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Information on EC 7.2.1.3 - ascorbate ferrireductase (transmembrane)
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7.2.1.3 ascorbate ferrireductase (transmembrane)IUBMB Comments
A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates.
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Word Map
- 7.2.1.3
- photosystem
- hepcidin
-
ferroportin
- hephaestin
-
iron-deficient
-
fe-deficient
- beta-hydroxylase
- hemochromatosis
-
high-potential
- monodehydroascorbate
-
oxygen-evolving
-
extravesicular
- pheophytin
-
iron-related
-
calcareous
-
ascorbate-reducible
-
flash-induced
- semidehydroascorbate
-
alpha-bands
-
3-3,4-dichlorophenyl-1,1-dimethylurea
- ferroxidase
-
fe-sufficient
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cytochrome b561, cytochrome b-559, dcytb, ferric chelate reductase, duodenal cytochrome b, cybrd1, cyt b561, cyb561, cyt-b561, lcytb, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ascorbate-cytochrome b5 reductase
-
-
-
-
ascorbate-dependent ferrireductase
CGCytb
chromaffin granule CYB561
chromaffin granule cytochrome b
CYB561
Cybrd1
Cyt b561
Cyt-b561
cytochrome b561
DCytb
duodenal cytochrome b
EC 1.10.2.1
-
-
formerly
-
EC 1.16.5.1
-
-
formerly
-
ferric reductase
LCytb
lysosomal cytochrome b
TCytb
cytochrome b561
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
-
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
reaction mechanism
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
reaction mechanism
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
reaction mechanism
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
reaction mechanism
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
reaction mechanism
ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Fe(III):ascorbate oxidorectuctase (electron-translocating)
A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates.
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CAS REGISTRY NUMBER
COMMENTARY
37237-57-3
-
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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
ascorbate[side 1] + Fe3+-EDTA[side 2]
monodehydroascorbate[side 1] + Fe2+-EDTA[side 2]
-
compared with FeCN, Fe3+-EDTA is a relatively poor substrate for the enzyme (20-35fold lower ferrireductase activities)
-
-
?
ascorbate[side 1] + ferricyanide[side 2]
monodehydroascorbate[side 1] + ferrocyanide[side2]
-
-
-
-
-
ascorbate[side 1] + nitroblue tetrazolium[side 2]
dehydroascorbate + ?
-
-
-
-
?
bathocuprionedisulfonate[side 1] + Cu(II)-nitrilotriacetic acid[side 2]
Cu(I)-bathocuproinedisulfonate
-
-
-
-
?
ferrozine[side 1] + Fe(III)-nitrilotriacetic acid[side 2]
Fe(II)-ferrozine
-
-
-
-
?
ascorbate[side 1] + Fe(CN)3[side 2]
monodehydroascorbate[side 1] + ?
-
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
r
ascorbate[side 1] + Fe3+-EDTA[side 2]
monodehydroascorbate[side 1] + ?
-
-
-
-
?
ascorbate[side 1] + Fe3+-EDTA[side 2]
monodehydroascorbate[side 1] + ?
-
-
-
-
?
ascorbate[side 1] + Fe3+-EDTA[side 2]
monodehydroascorbate[side 1] + ?
-
-
-
-
?
L-(+)-ascorbate + ferricytochrome b5
monodehydro-L(+)-ascorbate + ferrocytochrome b5
-
-
-
-
?
L-(+)-ascorbate + ferricytochrome b5
monodehydro-L(+)-ascorbate + ferrocytochrome b5
-
the microsomal enzyme participates in the ascorbate-dependent fatty acid desaturation
-
-
?
L-ascorbate + ferricytochrome b5
monodehydro-L-ascorbate + ferrocytochrome b5
-
-
-
-
?
L-ascorbate + ferricytochrome b5
monodehydro-L-ascorbate + ferrocytochrome b5
-
-
-
-
?
L-ascorbate + ferricytochrome b5
monodehydro-L-ascorbate + ferrocytochrome b5
-
-
-
-
?
L-ascorbate + ferricytochrome b5
monodehydro-L-ascorbate + ferrocytochrome b5
-
-
-
-
?
