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Information on EC 1.13.11.53 - acireductone dioxygenase (Ni2+-requiring) and Organism(s) Homo sapiens and UniProt Accession Q9BV57
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1.13.11.53 acireductone dioxygenase (Ni2+-requiring)IUBMB Comments
Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction catalysed by EC 1.13.11.54, acireductone dioxygenase [iron(II)-requiring], occurs instead . The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
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Word Map
- 1.13.11.53
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salvage
- monoxide
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cupins
- mta
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on-pathway
- oxytoca
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nickel-containing
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ketoacid
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ni2+-containing
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membrane-type
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submergence-induced
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nickel-dependent
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nickelii
- nife-hydrogenase
- benzil
- 2-keto-4-methylthiobutyrate
- ch3cn
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metallocenters
- analysis
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
Reaction Schemes
Synonyms
acireductone dioxygenase, aci-reductone dioxygenase, ni-ard, acireductone dioxygenase 1, sip-l, human aci-reductone dioxygenase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1
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MTCBP-1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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ARD (Ni) converts aci-reductone to 3-(methylthio)propanoate, carbon monoxide, and formate, and the reaction is not part of the methionine salvage pathway cycle (off-pathway).
SYSTEMATIC NAME
IUBMB Comments
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming)
Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction catalysed by EC 1.13.11.54, acireductone dioxygenase [iron(II)-requiring], occurs instead [1]. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
CAS REGISTRY NUMBER
COMMENTARY
221681-64-7
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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
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
n-butanoic acid + formic acid + CO
i.e. desthio-acireductone
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
-
-
-
ir
additional information
?
-
human ARD is capable of metal-dependent dual chemistry. The Fe2+-bound ARD shows the highest activity and catalyzes on-pathway chemistry, i.e. reaction of EC 1.13.11.54, whereas Ni2+, Co2+ or Mn2+ forms catalyze off-pathway chemistry, i.e. reasctions of EC 1.13.11.53. The enzymatic activity is metal ion cofactor dependent and the activity trend in decreasing order is Fe2+ > Ni2+ = Co2+ > Mn2+
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-
?
additional information
?
-
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human ARD is capable of metal-dependent dual chemistry. The Fe2+-bound ARD shows the highest activity and catalyzes on-pathway chemistry, i.e. reaction of EC 1.13.11.54, whereas Ni2+, Co2+ or Mn2+ forms catalyze off-pathway chemistry, i.e. reasctions of EC 1.13.11.53. The enzymatic activity is metal ion cofactor dependent and the activity trend in decreasing order is Fe2+ > Ni2+ = Co2+ > Mn2+
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?
additional information
?
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support Hepatitis C virus infection by enhance of cell uptake and replication of Hepatitis C virus
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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
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
the enzyme contains a non-heme, iron-binding site critical for its activity
Ni2+
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
enzyme expression promotes 5'-methylthioadenosine cycle to increase S-adenosylmethionine levels, which alter genome-wide promoter methylation profiles, resulting in altered gene expression and hepatocellular carcinoma growth suppression
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). MTND_HUMAN
179
0
21498
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E94A
the mutant has an increased percentage of apoptotic cells similar to those expressing wild type enzyme
H133A
the mutation at the metal-binding site abolishes both functions of the enzyme in cell growth inhibition and apoptosis enhancement
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Ni2+-bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
additional information
-
Ni2+-bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significant decrease in enzyme mRNA levels is observed after 14 h of iron depletion. Silencing of the intracellular iron chaperone poly r(C)-binding protein 1 leads to loss of enzyme expression
there is a significant reduction of enzyme, either in protein or mRNA level, in hepatocellular carcinoma tissues
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the enzyme level positively associates with postoperative recurrence-free survival in patients with hepatocellular carcinoma
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirano, W.; Gotoh, I.; Uekita, T.; Seiki, M.
Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway
Genes Cells
10
565-574
2005
Homo sapiens
Gotoh, I.; Uekita, T.; Seiki, M.
Regulated nucleo-cytoplasmic shuttling of human aci-reductone dioxygenase (hADI1) and its potential role in mRNA processing
Genes Cells
12
105-117
2007
Homo sapiens
Cheng, J.C.; Yeh, Y.J.; Pai, L.M.; Chang, M.L.; Yeh, C.T.
293 cells over-expressing human ADI1 and CD81 are permissive for serum-derived hepatitis C virus infection
J. Med. Virol.
81
1560-1568
2009
Homo sapiens
Deshpande, A.R.; Pochapsky, T.C.; Petsko, G.A.; Ringe, D.
Dual chemistry catalyzed by human acireductone dioxygenase
Protein Eng. Des. Sel.
30
197-204
2017
Homo sapiens (Q9BV57), Homo sapiens
Bae, D.H.; Lane, D.J.R.; Siafakas, A.R.; Sutak, R.; Paluncic, J.; Huang, M.L.H.; Jansson, P.J.; Rahmanto, Y.S.; Richardson, D.R.
Acireductone dioxygenase 1 (ADI1) is regulated by cellular iron by a mechanism involving the iron chaperone, PCBP1, with PCBP2 acting as a potential co-chaperone
Biochim. Biophys. Acta Mol. Basis Dis.
1866
165844
2020
Homo sapiens (Q9BV57), Homo sapiens
Chu, Y.D.; Lai, H.Y.; Pai, L.M.; Huang, Y.H.; Lin, Y.H.; Liang, K.H.; Yeh, C.T.
The methionine salvage pathway-involving ADI1 inhibits hepatoma growth by epigenetically altering genes expression via elevating S-adenosylmethionine
Cell Death Dis.
10
240
2019
Homo sapiens (Q9BV57), Homo sapiens
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