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Information on EC 1.14.14.10 - nitrilotriacetate monooxygenase
for references in articles please use BRENDA:EC1.14.14.10
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.10 nitrilotriacetate monooxygenase
IUBMB Comments
Requires Mg2+. The enzyme from Aminobacter aminovorans (previously Chelatobacter heintzii) is part of a two component system that also includes EC 1.5.1.42 (FMN reductase), which provides reduced flavin mononucleotide for this enzyme.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.14.14.10
- flavin
- mononucleotide
- iminodiacetate
-
radionuclides
-
nadh:fmn
-
nadh:flavine
-
homotetramer
-
two-enzyme
- dibenzothiophene
- fischeri
- ethylenediamine
-
recalcitrance
-
glucose-grown
-
photobacterium
-
thereof
- mesorhizobium
-
two-component
-
edda
- reductases
showSynonyms
nta-mo, edta monooxygenase, nta monooxygenase, nta-mob, nitrilotriacetate monooxygenase, nta-monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
component B of NTA monooxygenase
NTA monooxygenase
NTA-MO
NTA-monooxygenase
NtaA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nitrilotriacetate + FMNH2 + H+ + O2 = iminodiacetate + glyoxylate + FMN + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY SOURCE
PATHWAYS
MetaCyc
nitrilotriacetate degradation
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SYSTEMATIC NAME
IUBMB Comments
nitrilotriacetate,FMNH2:oxygen oxidoreductase (glyoxylate-forming)
Requires Mg2+. The enzyme from Aminobacter aminovorans (previously Chelatobacter heintzii) is part of a two component system that also includes EC 1.5.1.42 (FMN reductase), which provides reduced flavin mononucleotide for this enzyme.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
EDTA + O2 + FMNH2 + H+
ethylenediaminetriacetate + glyoxylate + H2O + FMN
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + O2 + FMNH2 + H+
iminodiacetate + glyoxylate + H2O + FMN
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
ir
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: specific substrate
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: nitrilotriacetate is only a substrate when complexed with cations such as Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+. The enzyme shows little preference for Mg-nitrilotriacetate over Co-nitrilotriacetate, Ni-nitrilotriacetate, and Zn-nitrilotriacetate
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: specific substrate
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: nitrilotriacetate is only a substrate when complexed with cations such as Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+. The enzyme shows little preference for Mg-nitrilotriacetate over Co-nitrilotriacetate, Ni-nitrilotriacetate, and Zn-nitrilotriacetate
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
ir
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
ir
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 2% reactivity with N-methyl-iminodiacetate, N-acetamido-iminodiacetate, N-hydroxyethyl-iminodiacetate, EDTA, trimethylamine, triethanolamine, dimethylamine, dimethylglycine, methylamine, sarcosine, anthranilate, betaine, N-methylglutamate, N-methylalanine, N-methylaspartate, N-acetylglutamate, N-methylphenylalanine, N-methylleucine, N-methyltryptophane, glutamate, aspartate, citrate, proline, imidazoleacetate, asparagine, and ethylenediamine-N,N'-diacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitrilotriacetate not complexed with cation is not degraded. The addition of Cr2+,Ba2+, Sr2+, Cr3+, K+, or Na+ results in no degradation of nitrilotriacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the NTA monooxygenase activity requires two component proteins, component A and component B. Component A is an NTA monooxygenase that uses FMNH2 and O2 to oxidize nitrilotriacetate, and component B is an NADH:FMN oxidoreductase that provides FMNH2 for nitrilotriacetate oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the