L-ascorbate + ferricytochrome b5
monodehydroascorbate + ferrocytochrome b5 + H+
-
-
-
-
r
L-ascorbate + ferricytochrome b5
monodehydroascorbate + ferrocytochrome b5 + H+
-
-
-
-
r
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
trans-membrane ferric reductase activity is also demonstrated in a reconstituted proteoliposome system with ascorbate as the electron donor inside the liposomes, recombinant CGCytb as trans-membrane electron carrier, and ferricyanide as the electron acceptor outside the liposomes. A few members of the CYB561 protein family function as ferric reductases in vivo. The other heme-b center is responsible for the ascorbate oxidation by iozyme CGCytb
-
-
?
additional information
?
-
enzyme assays also with purified chromaffin granule membrane ghosts, or purified proteins in detergent micelles, or in reconstituted membrane vesicles. Structure-function relationship, overview
-
-
?
additional information
?
-
the other heme-b center is responsible for the ascorbate oxidation by iozyme CGCytb. Structure-function relationship, overview
-
-
?
additional information
?
-
-
Dcytb has the capacity to reduce both iron and copper complexes
-
-
?
additional information
?
-
the other heme-b center is responsible for the ascorbate oxidation by iozyme CGCytb. Structure-function relationship, overview
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
a few members of the CYB561 protein family function as ferric reductases in vivo
-
-
?
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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
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
?
ascorbate[side 1] + Fe(III)[side 2]
monodehydroascorbate[side 1] + Fe(II)[side 2]
-
-
-
r
L-(+)-ascorbate + ferricytochrome b5
monodehydro-L(+)-ascorbate + ferrocytochrome b5
-
-
-
-
?
L-(+)-ascorbate + ferricytochrome b5
monodehydro-L(+)-ascorbate + ferrocytochrome b5
-
the microsomal enzyme participates in the ascorbate-dependent fatty acid desaturation
-
-
?
additional information
?
-
trans-membrane ferric reductase activity is also demonstrated in a reconstituted proteoliposome system with ascorbate as the electron donor inside the liposomes, recombinant CGCytb as trans-membrane electron carrier, and ferricyanide as the electron acceptor outside the liposomes. A few members of the CYB561 protein family function as ferric reductases in vivo. The other heme-b center is responsible for the ascorbate oxidation by iozyme CGCytb
-
-
?
additional information
?
-
a few members of the CYB561 protein family function as ferric reductases in vivo
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
additions of ascorbate to oxidized wild-type Zmb561 and His6-tagged recombinant Zmb561 causes a quick reduction of heme b reaching the final reduction level of about 80%, suggesting that Zmb561 might utilize ascorbate as a physiological reductant in maize cells
ascorbate
cytosolic ascorbate is the cellular electron donor for the CYB561 proteins
ascorbate
cytosolic ascorbate is the cellular electron donor for the CYB561 proteins
ascorbate
cytosolic ascorbate is the cellular electron donor for the CYB561 proteins
ascorbate
cytosolic ascorbate is the cellular electron donor for the CYB561 proteins
ascorbate
cytosolic ascorbate is the cellular electron donor for the CYB561 proteins
ascorbate
cytosolic ascorbate is the cellular electron donor for the CYB561 proteins
heme
each monomer of the homodimeric protein possesses cytoplasmic and apical heme groups
heme b
cytosolic heme b prosthetic group, the transmembrane electron transport protein cytochromes b561 has two heme ligation sites
heme b
two heme-b centers and CYB561 protein, structure analysis and comparisons, overview. Midpoint redox potentials of heme b, comparisons
heme b
two heme-b centers and CYB561 protein, structure analysis and comparisons, overview. Midpoint redox potentials, spin, and spectra of heme b, comparisons
heme b
two heme-b centers and CYB561 protein, structure analysis and comparisons, overview. Midpoint redox potentials, spin, and spectra of heme b, comparisons
heme b
two heme-b centers and CYB561 protein, structure analysis and comparisons, overview. Midpoint redox potentials, spin, and spectra of heme b, comparisons
heme b
two heme-b centers and CYB561 protein, structure analysis and comparisons, overview. Midpoint redox potentials, spin, and spectra of heme b, comparisons. The high-potential heme-b, characterized with a low-spin EPR signal in the vicinity of gz = 3.1, is located on the cytosolic side of the protein
heme b
two heme-b centers are coordinated by two pairs of His residues localized in the central four transmembrane domains, probably very close to the membrane interface. The midpoint redox potentials of the two hemes are above 0 mV and about 100 mV apart from each other. CYB561 protein structure analysis and comparisons, overview. Midpoint redox potentials, spin, and spectra of heme b, comparisons. The high-potential heme-b center of CGCytb is located on the cytosolic side of the protein, mutational analysis
additional information
neither ferrocyanide nor durohydroquinone can reduce nCGCytb
-
additional information
neither ferrocyanide nor durohydroquinone can reduce nCGCytb
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethylpyrocarbonate
-
the electron accepting ability of bovine cytochrome b561 from ascorbate is selectively inhibited by the treatment with diethylpyrocarbonate
Zn2+
1 mM, 43% residual activity. Zn2+ coordinates to two hydroxyl groups of the apical ascorbate and to a histidine residue. Fe3+ competes with Zn2+ for this binding site
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
cytb561 ferric reductase activity is greatly enhanced by the addition of ascorbate
dehydroascorbate
-
preloading cells with dehydroascorbate greatly increases both ferric and cupric reductase activities of Dcytb
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Overexpression of cellular iron import proteins is associated with malignant progression of esophageal adenocarcinoma.
