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Interaction between cytochrome P450 2B1 and cytochrome bs: inhibition by synthetic peptides indicates a role for P450 residues Lys-122 and Arg-125.

Abstract：

:Binding of cytochrome b5 to rat cytochrome P450 2B1 was inhibited (by 75%) by a synthetic peptide corresponding to P450 residues 116-134. The role of Lys-122 and Arg-125 were evaluated using peptides in which one or both of these basic residues were replaced with Glu. The Lys-122 substitution nearly abolished while the Arg-125 replacement decreased (by 20%) the inhibitory potential of the peptide. Substitution of both residues resulted in a peptide with no inhibitory activity. These results thus indicate a role for a specific P450 region as well as two basic residues within this region in the cytochrome P450-cytochrome b5 interaction.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Omata Y,Sakamoto H,Robinson RC,Pincus MR,Friedman FK

doi

10.1006/bbrc.1994.1817

subject

Has Abstract

pub_date

1994-06-30 00:00:00

pages

1090-5

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X84718171

journal_volume

201

pub_type

杂志文章

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