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2-aminoethanethiol + O2
hypotaurine
3-mercaptopropionic acid + O2
3-sulfinopropionic acid
cysteamine + O2
hypotaurine
homocysteamine + O2
2-aminopropansulfinic acid
-
-
-
-
?
mercaptoethanol + O2
2-hydroxyethanesulfinic acid
-
-
-
-
?
N-acetylcysteamine + O2
N-acetylhypotaurine
-
-
-
-
?
pantetheine + O2
pantothenate + cysteamine
-
oxidized at less than 3% of the cysteamine-dependent rate
-
-
?
additional information
?
-
2-aminoethanethiol + O2
hypotaurine
-
-
-
-
?
2-aminoethanethiol + O2
hypotaurine
-
-
-
-
?
2-aminoethanethiol + O2
hypotaurine
-
-
-
?
3-mercaptopropionic acid + O2
3-sulfinopropionic acid
-
-
-
-
?
3-mercaptopropionic acid + O2
3-sulfinopropionic acid
-
-
-
?
cysteamine + O2
hypotaurine
-
-
-
-
?
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
-
-
-
-
?
cysteamine + O2
hypotaurine
-
-
-
-
ir
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
-
-
-
ir
cysteamine + O2
hypotaurine
-
-
-
-
?
cysteamine + O2
hypotaurine
-
-
-
?
cysteamine + O2
hypotaurine
-
-
-
ir
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
cysteamine + O2
hypotaurine
-
-
-
-
ir
cysteamine + O2
hypotaurine
-
one of the main routes for taurine biosynthesis
-
?
additional information
?
-
no activity with cysteine
-
-
?
additional information
?
-
-
no activity with cysteine
-
-
?
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
-
-
overview: specificity
-
-
?
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
-
-
?
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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2-mercaptoethanol
-
inhibition at high concentration, activation at low concentration
8-hydroxyquinoline
-
complete inhibition at 7.5 mM
alpha,alpha'-dipyridyl
-
slight inhibition
azide
Fe(III)ADO incubated with azide displays a rhombic, high-spin (S = 5/2) EPR signal that closely resembles that of purified ADO. Azide may bind to the Fe(III)ADO active site by replacing a ligand with comparable donor strength, likely a solvent-derived hydroxide. Azide is unable to coordinate to cysteamine-bound Fe(III)ADO
cyanide
cyanide binds to either cysteamine- or Cys-bound Fe(III)ADO, binding causes the appearance of a dominant low-spin (S = 1/2) EPR signal and a small but noticeable change to the electronic absorption spectrum
diethyldithiocarbamate
-
70% inhibition at 10 mM
KCN
-
60-70% inhibition at 10 mM
mercaptoethylguanidine
-
noncompetitive to cysteamine
Neocuproine
-
45-55% inhibition at 10 mM
o-phenanthroline
-
45-55% inhibition at 10 mM
S
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
Salicylaldoxime
-
slight inhibition
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)
cysteine
-
-
cysteine
weak competitive inhibitor, Cys can bind directly to the ADO iron center with formation of a low-spin (S=1/2) FeIII complex. The ratio of low-spin to high-spin ferric species can be modulated by the addition of glycerol, with the high-spin Cys-FeIII-ADO complex being the predominant form in the absence of a glassing agent
Iron
substrate cysteamine is capable of reducing the catalytically inactive ferric center to the enzymatically active ferrous state. Presence of cysteamine alters the binding behavior of nitric oxide to the nonheme iron center of ADO
Iron
substrate cysteamine is capable of reducing the catalytically inactive ferric center to the enzymatically active ferrous state. Presence of cysteamine alters the binding behavior of nitric oxide to the nonheme iron center of ADO
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physiological function
ADO catalyzes conversion of N-terminal cysteine to cysteine sulfinic acid, reaction of EC 1.13.11.20, and is related to the plant cysteine oxidases that mediate responses to hypoxia by an identical post-translational modification. In human cells ADO regulates the RGS4/5 (regulator of G-protein signalling) N-degron substrates, modulates G-protein coupled Ca2+ signals and MAPK activity, and acts on N-terminal cysteine proteins including the angiogenic cytokine IL-32. Inactivation of ADO leads to constitutive upregulation of endogenous and transfected RGS4 and RGS5 proteins irrespective of oxygen levels
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
-