NTA monooxygenase activity requires two component proteins, component A and component B. Component A is an NTA monooxygenase that uses FMNH2 and O2 to oxidize nitrilotriacetate, and component B is an NADH:FMN oxidoreductase that provides FMNH2 for nitrilotriacetate oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 2% reactivity with N-methyl-iminodiacetate, N-acetamido-iminodiacetate, N-hydroxyethyl-iminodiacetate, EDTA, trimethylamine, triethanolamine, dimethylamine, dimethylglycine, methylamine, sarcosine, anthranilate, betaine, N-methylglutamate, N-methylalanine, N-methylaspartate, N-acetylglutamate, N-methylphenylalanine, N-methylleucine, N-methyltryptophane, glutamate, aspartate, citrate, proline, imidazoleacetate, asparagine, and ethylenediamine-N,N'-diacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitrilotriacetate not complexed with cation is not degraded. The addition of Cr2+,Ba2+, Sr2+, Cr3+, K+, or Na+ results in no degradation of nitrilotriacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the NTA monooxygenase activity requires two component proteins, component A and component B. Component A is an NTA monooxygenase that uses FMNH2 and O2 to oxidize nitrilotriacetate, and component B is an NADH:FMN oxidoreductase that provides FMNH2 for nitrilotriacetate oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also involved in 6 : 2 fluorotelomer sulfonate desulfonation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also involved in 6 : 2 fluorotelomer sulfonate desulfonation
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
nitrilotriacetate + FMNH2 + H+ + O2
iminodiacetate + glyoxylate + FMN + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also involved in 6 : 2 fluorotelomer sulfonate desulfonation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also involved in 6 : 2 fluorotelomer sulfonate desulfonation
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
omission of FMN or replacement of FMN by FAD results in a residual activity of 2% when component B is not resaturated with FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
Co2+
Cu2+
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
Fe2+
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
Mg2+
Mn2+
-
Mn2+ ions are able to replace Mg2+ but lead to a higher uncoupled NADH oxidation and enzyme activity is reduced to 70% of that with MgCl2
Ni2+
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
Zn2+
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
additional information
Co2+
-
may replace Mg2+, enzyme activity is reduced to 80% of that with MgCl2
Co2+
-
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+
Mg2+
-
the enzyme shows little preference for Mg-nitrilotriacetate over Co-nitrilotriacetate, Ni-nitrilotriacetate, and Zn-nitrilotriacetate
Mg2+
-
EDTA monooxygenase degrades nitrilotriacetate in the absence or presence of Mg2+
additional information
-
no nitrilotriacetate consumption is observed with Ca2+,Fe2+, Fe3+, Zn2+, Cu2+, or Ni2+
additional information
-
the enzyme contains less than 0.15 atom of Fe per mol of protein, indicating that neither Fe-sulfur clusters nor cytochromes are present
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
component A of NTA monooxygenase
-
the ability of component B of NTA monooxygenase to catalyze the oxidation of nitrilotriacetate to iminodiacetate and glyoxylate is completely dependent on the presence of component A
-
FMN
-
NTA-Mo activity increases by a factor of 4 when 0.003 mM FMN is included in the assay mixture, there is 0.4 mol of FMN per mol of purified component B
additional information
-
the activity is increased neither by additions of 20% (w/v) polyethylene glycol or sorbitol
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Dynamics of Substrate Consumption and Enzyme Synthesis in Chelatobacter heintzii during Growth in Carbon-Limited Continuous Culture with Different Mixtures of Glucose and Nitrilotriacetate.
