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InterPro: IPR002180 6,7-dimethyl-8-ribityllumazine synthase
Protein matches
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UniProtKB Matches: 1761 proteins |
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Accession
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IPR002180 DMRL_synthase |
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Type
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Signatures
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InterPro Relationships
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Children
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IPR006399 Riboflavin synthase, archaeal
IPR017420 6,7-dimethyl-8-ribityllumazine synthase, chloroplast
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GO Term annotation
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Process
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GO:0009231 riboflavin biosynthetic process
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Component
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GO:0009349 riboflavin synthase complex
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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6,7-dimethyl-8-ribityllumazine synthase (riboflavin synthase) catalyses the biosynthesis of riboflavin according to the reaction: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine .
The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules of ribulose 5-phosphate as substrates. The final step in the biosynthesis of the vitamin involves the dismutation of 6,7-dimethyl-8-ribityllumazine catalyzed by riboflavin synthase. 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 [1]. N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives inhibit riboflavin synthase [2].
This family includes the beta chain of 6,7-dimethyl-8-ribityllumazine synthase EC:2.5.1.9. The family also includes a subfamily of distant archaebacterial proteins that may also have the same function for example O28856.
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Structural links
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Database links
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Publications
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1.
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Fischer M, Bacher A.
Biosynthesis of vitamin B2: Structure and mechanism of riboflavin synthase.
Arch. Biochem. Biophys. 474 252-65 2008
[PubMed: 18298940]
http://dx.doi.org/10.1016/j.abb.2008.02.008
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2.
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Zhang Y, Illarionov B, Morgunova E, Jin G, Bacher A, Fischer M, Ladenstein R, Cushman M.
A new series of N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives as inhibitors of lumazine synthase and riboflavin synthase: design, synthesis, biochemical evaluation, crystallography, and mechanistic implications.
J. Org. Chem. 73 2715-24 2008
[PubMed: 18331058]
http://dx.doi.org/10.1021/jo702631a
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Additional Reading
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Klinke S, Zylberman V, Vega DR, Guimaraes BG, Braden BC, Goldbaum FA.
Crystallographic studies on decameric Brucella spp. Lumazine synthase: a novel quaternary arrangement evolved for a new function?
J. Mol. Biol. 353 2005 124-37
[PubMed: 16165152]
http://dx.doi.org/10.1016/j.jmb.2005.08.017
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Klinke S, Zylberman V, Bonomi HR, Haase I, Guimaraes BG, Braden BC, Bacher A, Fischer M, Goldbaum FA.
Structural and kinetic properties of lumazine synthase isoenzymes in the order Rhizobiales.
J. Mol. Biol. 373 2007 664-80
[PubMed: 17854827]
http://dx.doi.org/10.1016/j.jmb.2007.08.021
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Morgunova E, Illarionov B, Sambaiah T, Haase I, Bacher A, Cushman M, Fischer M, Ladenstein R.
Structural and thermodynamic insights into the binding mode of five novel inhibitors of lumazine synthase from Mycobacterium tuberculosis.
FEBS J. 273 2006 4790-804
[PubMed: 16984393]
http://dx.doi.org/10.1111/j.1742-4658.2006.05481.x
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Morgunova E, Meining W, Illarionov B, Haase I, Jin G, Bacher A, Cushman M, Fischer M, Ladenstein R.
Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: binding mode of a new class of purinetrione inhibitors.
Biochemistry 44 2005 2746-58
[PubMed: 15723519]
http://dx.doi.org/10.1021/bi047848a
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InterPro 23.1
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