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Information on EC 1.16.1.2 - diferric-transferrin reductase
for references in articles please use BRENDA:EC1.16.1.2
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EC Tree 1 Oxidoreductases
1.16 Oxidizing metal ions
1.16.1 With NAD+ or NADP+ as acceptor
1.16.1.2 diferric-transferrin reductase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.16.1.2
- ferricyanide
-
transplasma
-
transplasmalemma
- adriamycin
- malaria
- erythrocyte
-
retinyl
- bathophenanthroline
-
ferrous
-
retinoic
showSynonyms
nadh diferric transferrin reductase, diferric transferrin reductase, transferrin reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diferric transferrin reductase
-
-
-
-
NADH diferric transferrin reductase
-
-
-
-
transferrin reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
transferrin[Fe(II)]2 + NAD+ + H+ = transferrin[Fe(III)]2 + NADH
amino acid composition
-
transferrin[Fe(II)]2 + NAD+ + H+ = transferrin[Fe(III)]2 + NADH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
transferrin[Fe(II)]2:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
105238-49-1
-
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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
ferric ammonium citrate + NADH
ferrous ammonium citrate + NAD+
-
Substrates: -
Products: -
Products: -
?
transferrin[Fe(II)]2 + NAD+ + H+
transferrin[Fe(III)]2 + NADH
-
Substrates: -
Products: -
Products: -
r
ferritin[Fe(III)] + NADH
ferritin[Fe(II)] + NAD+
-
Substrates: -
Products: -
Products: -
?
ferritin[Fe(III)] + NADH
ferritin[Fe(II)] + NAD+
-
Substrates: -
Products: -
Products: -
?
ferritin[Fe(III)] + NADH
ferritin[Fe(II)] + NAD+
-
Substrates: -
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: -
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: -
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: -
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: enzyme of the malaria parasite Plasmodium falciparum together with parasite-derived transferrin receptor in the erythrocyte membrane forms a transferrin receptor-mediated uptake mechanism of iron
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: -
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: reduction of diferric transferrin at the cell surface may be an important function for diferric transferrin in stimulation of cell growth
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: role in iron transport
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
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: enzyme of the malaria parasite Plasmodium falciparum together with parasite-derived transferrin receptor in the erythrocyte membrane forms a transferrin receptor-mediated uptake mechanism of iron
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: reduction of diferric transferrin at the cell surface may be an important function for diferric transferrin in stimulation of cell growth
Products: -
Products: -
?
transferrin[Fe(III)]2 + NADH
transferrin[Fe(II)]2 + NAD+
-
Substrates: role in iron transport
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
dependent on, highest activity at about 0.1 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
potassium phosphate buffer leads to a slightly higher activity than sodium phosphate buffer
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
retinol and retinyl acetate have very little inhibitory effect
-
additional information
-
sensitive to proteinase K treatment
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
-
detergent, activates
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH 7.0: about 40% of activity maximum, pH 10.0: about 35% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
malaria parasite, erythrocytes infected with Plasmodium falciparum
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
infected with Plasmodium falciparum, synthesis of the enzyme by the intraerythrocytic parasite
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
erythrocytes infected with Plasmodium falciparum, synthesis and incorporation of the enzyme by the intraerythrocytic parasite
-
brenda
additional information
-
enzyme is found intracellular in Mycobacterium paratuberculosis infected bovine gut tissue
-
brenda
additional information
-
low activity in the membranes of Golgi apparatus, endoplasmic reticulum and mitochondria, about 10% of the activity in the plasma membrane
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fry, M.
Diferric transferrin reductase in Plasmodium falciparum-infected erythrocytes
Biochem. Biophys. Res. Commun.
158
469-473
1989
Plasmodium falciparum
brenda
Sun, I.L.; Navas, P.; Crane, F.L.; Morre, D.J.; Lw, H.
NADH diferric transferrin reductase in liver plasma membrane
J. Biol. Chem.
262
15915-15921
1987
Rattus norvegicus
brenda
Sun, I.L.; Toole-Simms, W.; Crane, F.L.; Golub, E.S.; Diaz de Pagan, T.; Morre, D.J.; Lw, H.
Retinoic acid inhibition of transplasmalemma diferric transferrin reductase
Biochem. Biophys. Res. Commun.
146
976-982
1987
Homo sapiens, Rattus norvegicus
brenda
Homuth, M.; Valentin-Weigand, P.; Rohde, M.; Gerlach, G.F.
Identification and characterization of a novel extracellular ferric reductase from Mycobacterium paratuberculosis
Infect. Immun.
66
710-716
1998
Mycobacterium avium subsp. paratuberculosis
brenda
EXTERNAL LINKS (specific for EC-Number 1.16.1.2)
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Release 2023.1 (January 2023)
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