Tuberculosis
Structure of nitrilotriacetate monooxygenase component B from Mycobacterium thermoresistibile.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0317
nitrilotriacetate
-
with equimolar Ni2+ (0.04-0.2 mM), in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
0.0367
nitrilotriacetate
-
with equimolar Co2+ (0.04-0.2 mM), in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
0.0404
nitrilotriacetate
-
with equimolar Mg2+ (0.04-0.2 mM), in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
0.043
nitrilotriacetate
-
with 2 mM Mg2+and varying nitrilotriacetate concentrations, in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
0.0576
nitrilotriacetate
-
with equimolar Zn2+ (0.04-0.2 mM), in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
0.0905
nitrilotriacetate
-
with equimolar Mn2+ (0.04-0.2 mM), in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
0.0968
nitrilotriacetate
-
with equimolar Fe2+ (0.04-0.2 mM), in 20 mM HEPES buffer (pH 7.6), 0.01 mM FMN, at 24°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.076
in 30 mM Tris-HCl (pH 8.0), 10 mM FMN, and 2 mM MgCl2, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
-
pH optimum for NTA consumption in cell extracts. At pH 7.2 and 8.4, 25% of the maximum activity is obtained, and no activity is left at pH 6.0 or 9.0
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.6
-
35% activity of the purified enzyme remains at pH 7.0 and 9.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
12% activity is left at 2°C, and no activity is observed at 40°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
component A of nitrilotriacetate monooxygenase
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (880 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
2 * 36000, component B of NTA monooxygenase, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 1.6 M NH2SO4, 0.1 M NaCl and 0.1 M HEPES pH 7.5
-
sitting drop vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M MES pH 6.0 and 20% PEG 6000
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity is rather unstable in crude cell extract, even in the presence of the protease inhibitors leupeptin and pepstatin
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified component B of NTA monooxygenase in 20 mM HEPES buffer with 2 mM dithiothreitol, at pH 7.8, several months, without any significant loss of activity
-
-80°C, partially purified, dialyzed enzyme, 3 months, no loss of activity
-
4°C, purified component B of NTA monooxygenase in 20 mM HEPES buffer at pH 7.8, 7 days, 70% loss of activity
-
4°C, purified component B of NTA monooxygenase in 20 mM HEPES buffer with 2 mM dithiothreitol and ammonium sulfate to 5% saturation, at pH 7.8, 7 days, 5% loss of activity
-
4°C, purified component B of NTA monooxygenase in 20 mM HEPES buffer with 2 mM dithiothreitol, at pH 7.8, 7 days, 20% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Blue 3GA agarose column chromatography, MonoQ HR 5/5 column chromatography, and hydroxyapatite column chromatography
-
ammonium sulfate precipitation, phenyl Sepharose column chromatography, TMAE-Fractogel column chromatography, and phenyl Superose column chromatography
-
HisTrap FF column chromatography and Superdex 75 gel filtration
Ni-NTA column chromatography, HiTrap Q anion-exchange column chromatography
-
partially purified by ammonium sulfate precipitation and phenyl agarose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) Rosetta cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction of nitrilotriacetate-degrading enzyme proceeds faster when the culture is supplied with mixtures of D-glucose and nitrilotriacetate rather than with nitrilotriacetate alone
starvation of nitrilotriacetate-grown cells leads to a loss of nitrilotriacetate monooxygenase protein. A transition from nitrilotriacetate to D-glucose is accompanied by a rapid loss of nitrilotriacetate monooxygenase
synthesis of nitrilotriacetate monooxygenase becomes induced when nitrilotriacetate contributes to more than approximately 1-3% of the total carbon in the substrate mixture supplied
induction of nitrilotriacetate-degrading enzyme proceeds faster when the culture is supplied with mixtures of D-glucose and nitrilotriacetate rather than with nitrilotriacetate alone
-
induction of nitrilotriacetate-degrading enzyme proceeds faster when the culture is supplied with mixtures of D-glucose and nitrilotriacetate rather than with nitrilotriacetate alone
-
-
starvation of nitrilotriacetate-grown cells leads to a loss of nitrilotriacetate monooxygenase protein. A transition from nitrilotriacetate to D-glucose is accompanied by a rapid loss of nitrilotriacetate monooxygenase
-
starvation of nitrilotriacetate-grown cells leads to a loss of nitrilotriacetate monooxygenase protein. A transition from nitrilotriacetate to D-glucose is accompanied by a rapid loss of nitrilotriacetate monooxygenase
-
-
synthesis of nitrilotriacetate monooxygenase becomes induced when nitrilotriacetate contributes to more than approximately 1-3% of the total carbon in the substrate mixture supplied
-
synthesis of nitrilotriacetate monooxygenase becomes induced when nitrilotriacetate contributes to more than approximately 1-3% of the total carbon in the substrate mixture supplied
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uetz, T.; Schneider, R.; Snozzi, M.; Egli, T.
Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600
J. Bacteriol.
174
1179-1188
1992
Aminobacter aminovorans, Aminobacter aminovorans ATCC 29600
brenda
Kim, K.J.; Kim, S.; Lee, S.; Kang, B.S.; Lee, H.S.; Oh, T.K.; Kim, M.H.
Crystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A
Acta Crystallogr. Sect. F
62
1141-1143
2006
Corynebacterium glutamicum
brenda
Zhang, Y.; Edwards, T.E.; Begley, D.W.; Abramov, A.; Thompkins, K.B.; Ferrell, M.; Guo, W.J.; Phan, I.; Olsen, C.; Napuli, A.; Sankaran, B.; Stacy, R.; Van Voorhis, W.C.; Stewart, L.J.; Myler, P.J.
Structure of nitrilotriacetate monooxygenase component B from Mycobacterium thermoresistibile
Acta Crystallogr. Sect. F
67
1100-1105
2011
Mycolicibacterium thermoresistibile (E5Q9D7), Mycolicibacterium thermoresistibile
brenda
Bally, M.; Egli, T.
Dynamics of substrate consumption and enzyme synthesis in Chelatobacter heintzii during growth in carbon-limited continuous culture with different mixtures of glucose and nitrilotriacetate
Appl. Environ. Microbiol.
62
133-140
1996
Aminobacter aminovorans, Aminobacter aminovorans ATCC 29600
brenda
Ternan, N.G.; McMullan, G.
Iminodiacetate and nitrilotriacetate degradation by Kluyveromyces marxianus IMB3
Biochem. Biophys. Res. Commun.
290
802-805
2002
Kluyveromyces marxianus, Kluyveromyces marxianus IMB3
brenda
Xun, L.; Reeder, R.; Plymale, A.; Girvin, D.; Bolton Jr., H.
Degradation of metal - nitrilotriacetate complexes by nitrilotriacetate monooxygenase
Environ. Sci. Technol.
30
1752-1755
1996
Aminobacter aminovorans, Aminobacter aminovorans ATCC 29600
-
brenda
Knobel, H.R.; Egli, T.; van der Meer, J.R.
Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600
J. Bacteriol.
178
6123-6132
1996
Aminobacter aminovorans (P54989), Aminobacter aminovorans, Aminobacter aminovorans ATCC 29600 (P54989)
brenda
Xu, Y.; Mortimer, M.W.; Fisher, T.S.; Kahn, M.L.; Brockman, F.J.; Xun, L.
Cloning, sequencing, and analysis of a gene cluster from Chelatobacter heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase
J. Bacteriol.
179
1112-1116
1997
Aminobacter aminovorans (P54989), Aminobacter aminovorans, Aminobacter aminovorans ATCC 29600 (P54989)
brenda
Payne, J.W.; Bolton, H.; Campbell, J.A.; Xun, L.
Purification and characterization of EDTA monooxygenase from the EDTA-degrading bacterium BNC1
J. Bacteriol.
180
3823-3827
1998
Chelativorans sp. BNC1
brenda
Bally, M.; Wilberg, E.; Kuhni, M.; Egli, T.
Growth and regulation of enzyme synthesis in the nitrilotriacetic acid (NTA)-degrading bacterium Chelatobacter heintzii ATCC 29600
Microbiology
140
1927-1936
1994
Aminobacter aminovorans, Aminobacter aminovorans ATCC 29600
brenda
Van Hamme, J.; Bottos, E.; Bilbey, N.; Brewer, S.
Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation to 6: 2 fluorotelomer sulfonate biodegradation
Microbiology
159
1618-1628
2013
Gordonia sp., Gordonia sp. NB4-1Y
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.10)
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