Information on EC 1.16.1.9 - ferric-chelate reductase (NADPH)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.16.1.9
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RECOMMENDED NAME
GeneOntology No.
ferric-chelate reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
Fe(II)-siderophore:NADP+ oxidoreductase
Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine [3]. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Ashley
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 Fe(II)-2,6-dichloroindophenol + NADP+ + H+
2 Fe(III)-2,6-dichloroindophenol + NADPH
show the reaction diagram
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-
-
-
?
2 Fe(II)-cytochrome c + NADP+ + H+
2 Fe(III)-cytochrome c + NADPH
show the reaction diagram
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-
-
-
?
2 Fe(II)-ferricyanide + NADP+ + H+
2 Fe(III)-ferricyanide + NADPH
show the reaction diagram
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-
-
-
?
2 Fe(II)-siderophore + NADP+ + H+
2 Fe(III)-siderophore + NADPH
show the reaction diagram
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
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-
-
-
?
2,6-dichloroindophenol + NADPH + H+
?
show the reaction diagram
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best substrate in the presence and absence of FAD
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-
?
an Fe(III)-siderophore + NADPH
Fe(II) + an apo-siderophore + NADP+ + H+
show the reaction diagram
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-
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?
cytochrome c + NADPH + H+
?
show the reaction diagram
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-
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?
Fe(II) + an apo-siderophore + NADP+ + H+
an Fe(III)-siderophore + NADPH
show the reaction diagram
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-
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-
?
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 + NADPH + H+
Fe(II) + (2,3-dihydroxybenzoyl-Gly-Thr)3 + NADP+
show the reaction diagram
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-
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?
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 + NADPH + H+
Fe(II) + (2,3-dihydroxybenzoyl-L-serine)3 + NADP+
show the reaction diagram
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-
-
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?
Fe(III)-aerobactin + NADPH + H+
Fe(II) + aerobactin + NADP+
show the reaction diagram
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-
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?
Fe(III)-bacillibactin + NADPH + H+
Fe(II) + bacillibacitin + NADP+
show the reaction diagram
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-
-
-
?
Fe(III)-citrate + NADPH + H+
?
show the reaction diagram
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-
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?
Fe(III)-deferoxamine + NADPH + H+
?
show the reaction diagram
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-
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?
Fe(III)-dicitrate + NADPH + H+
Fe(II) + citrate + NADP+
show the reaction diagram
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-
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?
Fe(III)-diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADPH + H+
Fe(II) + diethylenetriamine-N,N,N',N'',N''-pentaacetate + NADP+ + H+
show the reaction diagram
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-
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?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
show the reaction diagram
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+ + H+
show the reaction diagram
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-
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?
Fe(III)-enterobactin + NADPH + H+
Fe(II) + enterobactin + NADP+
show the reaction diagram
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-
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?
Fe(III)-ferrichrome + NADPH + H+
?
show the reaction diagram
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-
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?
Fe(III)-nitrilotriacetic acid + NADPH + H+
?
show the reaction diagram
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-
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?
Fe(III)-o,o-EDDHA I + NADPH
Fe(II)-o,o-EDDHA I + NADP+ + H+
show the reaction diagram
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i.e. ethylenediaminebis(o-hydroxyphenyl)acetic acid
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-
?
Fe(III)-vibriobactin + NADPH + H+
Fe(II) + vibriobactin + NADP+
show the reaction diagram
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?
ferric ammonium citrate + NADPH + H+
?
show the reaction diagram
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?
ferric enterobactin + NADPH + H+
?
show the reaction diagram
ferritin + NADPH + H+
?
show the reaction diagram
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?
tert-butyl hydroperoxide + NADPH + H+
?
show the reaction diagram
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?
transferrin + NADPH + H+
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 Fe(II)-siderophore + NADP+ + H+
2 Fe(III)-siderophore + NADPH
show the reaction diagram
additional information
?
