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Information on EC 1.13.11.19 - cysteamine dioxygenase and Organism(s) Homo sapiens and UniProt Accession Q96SZ5
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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].
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The taxonomic range for the selected organisms is: Homo sapiens
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
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-
-
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oxygenase, cysteamine
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-
-
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oxygenase, cysteamine di-
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persulfurase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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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. 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
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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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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
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
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_HUMAN
270
0
29751
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
presence of a Cys-Tyr cofactor, crosslinked between Cys220 and Tyr222 through a thioether (C-S) bond
additional information
-
presence of a Cys-Tyr cofactor, crosslinked between Cys220 and Tyr222 through a thioether (C-S) bond
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of human ADO at a resolution of 1.78 A with a nickel-bound metal center. Crystallization is achieved through both metal substitution and C18S/C239S double mutations. The metal center resides in a tunnel close to an entry site flanked by loops. ADO appears to use extensive flexibility to handle substrates of different sizes, and also employs proline and proline pairs to maintain the core protein structure and to retain the residues critical for catalysis in place
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
ADO functions as an oxygen sensor by modifying N-degron substrates to transduce responses to hypoxia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
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
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Release 2023.1 (January 2023)
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