Any feedback?
Information on EC 1.13.11.19 - cysteamine dioxygenase and Organism(s) Mus musculus and UniProt Accession Q6PDY2
for references in articles please use BRENDA:EC1.13.11.19Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.13.11.19 cysteamine dioxygenaseIUBMB Comments
A non-heme iron protein that is involved in the biosynthesis of taurine. 3-Aminopropanethiol (homocysteamine) and 2-sulfanylethan-1-ol (2-mercaptoethanol) can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
Specify your search results
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cysteamine dioxygenase, 2-aminoethanethiol dioxygenase, cysteamine oxygenase, persulfurase, gm237, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cysteamine oxygenase
-
-
-
-
oxygenase, cysteamine
-
-
-
-
oxygenase, cysteamine di-
-
-
-
-
persulfurase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
2-aminoethanethiol:oxygen oxidoreductase
A non-heme iron protein that is involved in the biosynthesis of taurine. 3-Aminopropanethiol (homocysteamine) and 2-sulfanylethan-1-ol (2-mercaptoethanol) can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
CAS REGISTRY NUMBER
COMMENTARY
9033-41-4
-
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
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
?
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
formation of an inner-sphere complex between FeIII-ADO and 2-aminoethanol. Binding occurs via a 3-His triad
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
hypotaurine is not in brain of either Vanin-1 (+/+) or Vanin-1 (-/-) mice that had been fed a non-purified rodent diet.
-
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.
-
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.
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
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
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
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_MOUSE
256
0
28372
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of cysteamine dioxygenase at 1.9 A resolution, an Fe and three-histidine (3-His) active site is situated at the end of a wide substrate access channel. Whole-protein models of ADO in complex with either cysteamine or an N-terminal-Cys peptide suggest occlusion of access to the active site by peptide substrate binding. A small tunnel that leads from the opposite face of the enzyme into the active site provides a path through which co-substrate O2 can access the Fe center. The entrance to the tunnel is guarded by two Cys residues that may form a disulfide bond to regulate O2 delivery
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Equus caballus, Gallus gallus, Mus musculus, octopus, Oryctolagus cuniculus, Rattus norvegicus, Scombridae, Sepiidae, Sus scrofa
-
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
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
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
Homo sapiens (Q96SZ5), Mus musculus (Q6PDY2)
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)
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
Homo sapiens (Q96SZ5), Homo sapiens, Mus musculus (Q6PDY2), Mus musculus
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)
EXTERNAL LINKS (specific for EC-Number 1.13.11.19)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
