Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
n-butanoic acid + formic acid + CO
1,2-dihydroxy-3-keto-1-hexene + O2
?
-
incorporation of O2 into C1 and C3 of 1,2-dihydroxy-3-keto-1-hexene
-
-
?
1,2-dihydroxy-3-oxo-3-phenyl-1-propene + O2
?
-
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
?
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
4-(methylthio)-2-oxobutanoate + formate
-
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-methylthio-2-ketobutyrate + formate
-
-
-
-
?
1,2-dihydroxyhex-1-en-3-one + O2
butyrate + formate + CO
-
-
-
-
?
1-phosphonooxy-2,2-dihydroxy-3-oxo-3-phenylpropane + O2
?
part of the Met salvage pathway
-
-
?
2-hydroxy-3-oxo-1,3-diphenylprop-1-en-1-olate + O2
?
-
-
-
-
?
additional information
?
-
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
n-butanoic acid + formic acid + CO
i.e. desthio-acireductone
-
-
?
(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-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
-
?
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
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
-
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
enzyme of the methionine salvage pathway
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
reaction is a shunt out of the methionine salvage pathway
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
the enzyme represents a branch point in the methionine salvage pathway leading from methylthioadenosine to methionine
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
Ni2+ or Co2+ bound to the enzyme protein. If Fe2+ is bound instead of Ni2+ reaction catalyzed by EC 1.13.11.54 occurs instead
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
ordered-sequential mechanism
-
-
?
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
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
-
-
?
additional information
?
-
-
support Hepatitis C virus infection by enhance of cell uptake and replication of Hepatitis C virus
-
-
?
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+
-
-
?
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+
-
-
?
additional information
?
-
-
aliphatic carbon-carbon bond cleavage reactivity of a mononuclear Ni(II) cis-beta-keto-enolate complex in the presence of base and O2: a model reaction for acireductone dioxygenase
-
-
?
additional information
?
-
-
paramagnetic nickel(II) complexes of macrocyclic N4 ligands are able to perform as enzyme-substrate mimic for the nickel containing acireductone dioxygenase enzyme
-
-
-
additional information
?
-
Schiff-base nickel biomimetic model complexes exhibit carbon-carbon bond cleavage activation of lithium acetylacetonate
-
-
-
additional information
?
-
the nickel complex [NiII(OPhN4(6-H-DPEN)(H2O))] is a structural analogue for the resting state of the active site of the nickel oxygenase nickel acireductone dioxyegenase and capable of carbon-carbon bond cleavage of a ketone presumably via dioxygenase type chemistry in line with the reactivity of the enzyme
-
-
-
additional information
?
-
-
it is proposed that Rnt1p cleavage and/or degradation by exonucleases helps prevent the accumulation of ADI1 mRNA prior to heat shock conditions. The ribonucleolytic pathways provide a mechanism to eliminate 3'-extended forms that arise from poor 3'-end processing signals present at the end of the ADI1 gene
-
-
?
additional information
?
-
-
a mononuclear NiII complex bearing the monoanion of 1-acetoxy-3-phenylpropane-2,3-dione as a ligand, i.e. (N,N-bis[(6-phenyl-2-pyridyl)methyl]-N-(2-pyridylmethyl)amine)Ni[PhC(O)C(O)CHOC(O)CH3]ClO4 after deprotection by the addition of NaOCH3 in methanol generates a NiII species that contains a coordinated dianionic C(1)-H acireductone. Exposure of this acireductone to O2 leads to regioselective oxidative cleavage reactivity akin to that found for the NiII-containing acireductone dioxygenase enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
?
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
4-(methylthio)-2-oxobutanoate + formate
-
-
-
-
?
additional information
?
-
-
it is proposed that Rnt1p cleavage and/or degradation by exonucleases helps prevent the accumulation of ADI1 mRNA prior to heat shock conditions. The ribonucleolytic pathways provide a mechanism to eliminate 3'-extended forms that arise from poor 3'-end processing signals present at the end of the ADI1 gene
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
3-(methylsulfanyl)propanoate + formate + CO
-
-
-
-
?
