Any feedback?
Information on EC 1.13.11.54 - acireductone dioxygenase [iron(II)-requiring]
for references in articles please use BRENDA:EC1.13.11.54Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.13.11.54 acireductone dioxygenase [iron(II)-requiring]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.
Specify your search results
Word Map
- 1.13.11.54
- metalloproteinase
- ethylene
- s-adenosylmethionine
- mt1-mmp
- mta
-
salvage
- polyamine
- adomet
-
cupin
-
metal-binding
-
aci-reductone
-
submergence
-
deepwater
-
adenosyltransferase
- methylthioribose
-
phytosiderophore
-
membrane-type
- mmp-2
-
submergence-induced
-
mt1-mmp-mediated
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
mtcbp-1, osard1, fe-ard, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aci-reductone dioxygenase
acireductone dioxygenase 1
ARD'
ARD1
ARD4
Ymr009p
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
oxidation
-
ARD (Fe), converts the substrate to formate and a keto-acid precursor of methionine that is then converted to methionine (on-pathway)
oxidation
-
ARD (Fe), converts the substrate to formate and a keto-acid precursor of methionine that is then converted to methionine (on-pathway)
oxidation
if Fe+2 is bound in the active site, the substrate acireductone reacts with O2 to yield formate and 3-(methylthio)propanoate
oxidation
-
ARD (Fe), converts the substrate to formate and a keto-acid precursor of methionine that is then converted to methionine (on-pathway)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
221681-63-6
-
221681-64-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
1,2-dihydroxyhex-1-en-3-one + O2
2-oxopentanoate + formate
-
incorporation of O2 into C1 and C2 of 1,2-dihydroxy-3-keto-1-hexene
-
-
?
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
2-oxovalerate + formic acid
i.e. desthio-acireductone
-
-
?
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
2-oxovalerate + formic acid
i.e. desthio-acireductone
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
A0A2V2XFM8; A0A2V2VIR7
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
2-keto-4-methyl thiobutyrate + formate
-
-
-
-
ir
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
2-keto-4-methyl thiobutyrate + formate
-
-
-
-
ir
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
2-keto-4-methyl thiobutyrate + formate
-
-
-
-
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
4-(methylthio)-2-oxobutanoate + formate
-
-
-
?
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-oxobutanoate + formate
-
-
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
enzyme of the methionine salvage pathway
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
Fe2+ bound to the enzyme protein. If Ni2+ or Co2+ is bound instead of Fe+, the reaction catalzed by EC 1.13.11.53 occurs instead
-
-
?
1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2
4-(methylthio)-2-oxobutanoate + formate
-
ordered-sequential mechanism
-
-
?
additional information
?
-
acireductone dioxygenase 1 primarily performs the on-pathway reaction with bound Fe2+ as metal cofactor. Acireductone dioxygenase 1 physically interacts with its regulator Arabidopsis thaliana G protein beta, identification of a potential Arabidopsis thaliana G protein beta-acireductone dioxygenase 1 interface, overview
-
-
?
additional information
?
-
acireductone dioxygenase 1 primarily performs the on-pathway reaction with bound Fe2+ as metal cofactor. Acireductone dioxygenase 1 physically interacts with its regulator Arabidopsis thaliana G protein beta, identification of a potential Arabidopsis thaliana G protein beta-acireductone dioxygenase 1 interface, overview
-
-
?
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
?
-
-
OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
-
-
?
additional information
?
-
A0A2V2XFM8; A0A2V2VIR7
the enzyme has two different catalytic domains, its N-terminal half related to acireductone dioxygenase and its C-terminal half related to thioredoxin-related protein of 14 kDa. Enolase from Trypanosoma cruzi is inhibited by its interaction with metallocarboxypeptidase-1 and the enzyme
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
-
-
-
-
?
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2
4-(methylsulfanyl)-2-oxobutanoate + formate
A0A2V2XFM8; A0A2V2VIR7
-
-
-
?
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-oxobutanoate + formate
-
-
-
?
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-oxobutanoate + formate
enzyme of the methionine salvage pathway
-
-
?
additional information
?
