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Affinity modification of NADPH-cytochrome P-450 reductase.

Abstract：

:The active centre of NADPH-cytochrome P-450 reductase contains the lysine residue essential for catalytic activity. Chemical modification of epsilon-amino group of this lysine residue is the subject of the present study. To modify the epsilon-amino group, we have employed the periodate-oxidized NADP+ and NAD+ (o-NAD(P]. The both reagents have appeared to be the competitive inhibitors of NADPH-cytochrome P-450 reductase (Ki for o-NADP approximately 10 microM, Ki for o-NAD greater than 100 microM). However, o-NADP has not a covalency bond with reductase, whilst o-NAD modifies the reductase at the binding site of NADPH. A protective effect of NADP+ and the labeling extent close to unity (0.7) at deep reductase inactivation indicate the affinity type of this modification. Different results of reductase modification by either o-NADP or o-NAD may be due to the difference in the structures of the analogs bound to the enzyme active site.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Slepneva IA,Weiner LM

doi

10.1016/s0006-291x(88)80599-0

subject

Has Abstract

pub_date

1988-09-15 00:00:00

pages

1026-32

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80599-0

journal_volume

155

pub_type

杂志文章

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