Genistein inhibits activities of methylenetetrahydrofolate reductase and lactate dehydrogenase, enzymes which use NADH as a substrate.

Abstract:

:Genistein (5, 7-dihydroxy-3- (4-hydroxyphenyl)-4H-1-benzopyran-4-one) is a natural isoflavone revealing many biological activities. Thus, it is considered as a therapeutic compound in as various disorders as cancer, infections and genetic diseases. Here, we demonstrate for the first time that genistein inhibits activities of bacterial methylenetetrahydrofolate reductase (MetF) and lactate dehydrogenase (LDH). Both enzymes use NADH as a substrate, and results of biochemical as well as molecular modeling studies with MetF suggest that genistein may interfere with binding of this dinucleotide to the enzyme. These results have implications for our understanding of biological functions of genistein and its effects on cellular metabolism.

authors

Grabowski M,Banecki B,Kadziński L,Jakóbkiewicz-Banecka J,Kaźmierkiewicz R,Gabig-Cimińska M,Węgrzyn G,Węgrzyn A,Banecka-Majkutewicz Z

doi

10.1016/j.bbrc.2015.08.004

subject

Has Abstract

pub_date

2015-09-25 00:00:00

pages

363-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(15)30394-6

journal_volume

465

pub_type

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