design of biomimetic model complexes where the 3-His coordination of the iron ion is simulated by three pyrazole donors of a trispyrazolyl borate ligand and protected cysteamine represent substrate ligands. Replacement of phenyl groups attached at the 3-positions of the pyrazole units in a previous model by mesityl residues has massive consequences, as the latter arrange to a more spacious reaction pocket. The reaction with O2 proceeds much faster and the structural characterization of an iron(II) eta2-O,O-sulfinate product became possible
metabolism
in the presence of nitric oxide as a spin probe and oxygen surrogate, both cysteamine and the peptide substrate regulator of G protein signaling 5 coordinate the iron center with their free thiols in a monodentate binding mode. A substrate-bound B-type dinitrosyl iron center complex is observed, as well as a substrate-mediated reduction of the iron center from ferric to the ferrous oxidation state with possible disulfide formation of the substrates
metabolism
in the presence of nitric oxide as a spin probe and oxygen surrogate, both cysteamine and the peptide substrate regulator of G protein signaling 5 coordinate the iron center with their free thiols in a monodentate binding mode. A substrate-bound B-type dinitrosyl iron center complex is observed, as well as a substrate-mediated reduction of the iron center from ferric to the ferrous oxidation state with possible disulfide formation of the substrates
metabolism
presence of a Cys-Tyr cofactor, crosslinked between Cys220 and Tyr222 through a thioether (C-S) bond. An autocatalytic oxidative carbon-fluorine bond activation and fluoride release is observed. The crosslinking results in a minimal structural change of the protein. A sequence motif C-X-Y-Y(F) is proposed for identifying Cys-Tyr crosslink
metabolism
substrates 2-aminoethanol and 3-mercaptopropionic acid bind to ADO in the same manner, potentially in a monodentate fashion through the terminal thiolate. The high-spin ferric species exhibit a more axial zero-field splitting relative to that reported for Cys-bound FeIIICDO
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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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
Wang, Y.; Griffith, W.P.; Li, J.; Koto, T.; Wherritt, D.J.; Fritz, E.; Liu, A.
Cofactor biogenesis in cysteamine dioxygenase C-F bond cleavage with genetically incorporated unnatural tyrosine
Angew. Chem. Int. Ed. Engl.
57
8149-8153
2018
Homo sapiens (Q96SZ5), Homo sapiens
brenda
Gonzales-Plasus, M.; Kondo, H.; Hirono, I.; Satoh, S.; Haga, Y.
Cysteamine dioxygenase as enzymes for taurine synthesis and the negative effect of high dietary cysteamine on growth and body shape of the common carp, Cyprinus carpio
Aquacult. Sci.
67
95-108
2020
Cyprinus carpio
-
brenda
Fernandez, R.L.; Elmendorf, L.D.; Smith, R.W.; Bingman, C.A.; Fox, B.G.; Brunold, T.C.
The crystal structure of cysteamine dioxygenase reveals the origin of the large substrate scope of this vital mammalian enzyme
Biochemistry
60
3728-3737
2021
Mus musculus (Q6PDY2)
brenda
Mueller, L.; Hoof, S.; Keck, M.; Herwig, C.; Limberg, C.
Enhancing tris(pyrazolyl)borate-based models of cysteine/cysteamine dioxygenases through steric effects increased reactivities, full product characterization and hints to initial superoxide formation
Chemistry
26
11851-11861
2020
synthetic construct
brenda
Wang, Y.; Davis, I.; Chan, Y.; Naik, S.G.; Griffith, W.P.; Liu, A.
Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates
J. Biol. Chem.
295
11789-11802
2020
Mus musculus (Q6PDY2), Mus musculus, Homo sapiens (Q96SZ5), Homo sapiens
brenda
Wang, Y.; Shin, I.; Li, J.; Liu, A.
Crystal structure of human cysteamine dioxygenase provides a structural rationale for its function as an oxygen sensor
J. Biol. Chem.
297
34508780
2021
Homo sapiens (Q96SZ5), Homo sapiens
brenda
Fernandez, R.L.; Juntunen, N.D.; Fox, B.G.; Brunold, T.C.
Spectroscopic investigation of iron(III) cysteamine dioxygenase in the presence of substrate (analogs) implications for the nature of substrate-bound reaction intermediates
J. Biol. Inorg. Chem.
26
947-955
2021
Mus musculus (Q6PDY2)
brenda
Puerta, M.; Perata, P.; Hopkinson, R.; Flashman, E.; Licausi, F.; Ratcliffe, P.
Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants
Science
364
65-69
2019
Homo sapiens (Q96SZ5)
brenda