Literature summary for 1.6.2.4 extracted from

Xia, C.; Shen, A.L.; Duangkaew, P.; Kotewong, R.; Rongnoparut, P.; Feix, J.; Kim, J.P.
Structural and functional studies of the membrane-binding domain of NADPH-cytochrome P450 oxidoreductase (2019), Biochemistry, 58, 2408-2418 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	replacement of all seven cysteine residues, no gross effect is observed on FMN and FAD binding and electron transfer from NADPH. Cytochrome c reduction is decreased to 2% of wild-type. Introduction of Cys residues S9C, S32C, S55C, T668C to the Cys-less mutant shows substantial conformational changes upon membrane reconstitution of mutant, while liposome insertion has little effect on the T668C	Homo sapiens
additional information	the deletion of more than 29 residues from the N-terminus of CYPOR decreases cytochrome P450 activity concomitant with alterations in electrophoretic mobility and an increased resistance to protease digestion. The altered kinetic properties of these mutants are consistent with electron transfer through random collisions rather than via formation of a stable CYPOR-P450 complex	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P16435	-	-

Subunits

Subunits	Comment	Organism
?	x * 77200, SDS-PAGE	Homo sapiens

Synonyms

Synonyms	Comment	Organism
CYPOR	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
FAD	after replacement of all seven cysteine residues, no gross effect is observed on FMN and FAD binding and electron transfer from NADPH	Homo sapiens
FMN	after replacement of all seven cysteine residues, no gross effect is observed on FMN and FAD binding and electron transfer from NADPH	Homo sapiens

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Release 2023.1 (January 2023)