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2.5.1.78: 6,7-dimethyl-8-ribityllumazine synthase

This is an abbreviated version!
For detailed information about 6,7-dimethyl-8-ribityllumazine synthase, go to the full flat file.

Word Map on EC 2.5.1.78

Reaction

1-deoxy-L-glycero-tetrulose 4-phosphate
+
5-amino-6-(D-ribitylamino)uracil
=
6,7-dimethyl-8-(D-ribityl)lumazine
+ 2 H2O +
phosphate

Synonyms

6,7-dimethyl-8-(d-ribityl)lumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase 1, 6,7-dimethyl-8-ribityllumazine synthase 2, 6,7-dimethyl-8-ribityllumazine-synthase, AaLS, BLS, DMRL synthase, DMRL synthase 2, heavy riboflavin synthase, LcLS1, LcLS2, lumazine synthase, lumazine synthase 1, lumazine synthase 2, lumazine synthase/riboflavin synthase complex, lumazinesynthase/riboflavin synthase complex, lumazinesynthase/riboflavin synthase complex, icosahedral capsid of 60 beta subunits enclosing a triplet of alpha subunits, luminazine synthase, MbtLS, MJ0303, Pbls, RIB4, ribE, RibH, ribH1, RibH1 protein, RibH2, type I lumazine synthase, type II lumazine synthase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase

Temperature Stability

Temperature Stability on EC 2.5.1.78 - 6,7-dimethyl-8-ribityllumazine synthase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120
-
melting temperature: 119.9°C
20
-
the higher molecular order of the decameric enzyme increases its stability at 20°C compared with pentameric lumazine synthases
50
-
lumazine synthase shows two distinct thermal transitions in phosphate containing buffers. The first transition around 50°C is due to the dissociation of phosphate ions from the protein and is reversible and the second strating from 80°C comes from the dissociation and conformational alteration of its icosahedral structure. The highest Tm values for both transitions are at pH 7.0
80
-
lumazine synthase shows two distinct thermal transitions in phosphate containing buffers. The first transition around 50°C is due to the dissociation of phosphate ions from the protein and is reversible and the second strating from 80°C comes from the dissociation and conformational alteration of its icosahedral structure. The highest Tm values for both transitions are at pH 7.0
88
-
melting temperature. The loss of secondary structure is not recovered after slow cooling of the samples, indicating that an irreversible unfolding takes place under these conditions