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
-
enzyme of the methionine salvage pathway
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
reaction is a shunt out of the methionine salvage pathway
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
3-(methylthio)propanoate + formate + CO
-
the enzyme represents a branch point in the methionine salvage pathway leading from methylthioadenosine to methionine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fe2+
-
the Fe2+ bound protein catalyzes the reaction of EC 1.13.11.54
Iron
the enzyme contains a non-heme, iron-binding site critical for its activity
Zn2+
Zn2+-form of enzyme, less than 1 mol per mol of protein
additional information
-
the identity of bound metal ion does not affect the oligomeric state of ARD
Co2+
Co2+-form of enzyme, about 1 mol per mol of protein
Co2+
quantum-classical dynamics simulations with Co2+ bound. both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD, but the mechanism involves a bifurcating transition state, and so the exact product distribution is determined by the reaction dynamics
Co2+
-
apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule
Co2+
-
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Mn2+
Mn2+-form of enzyme, less than 1 mol per mol of protein
Mn2+
-
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Ni2+
-
-
Ni2+
Ni2+-form of enzyme, less than 1 mol per mol of protein
Ni2+
-
apoenzyme is catalytically inactive. Addition of Ni2+ or Co2+ yields activity. Production in intact Escherichia coli of E-2' depends on the availability of the Fe2+. Enzyme contains 1.1 Ni2+ per enzyme molecule
Ni2+
-
enzyme contains 1 atom of Ni
Ni2+
-
enzyme contains Ni2+
Ni2+
-
Ni2+-containg enzyme
Ni2+
-
solution structure of the nickel-containing enzyme is determined using NMR methods. X-ray absorption spectroscopy, assignment of hyperfine shifted NMR resonance and conserved domain homology are used to model the metal-binding site because of the paramagnetism of the bound Ni2+
Ni2+
-
structure of the Ni site in resting Ni-ARD as containing a six coordinate Ni site composed of O/N-donor ligands including 3-4 histidine residues. The substrate binds to the Ni center in a bidentate fashion by displacing two ligands, at least one of which is a histidine ligand
Ni2+
-
required for activity
Ni2+
-
model for the solution structure of the paramagnetic Ni2+-containing enzyme
Ni2+
-
Ni2+ can be conservatively replaced by Mn2 +or Co2+, giving rise to ARD activity (CO production)
Ni2+
-
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Nickel
detection of one-bond 15N-13Calpha correlations in the vicinity of the paramagnetic Ni2+
Nickel
-
ligands are H96, H98, E102 and H140, the same as in the isoform requiring Fe2+, EC 1.13.11.54. Structural and functional differences between FeARD' and NiARD' forms are triggered by subtle differences in the local backbone. Both enzymes bind their respective metals with pseudo-octahedral geometry and both may lose a His ligand upon binding of substrate under anaerobic conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Carcinogenesis
Human acireductone dioxygenase (HsARD), cancer and human health: Black hat, white hat or gray?
Carcinoma
Human acireductone dioxygenase (HsARD), cancer and human health: Black hat, white hat or gray?
Carcinoma, Hepatocellular
Hepatitis C virus infection in mouse hepatoma cells co-expressing human CD81 and Sip-L.
Carcinoma, Hepatocellular
The methionine salvage pathway-involving ADI1 inhibits hepatoma growth by epigenetically altering genes expression via elevating S-adenosylmethionine.
Hepatitis C
dBMHCC: A comprehensive hepatocellular carcinoma (HCC) biomarker database provides a reliable prediction system for novel HCC phosphorylated biomarkers.
Hepatitis C
Emergence of mutation clusters in the HCV genome during sequential viral passages in Sip-L expressing cells.
Hepatitis C
Hepatitis C virus infection in mouse hepatoma cells co-expressing human CD81 and Sip-L.
Hepatitis C
Interaction between hepatic membrane type 1 matrix metalloproteinase and acireductone dioxygenase 1 regulates hepatitis C virus infection.
Hepatitis C
Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors.
Infections
Hepatitis C virus infection in mouse hepatoma cells co-expressing human CD81 and Sip-L.
Neoplasms
Human acireductone dioxygenase (HsARD), cancer and human health: Black hat, white hat or gray?
Neoplasms
The methionine salvage pathway-involving ADI1 inhibits hepatoma growth by epigenetically altering genes expression via elevating S-adenosylmethionine.
Prostatic Neoplasms
Expression and function of the human androgen-responsive gene ADI1 in prostate cancer.
Prostatic Neoplasms
The methionine salvage pathway-involving ADI1 inhibits hepatoma growth by epigenetically altering genes expression via elevating S-adenosylmethionine.
Virus Diseases
dBMHCC: A comprehensive hepatocellular carcinoma (HCC) biomarker database provides a reliable prediction system for novel HCC phosphorylated biomarkers.
