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Information on EC 1.13.11.19 - cysteamine dioxygenase
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1.13.11.19 cysteamine dioxygenaseIUBMB Comments
A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
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The enzyme appears in viruses and cellular organisms
Synonyms
cysteamine dioxygenase, 2-aminoethanethiol dioxygenase, cysteamine oxygenase, persulfurase, gm237, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-aminoethanethiol dioxygenase
ADO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminoethanethiol + O2 = hypotaurine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
2-aminoethanethiol:oxygen oxidoreductase
A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-mercaptoethanol can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
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CAS REGISTRY NUMBER
COMMENTARY
9033-41-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pantetheine + O2
pantothenate + cysteamine
-
oxidized at less than 3% of the cysteamine-dependent rate
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
-
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
-
?
additional information
additional information
-
-
specific for cysteamine
-
?
additional information
additional information
-
-
specific for cysteamine
-
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
specific for cysteamine
trace amounts of taurine and thiotaurine are also produced as a side reaction by further non-enzymatic reaction of hypotaurine
?
additional information
additional information
-
-
synthetic analogs of cysteamine oxidized: piperazinylcysteamine, N,N-dimethylcysteamine, trimethyl(2-mercaptoethyl)ammonium chloride, 2-mercaptoethanol, cysteine methyl ester
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Zn
Fe
-
a non-heme-iron protein, contains 1 g-atom of iron per mol of enzyme (based on a MW of 83000), nearly all of the iron is in the ferric state
Fe
-
nonheme iron involved in catalytic action of cysteamine oxygenase, high spin Fe(III)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
inhibition at high concentration, activation at low concentration
S
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Se
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Sulfide
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
stimulation at low concentration, inhibition at high concentration
hydroxylamine
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Se
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Sulfide
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
sulfur
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Effect of starvation and refeeding on cysteamine dioxygenase activity in rat liver and heart.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000021
-
substrate: hypertaurine, kidney, activity is lower than in mice kidney
0.000026
-
substrate: hypertaurine, liver, activity is lower than in mice liver
0.000037
-
substrate: hypertaurine, kidney, higher activity in mice kidney than in rat kidney
0.000091
-
substrate: hypertaurine, liver, higher activity in mice liver than in rat liver
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
Sprague-Dawley, rats switched from a high protein diet to a low protein diet or to a low protein diet supplemented with cysteamine do not demonstrate a change in tissue cysteamine dioxygenase activity over the course of 10 h.
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Cysteamine levels in plasma of rats fed the cysteamine supplemented diet are significantly higher than those in tissues of rats fed basal diet. Rats fed the cysteamine-supplemented diet have no markedly elevated levels of hypotaurine in plasma.
brenda
additional information
-
hypotaurine is not in brain of either Vanin-1 (+/+) or Vanin-1 (-/-) mice that had been fed a non-purified rodent diet.
brenda
-
Cysteamine levels in brain of rats fed the cysteamine supplemented diet are significantly higher than those in tissues of rats fed basal diet. Rats fed the cysteamine-supplemented diet have markedly elevated levels of hypotaurine in brain.
brenda
-
higher activity than in rat kidney. Hypotaurine is measurable in kidney, but levels are significantly higher in kidneys of the knock-out mice compared to wild-type mice.
brenda
-
lower activity than in mice kidney. Cysteamine levels in kidney of rats fed the cysteamine supplemented diet are significantly higher than those in tissues of rats fed basal diet. Rats fed the cysteamine-supplemented diet have markedly elevated levels of hypotaurine in kidney.
brenda
-
higher activity than in rat liver. hypotaurine is not in liver of either Vanin-1 (+/+) or Vanin-1 (-/-) mice that had been fed a non-purified rodent diet.
brenda
-
lower activity than in mice liver. Cysteamine levels in liver of rats fed the cysteamine supplemented diet are significantly higher than those in tissues of rats fed basal diet. Rats fed the cysteamine-supplemented diet have markedly elevated levels of hypotaurine in liver.
