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Literature summary for 1.6.2.4 extracted from

  • Campelo, D.; Lautier, T.; Urban, P.; Esteves, F.; Bozonnet, S.; Truan, G.; Kranendonk, M.
    The hinge segment of human NADPH-cytochrome P450 reductase in conformational switching The critical role of ionic strength (2017), Front. Pharmacol., 8, 755 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.6.2.4

Application

Application Comment Organism
analysis 96-well plate format assay to follow cytochrome c reduction Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
G240P mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
I245A mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
I245A/R246A mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
I245P mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
I245R/R246I mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
additional information specific residues of the hinge segment are important in the control of the conformational equilibrium of CPR. Mutations in residues G240, S243, I245 and R246 of the hinge segment, are capable of reducing cytochrome c yet with different efficiency and their maximal rates of cytochrome c reduction are shifted to lower salt concentration. Residue R246 seems to play a key role in a salt bridge network present at the interface of the hinge and the connecting domain Homo sapiens
R246A mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
R246P mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens
S243P mutation in the hinge segment, ionic strength profile is shifted to lower salt concentrations Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Homo sapiens 16020
-
soluble
-
 Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl optimum concentration 0.4-0.6 M, about 4fold activation for substrate ferricytochrome c Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P16435
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADPH + H+
-
 Homo sapiens 2 ferrocyanide + NADP+
-
 ?
2 ferricytochrome c + NADPH + H+
-
 Homo sapiens 2 ferrocytochrome c + NADP+
-
 ?
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
-
 Homo sapiens reduced 2,6-dichlorophenolindophenol + NADP+
-
 ?

Subunits

Subunits Comment Organism
? x * 70000, SDS-PAGE, x * 69000, calculated from sequence Homo sapiens
More specific residues of the hinge segment are important in the control of the conformational equilibrium of CPR Homo sapiens

Synonyms

Synonyms Comment Organism
CPR
-
 Homo sapiens
NP_000932
-
 Homo sapiens
POR
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism salt dependency of either cytochrome c or P450 reductions can be mostly attributed to a change in the conformational equilibrium of CPR. In the membrane bound form of wild-type CPR, the kobs value is lower than the one measured with the soluble form Homo sapiens