Biosynthesis of vitamin B2: Structure and mechanism of riboflavin synthase.

Abstract:

:The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules of ribulose 5-phosphate as substrates. GTP is hydrolytically opened, converted into 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione by a sequence of deamination, side chain reduction and dephosphorylation. Condensation with 3,4-dihydroxy-2-butanone 4-phosphate obtained from ribulose 5-phosphate leads to 6,7-dimethyl-8-ribityllumazine. The final step in the biosynthesis of the vitamin involves the dismutation of 6,7-dimethyl-8-ribityllumazine catalyzed by riboflavin synthase. The mechanistically unusual reaction involves the transfer of a four-carbon fragment between two identical substrate molecules. The second product, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, is recycled in the biosynthetic pathway by 6,7-dimethyl-8-ribityllumazine synthase. This article will review structures and reaction mechanisms of riboflavin synthases and related proteins up to 2007 and 122 references are cited.

journal_name

Arch Biochem Biophys

authors

Fischer M,Bacher A

doi

10.1016/j.abb.2008.02.008

subject

Has Abstract

pub_date

2008-06-15 00:00:00

pages

252-65

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(08)00070-2

journal_volume

474

pub_type

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