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Information on EC 1.13.11.54 - acireductone dioxygenase [iron(II)-requiring] and Organism(s) Homo sapiens

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IUBMB Comments
Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-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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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mtcbp-1, osard1, fe-ard, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aci-reductone dioxygenase
-
-
Fe(II)-bound acireductone dioxygenase
-
MTCBP-1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
ARD (Fe), converts the substrate to formate and a keto-acid precursor of methionine that is then converted to methionine (on-pathway)
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate-forming)
Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-requiring), occurs instead. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
221681-63-6
-
221681-64-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
2-oxovalerate + formic acid
show the reaction diagram
i.e. desthio-acireductone
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
show the reaction diagram
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
2-keto-4-methyl thiobutyrate + formate
show the reaction diagram
-
-
-
-
ir
1,2-dihydroxy-hex-1-en-3-one + O2
?
show the reaction diagram
-
-
-
?
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+
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTND_HUMAN
179
0
21498
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with selenomethionine, sitting drop vapor diffusion method, using 1:0.8 sodium acetate (0.1 M), ammonium sulfate (2.0 M pH 4.5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E94A
-
no activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Ni2+-bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Superdex 200 gel filtration
Strep-Tactin resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) codon Plus RIPL cells
expressed in Escherichia coli BL21(DE3)-CodonPlus-RIPL cells
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
matrix metalloproteinase MT1-MMP physically interacts with claudin-1 and acireductone dioxygenase 1, both associated with hepatitis C virus cell entry. Positive cytoplasmic ADI1 in liver biopsies is associated with higher serum hepatitis C virus RNA levels. Positive MT1-MMP and ADI1 interaction is associated with lower tissue hepatitis C virus RNA levels. Hepatic hepatitis C virus RNA levels are positively associated with ADI1 levels in the MT1-MMP and ADI1 coimmunoprecipitates
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, Saccharomyces cerevisiae, Saccharomyces cerevisiae Y700
Manually annotated by BRENDA team
Chang, M.L.; Huang, Y.H.; Cheng, J.C.; Yeh, C.T.
Interaction between hepatic membrane type 1 matrix metalloproteinase and acireductone dioxygenase 1 regulates hepatitis C virus infection
J. Viral Hepat.
23
256-266
2016
Homo sapiens (Q9BV57)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Liu, X.; Garber, A.; Ryan, J.; Deshpande, A.; Ringe, D.; Pochapsky, T.C.
A model for the solution structure of human Fe(II)-bound acireductone dioxygenase and interactions with the regulatory domain of matrix metalloproteinase I (MMP-I)
Biochemistry
59
4238-4249
2020
Homo sapiens (Q9BV57), Homo sapiens
Manually annotated by BRENDA team
Milaczewska, A.; Kot, E.; Amaya, J.; Makris, T.; Zaj?c, M.; Korecki, J.; Chumakov, A.; Trzewik, B.; Kedracka-Krok, S.; Minor, W.; Chruszcz, M.; Borowski, T.
On the structure and reaction mechanism of human acireductone dioxygenase
Chemistry
24
5225-5237
2018
Homo sapiens (Q9BV57)
Manually annotated by BRENDA team