceability of malignant testicular tumours using hospital discharge records: an experience in Veneto Region (Northern Italy)].
Neurodegenerative Diseases
Identification of a novel homozygous nonsense variant in a Chinese patient with ethylmalonic encephalopathy and a genotype-phenotype spectrum review.
Neurodegenerative Diseases
Response to medical and a novel dietary treatment in newborn screen identified patients with ethylmalonic encephalopathy.
Obesity
Obesity discrimination: the role of physical appearance, personal ideology, and anti-fat prejudice.
Ovarian Neoplasms
Salpingectomy for the Risk Reduction of Ovarian Cancer: Is It Time for a Salpingectomy-alone Approach?
Paraparesis, Spastic
Ethylmalonic encephalopathy: Clinical course and therapy response in an uncommon mild case with a severe ETHE1 mutation.
Parkinson Disease
Spatiotemporal characteristics of postsaccadic dynamic overshoot in young and elderly subjects.
persulfide dioxygenase deficiency
Deficiency of the mitochondrial sulfide regulator ETHE1 disturbs cell growth, glutathione level and causes proteome alterations outside mitochondria.
persulfide dioxygenase deficiency
ETHE1 and MOCS1 deficiencies: Disruption of mitochondrial bioenergetics, dynamics, redox homeostasis and endoplasmic reticulum-mitochondria crosstalk in patient fibroblasts.
persulfide dioxygenase deficiency
Evidence that thiol group modification and reactive oxygen species are involved in hydrogen sulfide-induced mitochondrial permeability transition pore opening in rat cerebellum.
persulfide dioxygenase deficiency
Evidence that Thiosulfate Inhibits Creatine Kinase Activity in Rat Striatum via Thiol Group Oxidation.
persulfide dioxygenase deficiency
Morphologic evidence of diffuse vascular damage in human and in the experimental model of ethylmalonic encephalopathy.
persulfide dioxygenase deficiency
Quantitative proteomics suggests metabolic reprogramming during ETHE1 deficiency.
persulfide dioxygenase deficiency
The Role of Persulfide Metabolism During Arabidopsis Seed Development Under Light and Dark Conditions.
persulfide dioxygenase deficiency
Untargeted Metabolomics Analysis Reveals a Link between ETHE1-Mediated Disruptive Redox State and Altered Metabolic Regulation.
Pulmonary Disease, Chronic Obstructive
Suicide Attempt and Suicidal Drug Overdose in Chronic Obstructive Pulmonary Disease Patients With or Without Depression.
Starvation
The mitochondrial sulfur dioxygenase ETHE1 is required for amino acid catabolism during carbohydrate starvation and embryo development in Arabidopsis thaliana.
Starvation
The Role of Persulfide Metabolism During Arabidopsis Seed Development Under Light and Dark Conditions.
Stroke
Suicidal drug overdose following stroke in elderly patients: a retrospective population-based cohort study.
Synostosis
Piezosurgical Suturectomy and Sutural Distraction Osteogenesis for the Treatment of Unilateral Coronal Synostosis.
Synovitis
Identification of pathways and genes associated with synovitis in osteoarthritis using bioinformatics analyses.
Testicular Neoplasms
[Extending traceability of malignant testicular tumours using hospital discharge records: an experience in Veneto Region (Northern Italy)].
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
bacillithiol persulfide
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
0.0011
CoASSH
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
0.02
S-sulfanyl-L-cysteine
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
additional information
additional information
-
kinetics of sulfur-transfer reaction
-
0.0078
S-sulfanylglutathione
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
0.037
S-sulfanylglutathione
-
recombinant mutant C314S, pH 7.4, 22°C
0.07
S-sulfanylglutathione
-
recombinant wild-type enzyme, pH 7.4, 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.7
bacillithiol persulfide
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
19.3
CoASSH
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
2 - 8
S-sulfanyl-L-cysteine
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
5
S-sulfanylglutathione
-
recombinant mutant C314S, pH 7.4, 22°C
6.5
S-sulfanylglutathione
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
143
S-sulfanylglutathione
-
recombinant wild-type enzyme, pH 7.4, 22°C
198
S-sulfanylglutathione
sigmoidal curve with Hill coefficient 2.3, pH 7.5, 40°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10944
bacillithiol persulfide
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
17545
CoASSH
recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity
1100