2',3'-Dialdehydo-UDP-N-acetylglucosamine inhibits UDP-N-acetylglucosamine 2-epimerase, the key enzyme of sialic acid biosynthesis.

Abstract:

:Sialic acids comprise a family of terminal sugars essential for a variety of biological recognition systems. UDP-N-acetylglucosamine 2-epimerase catalyzes the first step of their biosynthesis. Periodate-oxidized UDP-N-acetylglucosamine, namely 2',3'-dialdehydo-UDP-alpha-D-N-acetylglucosamine, was found to be an effective inhibitor of this enzyme, compared with the periodate oxidation products of compounds such as UDP, uridine or methyl riboside. It bound covalently to amino acids in the active site causing an irreversible inhibition. This compound may therefore represent a basis for the synthesis of potent inhibitors of UDP-N-acetylglucosamine 2-epimerase and, as a consequence, of the biosynthesis of sialic acids.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Blume A,Chen H,Reutter W,Schmidt RR,Hinderlich S

doi

10.1016/s0014-5793(02)02856-9

keywords:

subject

Has Abstract

pub_date

2002-06-19 00:00:00

pages

127-32

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302028569

journal_volume

521

pub_type

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