brenda
additional information
-
overview: distribution in animal tissues
brenda
additional information
-
overview: distribution in animal tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
functional roles of ADO in metabolism include removal of thiol substrates (cysteamine), thus regulating cysteine or cysteamine levels in body tissues and fluids and production of hypotaurine/taurine from cysteine metabolite cysteamine
metabolism
functional roles of ADO in metabolism include removal of thiol substrates (cysteamine), thus regulating cysteine or cysteamine levels in body tissues and fluids and production of hypotaurine/taurine from cysteine metabolite cysteamine
metabolism
-
the enzyme is involved in the taurine biosynthetic pathway. addition of taurine to cells grown in taurine-free medium has little effect on transcript levels of the biosynthetic pathway genes for cysteine dioxygenase (CDO), cysteine sulfinate decarboxylase (CSAD), or cysteamine dioxygenase (ADO). In contrast, supplementation with taurine causes a 30% reduction in transcript levels of the taurine transporter, TauT. Hypotaurine can be produced via of cysteamine, the end product of coenzyme A degradation, via oxidation by 2-aminoethanethiol dioxygenase (ADO). Taurine biosynthetic pathway from methionine?derived cysteine, overview
metabolism
-
the enzyme is involved in the taurine biosynthetic pathway. addition of taurine to cells grown in taurine-free medium has little effect on transcript levels of the biosynthetic pathway genes for cysteine dioxygenase (CDO), cysteine sulfinate decarboxylase (CSAD), or cysteamine dioxygenase (ADO). In contrast, supplementation with taurine causes a 30% reduction in transcript levels of the taurine transporter, TauT. Hypotaurine can be produced via of cysteamine, the end product of coenzyme A degradation, via oxidation by 2-aminoethanethiol dioxygenase (ADO). Taurine biosynthetic pathway from methionine?derived cysteine, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AEDO_DICDI
218
0
24708
Swiss-Prot
other Location (Reliability: 3)
AEDO_HUMAN
270
0
29751
Swiss-Prot
Mitochondrion (Reliability: 4)
AEDO_MOUSE
256
0
28372
Swiss-Prot
Mitochondrion (Reliability: 3)
B5X7N2_SALSA
248
0
27494
TrEMBL
Mitochondrion (Reliability: 5)
M2Y3X5_GALSU
219
0
25626
TrEMBL
other Location (Reliability: 2)
B3NF54_DROER
240
0
27254
TrEMBL
Mitochondrion (Reliability: 3)
B4KWX7_DROMO
242
0
27554
TrEMBL
other Location (Reliability: 5)
B4LGZ5_DROVI
242
0
27735
TrEMBL
Mitochondrion (Reliability: 5)
A0A1Z5JFZ1_FISSO
294
0
33010
TrEMBL
other Location (Reliability: 2)
A0A3S5IQT6_9TRYP
267
0
29082
TrEMBL
Mitochondrion (Reliability: 4)
B4MXE0_DROWI
270
0
29735
TrEMBL
Mitochondrion (Reliability: 5)
A0A088S2L1_9TRYP
271
0
29596
TrEMBL
other Location (Reliability: 4)
Q29FE0_DROPS
248
0
28152
TrEMBL
Mitochondrion (Reliability: 4)
B4PCS9_DROYA
240
0
27187
TrEMBL
Mitochondrion (Reliability: 3)
A0A422NM88_TRYRA
267
0
29373
TrEMBL
Mitochondrion (Reliability: 4)
A0A1Z5KG15_FISSO
294
0
33074
TrEMBL
other Location (Reliability: 2)
B3M422_DROAN
243
0
27642
TrEMBL
Mitochondrion (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
exhaustive dialysis against water: partial denaturation, dialysis against water brought to pH 7.5 with concentrated ammonia or against 0.01 M potassium phosphate buffer, pH 7.6, has no effect
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
relative expression level determination in cells grown in taurin-free or taurine-containing medium, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of taurine to cells grown in taurine-free medium has little effect on transcript levels of the biosynthetic pathway genes for cysteine dioxygenase (CDO), cysteine sulfinate decarboxylase (CSAD), or cysteamine dioxygenase (ADO). In contrast, supplementation with taurine causes a 30% reduction in transcript levels of the taurine transporter, TauT
addition of taurine to cells grown in taurine-free medium has little effect on transcript levels of the biosynthetic pathway genes for cysteine dioxygenase (CDO), cysteine sulfinate decarboxylase (CSAD), or cysteamine dioxygenase (ADO). In contrast, supplementation with taurine causes a 30% reduction in transcript levels of the taurine transporter, TauT
-
addition of taurine to cells grown in taurine-free medium has little effect on transcript levels of the biosynthetic pathway genes for cysteine dioxygenase (CDO), cysteine sulfinate decarboxylase (CSAD), or cysteamine dioxygenase (ADO). In contrast, supplementation with taurine causes a 30% reduction in transcript levels of the taurine transporter, TauT
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nozaki, M.