Anemia
Altered expression of intestinal duodenal cytochrome b and divalent metal transporter 1 might be associated with cardio-renal anemia syndrome.
Anemia
Fermented Goat's Milk Consumption Improves Duodenal Expression of Iron Homeostasis Genes during Anemia Recovery.
Anemia
Immunolocalization of duodenal cytochrome B: a relationship with circulating markers of iron status.
Anemia, Hypochromic
CIPK23 is involved in iron acquisition of Arabidopsis by affecting ferric chelate reductase activity.
Anemia, Hypochromic
Overexpression of AtFRO6 in transgenic tobacco enhances ferric chelate reductase activity in leaves and increases tolerance to iron-deficiency chlorosis.
Anemia, Sideroblastic
Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers.
ascorbate ferrireductase (transmembrane) deficiency
Congenital absence of norepinephrine due to CYB561 mutations.
Brain Diseases
Clonic seizures, continuous spikes-and-waves during slow sleep, choreoathetosis and response to sulthiame in a child with FRRS1L encephalopathy.
Brain Diseases
Loss of Frrs1l disrupts synaptic AMPA receptor function, and results in neurodevelopmental, motor, cognitive and electrographical abnormalities.
Breast Neoplasms
DCYTB is a predictor of outcome in breast cancer that functions via iron-independent mechanisms.
Carcinoma
Expression profiling of adrenocortical neoplasms suggests a molecular signature of malignancy.
Colorectal Neoplasms
A novel test for gene-ancestry interactions in genome-wide association data.
Colorectal Neoplasms
Duodenal cytochrome b (Cybrd1) ferric reductase functional studies in cells.
Fatty Liver
Association of mRNA expression of iron metabolism-associated genes and progression of non-alcoholic steatohepatitis in rats.
Friedreich Ataxia
Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers.
Glioblastoma
Highly Expressed CYBRD1 Associated with Glioma Recurrence Regulates the Immune Response of Glioma Cells to Interferon.
Glioblastoma
Mouse cytochrome b561: cDNA cloning and expression in rat brain, mouse embryos, and human glioma cell lines.
Glioma
Highly Expressed CYBRD1 Associated with Glioma Recurrence Regulates the Immune Response of Glioma Cells to Interferon.
Glioma
Mouse cytochrome b561: cDNA cloning and expression in rat brain, mouse embryos, and human glioma cell lines.
Hemochromatosis
A novel association between a SNP in CYBRD1 and serum ferritin levels in a cohort study of HFE hereditary haemochromatosis.
Hemochromatosis
Analysis of genes implicated in iron regulation in individuals presenting with primary iron overload.
Hemochromatosis
Analysis of polymorphism and hepatic expression of duodenal cytochrome b in chronic hepatitis C.
Hemochromatosis
Duodenal cytochrome b (Cybrd1) ferric reductase functional studies in cells.
Hemochromatosis
Duodenal cytochrome b and hephaestin expression in patients with iron deficiency and hemochromatosis.
Hemochromatosis
Duodenal Dcytb and hephaestin mRNA expression are not significantly modulated by variations in body iron homeostasis.