-
acireductone dioxygenase 1 primarily performs the on-pathway reaction with bound Fe2+ as metal cofactor. Acireductone dioxygenase 1 physically interacts with its regulator Arabidopsis thaliana G protein beta, identification of a potential Arabidopsis thaliana G protein beta-acireductone dioxygenase 1 interface, overview
-
-
?
additional information
?
-
acireductone dioxygenase 1 primarily performs the on-pathway reaction with bound Fe2+ as metal cofactor. Acireductone dioxygenase 1 physically interacts with its regulator Arabidopsis thaliana G protein beta, identification of a potential Arabidopsis thaliana G protein beta-acireductone dioxygenase 1 interface, overview
-
-
?
additional information
?
-
-
OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Iron
ligands are H96, H98, E102 and H140, the same as in the isoform requiring Ni2+, 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
additional information
the identity of bound metal ion does not affect the oligomeric state of ARD
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
Fe2+
dependent on, acireductone dioxygenase 1 is an active metalloenzyme, Fe2+ is active site bound
Fe2+
apoenzyme is catalytically inactive. Addition of Fe2+ yields activity. Production of the enzyme in intact Escherichia coli depends on the availability of the Fe2+. Enzyme contains 0.9 Fe2+ per enzyme molecule
Fe2+
-
dependent on. Fe2+ transmits electrons from the residues, coordinating it to bound dioxygen and populating its formerly p*-orbital. This leads to dioxygen splitting in the second intermediate and eventual access to the Fe2+-dependent acireductone dioxygenase reaction route
Fe2+
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Arabidopsis thaliana G protein beta
possible mechanism for Arabidopsis thaliana G protein beta activation of acireductone dioxygenase 1 activity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Neoplasms
Evidence of MTCBP-1 interaction with the cytoplasmic domain of MT1-MMP: Implications in the autophagy cell index of high-grade glioblastoma.
Glioblastoma
Evidence of MTCBP-1 interaction with the cytoplasmic domain of MT1-MMP: Implications in the autophagy cell index of high-grade glioblastoma.
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.
Neoplasm Metastasis
Alterations of metastasis-related genes identified using an oligonucleotide microarray of genistein-treated HCC1395 breast cancer cells.
Neoplasm Metastasis
Pancreatic tumor cell metastasis is restricted by MT1-MMP binding protein MTCBP-1.
Neoplasms
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.
Neoplasms
Pancreatic tumor cell metastasis is restricted by MT1-MMP binding protein MTCBP-1.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
strongly induced in adventitious roots and in the youngest internode of partially submerged plants
brenda
-
strongly induced in adventitious roots and in the youngest internode of partially submerged plants
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme plays an important role in ethylene synthesis pathway
physiological function
additional information
physiological function
-
either facilitates recycling of methionine in living cells or exits this recycling pathway. Fe2+-dependent acireductone dioxygenase produces the 2-oxo acid precursor of methionine and formate
physiological function
one function of acireductone dioxygenases is to operate in the methionine salvage pathway. Acireductone dioxygenase 1 physically interacts with Arabidopsis thaliana G protein beta, and acireductone dioxygenase enzymatic activity is stimulated by Arabidopsis thaliana G protein beta in vitro. Overexpression of acireductone dioxygenase 1 suppresses the 2-day-old etiolated phenotype of agb1-2. Acireductone dioxygenase 1 and Arabidopsis thaliana G protein beta both control embryonic hypocotyl length by modulating cell division. They also may contribute to the production of ethylene, a product of the methionine salvage pathway. Arabidopsis thaliana G protein beta regulates acireductone dioxygenase 1 activity to control cell division, possible mechanism for Arabidopsis thaliana G protein beta activation of acireductone dioxygenase 1 activity, overview
physiological function
matrix metalloproteinase MT1-MMP physically interacts with claudin-1 and acireductone dioxygenase 1, both associated with hepatitis C virus cell entry
physiological function
-
enzyme overexpression improves submergence, drought, and salt tolerances of seedling through the enhancement of ethylene synthesis in rice
physiological function
isoform ARD4 regulates the ethylene and carotenoid signaling pathway, increases ethylene and carotenoid concentrations, and accelerates fruit ripening. Furthermore, ARD4 increases the antioxidative ability and cold hardiness in tomato