Nonheme iron dioxygenase
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
135-165
1974
Equus caballus
-
brenda
Richerson, R.B.; Ziegler, D.M.
Cysteamine dioxygenase
Methods Enzymol.
143
410-415
1987
Sus scrofa
brenda
Duffel, M.W.; Logan, D.J.; Ziegler, D.M.
Selenocysteine
Methods Enzymol.
143
148-155
1987
Equus caballus, Sus scrofa
brenda
Cavallini, D.; Scandurra, R.; Dupre, S.
Cysteamine oxygenase (horse kidney)
Methods Enzymol.
17B
479-483
1971
Equus caballus
-
brenda
Cavallini, D.; Federici, G.; Ricci, G.; Dupre, S.; Antonucci, A.; De Marco, C.
The specificity of cysteamine oxygenase
FEBS Lett.
56
348-351
1975
Equus caballus
brenda
Rotilio, G.; Federici, G.; Calabrese, L.; Costa, M.; Cavallini, D.
An electron paramagnetic resonance study of the nonheme iron of cysteamine oxygenase
J. Biol. Chem.
245
6235-6239
1970
Equus caballus
brenda
Cavallini, D.; Canella, C.; Federici, G.; Dupre, S.; Fiori, A.; Del Grosso, E.
Molecular weight of native and dissociated cysteamine oxygenase
Eur. J. Biochem.
16
537-540
1970
Equus caballus
brenda
Cavallini, D.; Canella, C.; Barboni, E.; Fiori, A.; Marcucci, M.
Interaction of cysteamine oxygenase with o-phenanthroline
Eur. J. Biochem.
11
360-363
1969
Equus caballus
brenda
Cavallini, D.; Dupre, S.; Scandurra, R.; Graziani, M.T.; Cotta-Ramusino, F.
Metal content of cysteamine oxygenase
Eur. J. Biochem.
4
209-212
1968
Equus caballus
brenda
Wood, J.L.; Cavallini, D.
Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor
Arch. Biochem. Biophys.
119
368-372
1967
Equus caballus
brenda
Cavallini, D.; De Marco, C.; Scandurra, R.; Dupre, S.; Graziani, M.T.
The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme
J. Biol. Chem.
241
3189-3196
1966
Equus caballus
brenda
Kataoka, H.; Ohishi, K.; Imai, J.; Mukai, M.
Distribution of cysteamine oxygenase in animal tissues
Agric. Biol. Chem.
52
1611-1613
1988
Bos taurus, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Sepiidae, Equus caballus, Scombridae, Mus musculus, octopus, Rattus norvegicus, Sus scrofa
-
brenda
Coloso Relicardo , C.R.; Hirschberger Lawrence , H.L.; Dominy John , D.J.; Lee Jeong-I, L.J.; Stipanuk Martha , S.M.
Cysteamine dioxygenase: evidence for the physiological conversion of cysteamine to hypotaurine in rat and mouse tissues
Adv. Exp. Med. Biol.
583
25-36
2006
Mus musculus, Rattus norvegicus
brenda
Dominy, J.E.; Simmons, C.R.; Hirschberger, L.L.; Hwang, J.; Coloso, R.M.; Stipanuk, M.H.
Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase
J. Biol. Chem.
282
25189-25198
2007
Mus musculus (Q6PDY2), Mus musculus
brenda
Stipanuk, M.H.; Simmons, C.R.; Andrew Karplus, P.; Dominy, J.E.
Thiol dioxygenases: unique families of cupin proteins
Amino Acids
41
91-102
2011
Mus musculus (Q6PDY2), Homo sapiens (Q96SZ5)
brenda
Liu, C.L.; Watson, A.M.; Place, A.R.; Jagus, R.
Taurine biosynthesis in a fish liver cell line (ZFL) adapted to a serum-free medium
Mar. Drugs
15
147-161
2017
Danio rerio, Danio rerio ATCC CRL-2643
brenda
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