Hemochromatosis
Duodenal expression of iron transport molecules in untreated haemochromatosis subjects.
Hemochromatosis
Regulatory defects in liver and intestine implicate abnormal hepcidin and Cybrd1 expression in mouse hemochromatosis.
Hepatitis C, Chronic
Analysis of polymorphism and hepatic expression of duodenal cytochrome b in chronic hepatitis C.
Hypotension, Orthostatic
Mutations in CYB561 Causing a Novel Orthostatic Hypotension Syndrome.
Iron Deficiencies
CIPK23 is involved in iron acquisition of Arabidopsis by affecting ferric chelate reductase activity.
Iron Deficiencies
Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice.
Iron Deficiencies
Differing expression of genes involved in non-transferrin iron transport across plasma membrane in various cell types under iron deficiency and excess.
Iron Deficiencies
Duodenal cytochrome b and hephaestin expression in patients with iron deficiency and hemochromatosis.
Iron Deficiencies
Duodenal Dcytb and hephaestin mRNA expression are not significantly modulated by variations in body iron homeostasis.
Iron Deficiencies
Duodenal Reductase Activity and Spleen Iron Stores Are Reduced and Erythropoiesis Is Abnormal in Dcytb Knockout Mice Exposed to Hypoxic Conditions.
Iron Deficiencies
FIT interacts with AtbHLH38 and AtbHLH39 in regulating iron uptake gene expression for iron homeostasis in Arabidopsis.
Iron Deficiencies
Gene expression profiling of Hfe-/- liver and duodenum in mouse strains with differing susceptibilities to iron loading: identification of transcriptional regulatory targets of Hfe and potential hemochromatosis modifiers.
Iron Deficiencies
High-fat diet causes iron deficiency via hepcidin-independent reduction of duodenal iron absorption.
Iron Deficiencies
Immunolocalization of duodenal cytochrome B: a relationship with circulating markers of iron status.
Iron Deficiencies
Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency.
Iron Deficiencies
Microbial siderophores exert a subtle role in Arabidopsis during infection by manipulating the immune response and the iron status.
Iron Deficiencies
Molecular and functional roles of duodenal cytochrome B (Dcytb) in iron metabolism.
Iron Deficiencies
Mutational reconstructed ferric chelate reductase confers enhanced tolerance in rice to iron deficiency in calcareous soil.
Iron Deficiencies
Nonclinical Characterization of the Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibitor Roxadustat, a Novel Treatment of Anemia of Chronic Kidney Disease.
Iron Deficiencies
Overexpression of AtFRO6 in transgenic tobacco enhances ferric chelate reductase activity in leaves and increases tolerance to iron-deficiency chlorosis.
Iron Deficiencies
Overexpression of the FRO2 ferric chelate reductase confers tolerance to growth on low iron and uncovers posttranscriptional control.
Iron Deficiencies
Regulatory networks for the control of body iron homeostasis and their dysregulation in HFE mediated hemochromatosis.
Iron Deficiencies
Responses to iron deficiency in Arabidopsis thaliana: the Turbo iron reductase does not depend on the formation of root hairs and transfer cells.
Iron Deficiencies
The molecular circuitry regulating the switch between iron deficiency and overload in mice.
Iron Deficiencies
[Mutational reconstructed ferric chelate reductase confers enhanced tolerance in rice to iron deficiency in calcareous soil]
Iron Overload
Analysis of genes implicated in iron regulation in individuals presenting with primary iron overload.
Iron Overload
Analysis of polymorphism and hepatic expression of duodenal cytochrome b in chronic hepatitis C.
Iron Overload
Effect of lipopolysaccharide and bleeding on the expression of intestinal proteins involved in iron and haem transport.
Iron Overload
Iron overload in adult Hfe-deficient mice independent of changes in the steady-state expression of the duodenal iron transporters DMT1 and Ireg1/ferroportin.
Iron Overload
The molecular circuitry regulating the switch between iron deficiency and overload in mice.
Lymphoma, B-Cell
Genomic structure and expression of the human gene encoding cytochrome b561, an integral protein of the chromaffin granule membrane.
Neoplasm Metastasis
DCYTB is a predictor of outcome in breast cancer that functions via iron-independent mechanisms.
Neoplasms
DCYTB is a predictor of outcome in breast cancer that functions via iron-independent mechanisms.