Virus Diseases
Hepatitis C virus infection in mouse hepatoma cells co-expressing human CD81 and Sip-L.
Virus Diseases
Interaction between hepatic membrane type 1 matrix metalloproteinase and acireductone dioxygenase 1 regulates hepatitis C virus infection.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Dai, Y.; Pochapsky, T.C.; Abeles, R.H.
Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae
Biochemistry
40
6379-6387
2001
Klebsiella pneumoniae
brenda
Al-Mjeni, F.; Ju, T.; Pochapsky, T.C.; Maroney, M.J.
XAS investigation of the structure and function of Ni in acireductone dioxygenase
Biochemistry
41
6761-6769
2002
Klebsiella pneumoniae
brenda
Szajna, E.; Arif, A.M.; Berreau, L.M.
Aliphatic carbon-carbon bond cleavage reactivity of a mononuclear Ni(II) cis-beta-keto-enolate complex in the presence of base and O2: a model reaction for acireductone dioxygenase (ARD)
J. Am. Chem. Soc.
127
17186-17187
2005
Klebsiella pneumoniae
brenda
Furfine, E.S.; Abeles, R.H.
Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumonia
J. Bacteriol.
263
9598-9606
1988
Klebsiella pneumoniae
brenda
Wray, J.W.; Abeles, R.H.
A bacterial enzyme that catalyzes formation of carbon monoxide
J. Biol. Chem.
268
21466-21469
1993
Klebsiella pneumoniae
brenda
Wray, J.W.; Abeles, R.B.
The methionine salvage pathway in Klebsiella pneumoniae and rat liver
J. Biol. Chem.
270
3147-3153
1995
Klebsiella pneumoniae
brenda
Dai, Y.; Wensink, P.C.; Abeles, R.H.
One protein, two enzymes
J. Biol. Chem.
274
1193-1195
1999
Klebsiella pneumoniae
brenda
Zer, C.; Chanfreau, G.
Regulation and surveillance of normal and 3'-extended forms of the yeast acireductone dioxygenase mRNA by RNase III cleavage and exonucleolytic degradation
J. Biol. Chem.
280
28997-29003
2005
Saccharomyces cerevisiae
brenda
Mo, H.; Dai, Y.; Pochapsky, S.S.; Pochapsky, T.C.
1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae
J. Biomol. NMR
14
287-288
1999
Klebsiella pneumoniae
brenda
Pochapsky, T.C.; Pochapsky, S.S.; Ju, T.; Hoefler, C.; Liang, J.
A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings
J. Biomol. NMR
34
117-127
2006
Klebsiella sp.
brenda
Pochapsky, T.C.; Pochapsky, S.S.; Ju, T.; Mo, H.; Al-Mjeni, F.; Maroney, M.J.
Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae
Nat. Struct. Biol.
9
966-972
2002
Klebsiella pneumoniae
brenda
Sauter, M.; Lorbiecke, R.; Ouyang, B.; Pochapsky, T.C.; Rzewuski, G.
The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine
Plant J.
44
718-729
2005
Oryza sativa (A2Z7C4), Oryza sativa
brenda
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
brenda
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
brenda
Szajna-Fuller, E.; Chambers, B.M.; Arif, A.M.; Berreau, L.M.
Carboxylate coordination chemistry of a mononuclear Ni(II) center in a hydrophobic or hydrogen bond donor secondary environment: Relevance to acireductone dioxygenase
Inorg. Chem.
46
5486-5498
2007
Klebsiella sp.
brenda
Szajna-Fuller, E.; Rudzka, K.; Arif, A.M.; Berreau, L.M.
Acireductone dioxygenase-(ARD-) type reactivity of a nickel(II) complex having monoanionic coordination of a model substrate: Product identification and comparisons to unreactive analogues
Inorg. Chem.
46
5499-5507
2007
Klebsiella sp.
brenda
Ju, T.; Goldsmith, R.B.; Chai, S.C.; Maroney, M.J.; Pochapsky, S.S.; Pochapsky, T.C.