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DNA degradation occurring in the presence of NADPH, Fe(III)-EDTA and hydrogen peroxide is potently enhanced by the purified enzyme, indicating that the enzyme may drive the Fenton reaction, reducing ferric iron to ferrous iron when it evokes the Fenton reaction
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavocytochrome b
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NADP+
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dependent on
NADPH
additional information
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the enzyme is flavin-independent
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
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the enzyme is able to reduce iron compounds in the absence of free flavin, but the ferric reduction by the enzyme is enhanced by the addition of free flavin n the presence of natural chelate iron compounds but also synthetic chelate iron compounds
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0042
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3
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wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25C
0.0018 - 0.04
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
0.048
Fe(III)-aerobactin
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wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25C
0.0276 - 0.16
Fe(III)-citrate
0.0134 - 0.066
Fe(III)-dicitrate
0.0168 - 0.5762
Fe(III)-EDTA
0.0004 - 0.0078
Fe(III)-enterobactin
0.0014
Fe(III)-vibriobactin
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wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25C
0.043
NADPH
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at pH 7.5 and 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 1.11
Fe(III)-citrate
0.95 - 2
Fe(III)-EDTA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.193
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3
Escherichia coli
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wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25C
89208
0.091 - 23.35
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3
28937
0.02
Fe(III)-aerobactin
Escherichia coli
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wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25C
89207
1.59 - 41
Fe(III)-citrate
10915
0.139 - 5.427
Fe(III)-dicitrate
28938
0.12 - 122
Fe(III)-EDTA
4739
0.032 - 8.211
Fe(III)-enterobactin
28936
1.268
Fe(III)-vibriobactin
Escherichia coli
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wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25C
89206
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001
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using ferric enterobactin as substrate, at pH 7.5 and 37C
0.02
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crude extract, using tert-butyl hydroperoxide as substrate, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25C
0.022
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using Fe(III)-EDTA as substrate, at pH 7.5 and 37C
0.91
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after 45.5fold purification, using tert-butyl hydroperoxide as substrate, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.4
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calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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detected in mesophyll and parenchyma cells
Manually annotated by BRENDA team
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detected in the infection zone and nitrogen-fixing region
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 34000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M succinic acid-sodium phosphate dibasic-glycine buffer pH 4.0 and 18% (w/v) PEG 1500
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl Toyopearl column chromatography, DEAE Sepharose column chromatography, POROS HQ-H column chromatography, and Red Sepharose column chromatography; native enzyme
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HiTrap DEAE column chromatography, Superdex 75 gel filtration
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Ni-NTA-Sepharose column chromatography and DEAE Sepharose column chromatography
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Strep-Tactin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli DH10B cells
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expressed in Escherichia coli strain JM109
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expressed in Saccharomyces cerevisiae strain DY1457
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of Fe2+ decreases yqjH expression starting at 100 nM, with a maximum repression of 4fold occurring at 0.01 mM Fe2+. Addition of CoCl2 concentrations of more than 500 nM also repress yqjH expression by about 50%
FRO2 transcript shows abundance under iron deficiency. The addition of 300 mM bathocuproine disulfonic acid further reduces FRO2 transcript abundance in plants grown under high-iron conditions for 3 days
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the enzyme is expressed at high levels in iron-deficient roots
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YqjI-dependent transcriptional repression is reduced when cells are exposed to elevated nickel levels, resulting in increased expression of yqjH. Upon addition of NiCl2, yqjH expression increases starting at 100 nM NiCl2, with maximum induction by 0.001 mM NiCl2 (42%). Deletion of yqjI leads to constitutive expression levels of yqjH that are 30fold higher than wild type basal expression levels
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K55A
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the mutant shows strongly reduced activity compared to the wild type enzyme
R130A
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the mutant shows strongly reduced activity compared to the wild type enzyme
R246A
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the variant is rather unstable, showing precipitate formation and cofactor release during protein concentration
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