physiological function
the enzyme regulates the activity of matrix metalloproteinase I, which is involved in tumor metastasis, by binding the cytoplasmic transmembrane tail peptide of matrix metalloproteinase I
physiological function
-
transgenic rice plants overexpressing isoform ARD4 exhibit root growth characteristics including faster radical emergence, more rapid elongation of primary roots, early initiation of crown/lateral roots, and higher root biomass than the non-transgenic plants
physiological function
-
one function of acireductone dioxygenases is to operate in the methionine salvage pathway. Acireductone dioxygenase 1 physically interacts with Arabidopsis thaliana G protein beta, and acireductone dioxygenase enzymatic activity is stimulated by Arabidopsis thaliana G protein beta in vitro. Overexpression of acireductone dioxygenase 1 suppresses the 2-day-old etiolated phenotype of agb1-2. Acireductone dioxygenase 1 and Arabidopsis thaliana G protein beta both control embryonic hypocotyl length by modulating cell division. They also may contribute to the production of ethylene, a product of the methionine salvage pathway. Arabidopsis thaliana G protein beta regulates acireductone dioxygenase 1 activity to control cell division, possible mechanism for Arabidopsis thaliana G protein beta activation of acireductone dioxygenase 1 activity, overview
-
additional information
-
Fe2+-dependent acireductone dioxygenase passes through an additional split dioxygen intermediate and then proceeds through an epoxy-like transition state with a small activation energy to the two products, crystal structure analysis, structure modeling and molecular simulations of the Fe2+ and Ni2+ enzyme, cf. 1.13.11.53, QM-DMD domain, overview. The ability of Fe2+-dependent acireductone dioxygenase to stabilize an additional intermediate and thus produce the two products is due to the RedOx flexibility of the Fe2+ as compared to the more electron-rich Ni2+
additional information
identification of potential effectors in the Arabidopsis thaliana G protein beta signaling pathway by an activation tagging approach to randomly create dominant suppressors of agb1-2, overview. Homology modeling of acireductone dioxygenase 1, overview
additional information
-
identification of potential effectors in the Arabidopsis thaliana G protein beta signaling pathway by an activation tagging approach to randomly create dominant suppressors of agb1-2, overview. Homology modeling of acireductone dioxygenase 1, overview
-
Show AA Sequence and Transmembrane Helices (8138 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus anthracis str. 'Ames Ancestor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20240
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
A0A2V2XFM8; A0A2V2VIR7
1 * 37600, calculated from amino acid sequence
additional information
homology modeling of acireductone dioxygenase 1, overview
additional information
-
homology modeling of acireductone dioxygenase 1, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
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. with low spin Co2+, the reaction exclusively follows the Fe2+-dependent pathways, producing alpha-keto acid precursor of methionine and formate, while the high spin Co2+ path contains a bifurcation in the pathway that follows along both the Fe2+-dependent pathway and Ni2+-dependent pathway that produces methylthiopropionate, carbon monoxide and formate
Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E100A
about 2% of wild-type activity. E100 is not essential for metal binding
H98S
no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals
E100A
-
about 2% of wild-type activity. E100 is not essential for metal binding
-
H98S
E91A
additional information
H98S
-
no catalytic activity. Mutant exhibits little affinity for either Ni2+ or Fe2+, indicating that His 98 is likely involved in binding both metals
-
H98S
mutation results in the formation of a stable soluble protein that while structurally different from ARD shows a high degree of similarity to the ARD' enzyme
additional information
usage of three tDNA insertion mutant alleles, ard1-1 (SALK_119327), ard1-2 (GABI_595C04), and ard1-3 (SALK_034308).
additional information
-
usage of three tDNA insertion mutant alleles, ard1-1 (SALK_119327), ard1-2 (GABI_595C04), and ard1-3 (SALK_034308).
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Ni2+-bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant
recombinant His-tagged acireductone dioxygenase 1 and GST-tagged acireductone dioxygenase 1 by nickel affinity and glutathione affinity chromatographies, respectively
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Oryza sativa subsp. indica rice variety ASD16 through
-
expressed