Neoplasms
Electron Transfer Reactions of Candidate Tumor Suppressor 101F6 Protein, a Cytochrome b561 Homologue, with Ascorbate and Monodehydroascorbate Radical.
Neoplasms
Elevated expression of the cytochrome b561, a neuroendocrine vesicle protein, in castration resistant prostate tumors.
Neoplasms
Genomic structure and expression of the human gene encoding cytochrome b561, an integral protein of the chromaffin granule membrane.
Neoplasms
Highly Expressed CYBRD1 Associated with Glioma Recurrence Regulates the Immune Response of Glioma Cells to Interferon.
Neoplasms
Identification of potential genes in upper tract urothelial carcinoma using next-generation sequencing with bioinformatics and in vitro analyses.
Neoplasms
Overexpression of the natural antisense hypoxia-inducible factor-1alpha transcript is associated with malignant phaeochromocytoma/paraganglioma.
Neoplasms
Spectral characterization of the recombinant mouse tumor suppressor 101F6 protein.
Porphyria Cutanea Tarda
Iron homeostasis in porphyria cutanea tarda: mutation analysis of promoter regions of CP, CYBRD1, HAMP and SLC40A1.
Porphyrias
Iron homeostasis in porphyria cutanea tarda: mutation analysis of promoter regions of CP, CYBRD1, HAMP and SLC40A1.
Prostatic Neoplasms
Elevated expression of the cytochrome b561, a neuroendocrine vesicle protein, in castration resistant prostate tumors.
Urinary Bladder Neoplasms
Identification of potential genes in upper tract urothelial carcinoma using next-generation sequencing with bioinformatics and in vitro analyses.
Vitamin A Deficiency
Vitamin a modulates the expression of genes involved in iron bioavailability.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
stopped-flow kinetic analysis at pH 5.0-7.0
-
0.0152
Cu(II)-nitrilotriacetic acid[side 2]
-
in 25 mM MOPS, 25 mM MES, 5.4 mM KCl, 5 mM glucose, 140 mM NaCl, 1.8 mM CaCl2, 0.8 mM MgCl2, pH 7.0, at 22°C
0.0231
Cu(II)-nitrilotriacetic acid[side 2]
-
in 25 mM MOPS, 25 mM MES, 5.4 mM KCl, 5 mM glucose, 140 mM NaCl, 1.8 mM CaCl2, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0018
cytochrome b5
-
rat microsome cytochrome-b5, detergent preparation
-
0.0022
cytochrome b5
-
rabbit microsome cytochrome-b5, trypsin preparation
-
0.0025
cytochrome b5
-
pig microsome cytochrome-b5, detergent preparation
-
0.003
cytochrome b5
-
rabbit microsome cytochrome-b5, detergent preparation
-
0.074
Fe(III)-nitrilotriacetic acid[side 2]
-
in 25 mM MOPS, 25 mM MES, 5.4 mM KCl, 5 mM glucose, 140 mM NaCl, 1.8 mM CaCl2, 0.8 mM MgCl2, pH 7.0, at 37°C
0.0921
Fe(III)-nitrilotriacetic acid[side 2]
-
in 25 mM MOPS, 25 mM MES, 5.4 mM KCl, 5 mM glucose, 140 mM NaCl, 1.8 mM CaCl2, 0.8 mM MgCl2, pH 7.0, at 22°C
0.001
ferricytochrome b5
-
pig microsome cytochrome-b5, detergent preparation
0.001
ferricytochrome b5
-
long ferricytochrome b5 from pig microsomes, at pH 6.5 and 30°C
0.0014
ferricytochrome b5
-
rabbit microsome cytochrome-b5, detergent preparation
0.0014
ferricytochrome b5
-
rat microsome cytochrome-b5, detergent preparation
0.0014
ferricytochrome b5
-
long ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C
0.0016
ferricytochrome b5
-
rat microsome cytochrome-b5, trypsin preparation
0.0016
ferricytochrome b5
-
short ferricytochrome b5 from rat microsomes, at pH 6.5 and 30°C
0.0017
ferricytochrome b5
-
short ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C
0.0022
ferricytochrome b5
-
long ferricytochrome b5 from rabbit microsomes, at pH 6.5 and 30°C
0.0027
ferricytochrome b5
-
pig microsome cytochrome-b5, trypsin preparation