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2.5.1.9: riboflavin synthase

This is an abbreviated version!
For detailed information about riboflavin synthase, go to the full flat file.

Word Map on EC 2.5.1.9

Reaction

2 6,7-dimethyl-8-(1-D-ribityl)lumazine =

riboflavin
+
4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine

Synonyms

heavy riboflavin synthase, light riboflavin synthase, lumazine synthase/riboflavin synthase complex, RibD, RibE1, riboflavin synthase, riboflavin synthetase, riboflavine synthase, riboflavine synthetase, synthase, riboflavin

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)
                2.5.1.9 riboflavin synthase

Engineering

Engineering on EC 2.5.1.9 - riboflavin synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1-180
-
variant that lacks the C-terminal extension the coiled-coil and C-terminal peptide (AaRS1-180)
DELTA1-196
-
variant that lacks the C-terminal extension (1-196). Substantial decrease in association efficiency with lumazine synthase is observed for the truncated variant
DELTA180-196
-
variant that lacks the C-terminal extension the coiled-coil segment (DELTA180-196). The mutant enzyme associated with lumazine synthase to an about 3fold higher extent than the full-length riboflavin synthase
W207A
-
the mutant enzyme is taken up by lumazine synthase only 30% less efficiently than wild-type enzyme
A43L
-
decrease in affinity for substrate 6,7-dimethyl-8-ribityllumazine. A43L replacement causes substantial perturbation of the overall binding site topology
C48S
-
mutation in the activity cavity, causes significant 19F NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein. Replacement of C48 changes the electron density topology in the N-terminal substrate binding site in the vicinity of C-6 and C-7 atoms of bound ligand
D143G
-
site-directed mutagenesis, soluble protein, too unstable to be purified
D143N
-
site-directed mutagenesis, soluble protein, too unstable to be purified
D185L
-
site-directed mutagenesis, low remaining activity
E183G
-
site-directed mutagenesis, reduced activity
E66G
-
site-directed mutagenesis, low remaining activity
E85G
-
site-directed mutagenesis, reduced activity
F2Y
-
site-directed mutagenesis, very low remaining activity
H102Q
H97Q
-
site-directed mutagenesis, low remaining activity
K137A
-
site-directed mutagenesis, low remaining activity
N181G
-
site-directed mutagenesis, soluble protein, too unstable to be purified
N45G
-
site-directed mutagenesis, slightly reduced activity
N83G
-
site-directed mutagenesis, reduced activity
S146G
-
site-directed mutagenesis, low remaining activity
T3R
-
site-directed mutagenesis, slightly reduced activity, low expression rate
T50A
-
production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude
T67A
-
production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude
T71A
-
site-directed mutagenesis, slightly reduced activity
Y133A
-
site-directed mutagenesis, soluble protein, too unstable to be purified
C48A
site-directed mutagenesis, nearly inactive mutant
C48M
site-directed mutagenesis, nearly inactive mutant
C48S
site-directed mutagenesis, highly decreased activity compared to the wild-type enzyme
S146A
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
S146C
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
additional information