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
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2.5.1.9
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6,7-dimethyl-8-ribityllumazine
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cyclohydrolase
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5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
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dismutation
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guilliermondii
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3,4-dihydroxy-2-butanone
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icosahedral
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bartonellae
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photobacterium
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flavinogenic
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flavinogenesis
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ashbyii
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eremothecium
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ribitylated
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leiognathi
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henselae
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famata
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drug development
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pharmacology
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medicine
- 2.5.1.9
- 6,7-dimethyl-8-ribityllumazine
-
cyclohydrolase
-
5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
-
dismutation
- guilliermondii
- 3,4-dihydroxy-2-butanone
-
icosahedral
-
bartonellae
- photobacterium
-
flavinogenic
-
flavinogenesis
-
ashbyii
- eremothecium
-
ribitylated
- leiognathi
- henselae
- famata
- drug development
- pharmacology
- medicine
Reaction
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = +
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
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Engineering
Engineering on EC 2.5.1.9 - riboflavin synthase
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DELTA1-180
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variant that lacks the C-terminal extension the coiled-coil and C-terminal peptide (AaRS1-180)
DELTA1-196
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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
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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
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the mutant enzyme is taken up by lumazine synthase only 30% less efficiently than wild-type enzyme
A43L
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decrease in affinity for substrate 6,7-dimethyl-8-ribityllumazine. A43L replacement causes substantial perturbation of the overall binding site topology
C48S
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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
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site-directed mutagenesis, soluble protein, too unstable to be purified
D143N
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site-directed mutagenesis, soluble protein, too unstable to be purified
F2A
H102Q
N181G
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site-directed mutagenesis, soluble protein, too unstable to be purified
S41A
T3R
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site-directed mutagenesis, slightly reduced activity, low expression rate
T50A
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production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude
T67A
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production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude
Y133A
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site-directed mutagenesis, soluble protein, too unstable to be purified
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
F2A
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nearly inactive mutant, comparison of kinetics for wild-type and mutant enzymes
H102Q
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highly reduced activity compared to the wild-type enzyme, comparison of kinetics for wild-type and mutant enzymes
S41A
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site-directed mutagenesis, mutant produces a dimeric pentacyclic reaction intermediate, i.e. compound Q, which can be cleaved in 2 different ways by the enzyme
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recombinant sequence segment 1-97 forms a homodimer that can bind riboflavin, 6,7-dimethyl-8-ribityllumazine, and trifluoromethyl-substituted 8-ribityllumazine derivatives, and is required for ligand binding, recombinant sequence segment 101-213 is unstable and only partially involved in riboflavin binding
additional information
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5 mutants genes cannot be expressed recombinantly in Escherichia coli: C48S, T50R, T67R, T148R, T165R
additional information
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a F2DELTA deletion mutant construct has no remaining activity
additional information
overexpression in Escherichia coli can suppress the lack of pyrimidine deaminase/reductase in a riboflavin-deficient ribD- strain
additional information
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overexpression in Escherichia coli can suppress the lack of pyrimidine deaminase/reductase in a riboflavin-deficient ribD- strain