One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase
J. Mol. Biol.
363
823-834
2006
Mus musculus
brenda
Xu Q.; Schwarzenbacher R.; Krishna SS.; McMullan D.; Agarwalla S.; Quijano K.; Abdubek P.; Ambing E.; Axelrod H.; Biorac T.; Canaves JM.; Chiu HJ.; Elsliger MA.; Grittini C.; Grzechnik SK.; DiDonato M.; Hale J.; Hampton E.; Han GW.; Haugen J.; Hornsby M.; Jaroszewski L.; Klock H.E.; Knuth MW.; Koesema E.; Kreusch A.; Kuhn P.; Miller M.D.; Moy K.; Nigoghossian E.; Paulsen J.; Reyes R.; Rife C.; Spraggon G.; Stevens RC.; van den Bedem H.; Velasquez J.; White A.; Wolf G.; Hodgson K.O.; Wooley J.; Deacon A.M.; Godzik A.; Lesley SA.; Wilson I.A.
Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 A resolution
Proteins
64
808-813
2006
Mus musculus (Q99JT9), Mus musculus
brenda
Chai, S.C.; Ju, T.; Dang, M.; Beaulieu Goldsmith, R.; Maroney, M.J.; Pochapsky, T.C.
Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724
Biochemistry
47
2428-2438
2008
Klebsiella sp.
brenda
Pochapsky, S.S.; Sunshine, J.C.; Pochapsky, T.C.
Completing the circuit: direct-observe 13C,15N double-quantum spectroscopy permits sequential resonance assignments near a paramagnetic center in acireductone dioxygenase
J. Am. Chem. Soc.
130
2156-2157
2008
Klebsiella oxytoca (Q9ZFE7)
brenda
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
brenda
Kim, J.H.; Kim, H.S.; Lee, Y.H.; Kim, Y.S.; Oh, H.W.; Joung, H.; Chae, S.K.; Suh, K.H.; Jeon, J.H.
Polyamine biosynthesis regulated by StARD expression plays an important role in potato wound periderm formation
Plant Cell Physiol.
49
1627-1632
2008
Solanum tuberosum (A8UGP3), Solanum tuberosum
brenda
Allpress, C.J.; Grubel, K.; Szajna-Fuller, E.; Arif, A.M.; Berreau, L.M.
Regioselective aliphatic carbon-carbon bond cleavage by a model system of relevance to iron-containing acireductone dioxygenase
J. Am. Chem. Soc.
135
659-668
2013
Klebsiella oxytoca
brenda
Deshpande, A.R.; Wagenpfeil, K.; Pochapsky, T.C.; Petsko, G.A.; Ringe, D.
Metal-dependent function of a mammalian acireductone dioxygenase
Biochemistry
55
1398-1407
2016
Mus musculus
brenda
Valdez, C.; Gallup, N.; Alexandrova, A.
Co2+ acireductone dioxygenase Fe2+ mechanism, Ni2+ mechanism, or something else?
Chem. Phys. Lett.
604
77-82
2014
Klebsiella oxytoca (Q9ZFE7)
-
brenda
Allpress, C.; Berreau, L.
A nickel-containing model system of acireductone dioxygenases that utilizes a C(1)-H acireductone substrate
Eur. J. Inorg. Chem.
2014
4642-4649
2014
synthetic construct
-
brenda
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
brenda
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
Mus musculus (Q99JT9), Mus musculus
brenda
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
brenda
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
brenda
Raje, S.; Mani, K.; Kandasamy, P.; Butcher, R.J.; Angamuthu, R.
Bioinspired oxidative cleavage of aliphatic C-C bonds utilizing aerial oxygen by nickel acireductone dioxygenase mimics
Eur. J. Inorg. Chem.
2019
2164-2167
2019
Klebsiella pneumoniae
-
brenda
Ivan, D.A.; Gremillion, A.J.; Sanchez, A.; Sanchez, S.; Lynch, V.M.; Toledo, S.A.
The first structural model for the resting state of the active site of nickel acireductone dioxygenase (Ni-ARD)
Inorg. Chem. Commun.
89
37-40
2018
Mus musculus (Q99JT9)
-
brenda
Blade, G.A.; Parveen, R.; Jaimes, J.L.; Ilustre, W.; Saldana, D.; Ivan, D.A.; Lynch, V.M.; Cundari, T.R.; Toledo, S.
A family of structural and functional models for the active site of a unique dioxygenase Acireductone dioxygenase (ARD)
J. Inorg. Biochem.
212
111253
2020
Mus musculus (Q99JT9)
brenda
Alfano, M.; Cavazza, C.
Structure, function, and biosynthesis of nickel-dependent enzymes
Protein Sci.
29
1071-1089
2020
Klebsiella oxytoca (Q9ZFE7)
brenda