4.1.99.12: 3,4-dihydroxy-2-butanone-4-phosphate synthase
This is an abbreviated version!
For detailed information about 3,4-dihydroxy-2-butanone-4-phosphate synthase, go to the full flat file.
Word Map on EC 4.1.99.12
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4.1.99.12
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disinfection
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trihalomethanes
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haloacetic
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brominate
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halogen
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haloacetonitriles
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chloramination
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bromide
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genotoxicity
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chloroform
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effluent
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wastewater
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iodin
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ozone
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swimming
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humic
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unregulated
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trichloronitromethane
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n-nitrosodimethylamine
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carbonaceous
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chloral
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speciation
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dichloroacetic
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dichloroacetonitrile
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monochloramine
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haloketones
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bromodichloromethane
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swimmers
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fulvic
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hypochlorite
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non-regulated
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micropollutants
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clo2
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pilot-scale
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n-nitrosamines
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naclo
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excitation-emission
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bromoacetic
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chlorite
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ballast
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shower
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acid-like
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pipe
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potable
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suwannee
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drug development
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synthesis
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nanofiltration
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biofiltration
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bromoform
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indoor
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iodate
- 4.1.99.12
-
disinfection
-
trihalomethanes
-
haloacetic
-
brominate
-
halogen
-
haloacetonitriles
-
chloramination
- bromide
-
genotoxicity
- chloroform
-
effluent
-
wastewater
-
iodin
- ozone
-
swimming
-
humic
-
unregulated
-
trichloronitromethane
- n-nitrosodimethylamine
-
carbonaceous
- chloral
-
speciation
-
dichloroacetic
-
dichloroacetonitrile
- monochloramine
- haloketones
-
bromodichloromethane
-
swimmers
-
fulvic
-
hypochlorite
-
non-regulated
-
micropollutants
- clo2
-
pilot-scale
-
n-nitrosamines
- naclo
-
excitation-emission
-
bromoacetic
- chlorite
-
ballast
-
shower
-
acid-like
- pipe
-
potable
-
suwannee
- drug development
- synthesis
-
nanofiltration
-
biofiltration
- bromoform
-
indoor
- iodate
Reaction
Synonyms
3,4-dihydroxy 2-butanone-4-phosphate synthase, 3,4-dihydroxy-2-butanone 4-phosphate synthase, 3,4-dihydroxy-2-butanone-4-phosphate synthase, AtRIBA1, AtRIBA2, bifunctional GCHYII/DHBP, bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase, DBPS, DHBP synthase, DHBPS, DHBPS/GCHII, dihydroxybutanone phosphate synthase, L-3,4-dihydroxy-2-butanone 4-phosphate synthase, L-3,4-dihydroxy-2-butanone-4-phosphate synthase, LcRIBA, More, Mtb-DHBPS, Mtb-ribA2, NbRibA, Rib3, ribA, ribA2, ribB, Sp0176, vDHBPS, vribB
ECTree
4.1.99.12 3,4-dihydroxy-2-butanone-4-phosphate synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.1.99.12 - 3,4-dihydroxy-2-butanone-4-phosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C59A
site-directed mutagenesis, the mutant shows 70% of wild-type enzyme activity
Q181R/Q183R
site-directed mutagenesis, construction of a synthetic gene, derived from orf 6.2440, with nucleotide exchanges at positions 414, 426, 477, 480, and 581
Y87A
site-directed mutagenesis, the mutant shows 2% of wild-type enzyme activity
H147S
A137T
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naturally occuring Rib3 mutant which is partially deficient in cytochromes a, a3, and cytochrome b, the respiratory defect elicited by this mutation cannot be explained by a flavin insufficiency based on the following evidence: 1. growth of the aE280/U1 on respiratory substrates is not rescued by exogenous riboflavin, 2. the levels of flavin nucleotides are not significantly different in the mutant and wild type, phenotype, overview
D32A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E163A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E30A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H125A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H142A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T143A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T96A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D32A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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E163A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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E30A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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H125A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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H142A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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E41A
site-directed mutagenesis, the mutant is almost inactive
F139A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
M84A
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
N89A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
R61A
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
S64A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V98A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
E39A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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site-directed mutagenesis, inactive mutant
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F139A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
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H154A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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site-directed mutagenesis, inactive mutant
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N89A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
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S64A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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additional information
H147S
site-directed mutagenesis, the mutant enzyme shows about 10% of the wild-type enzyme activity
H147S
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site-directed mutagenesis, the mutant shows about 10% of wild-type enzyme activity, crystal structure determination with bound substrate
additional information
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an additional single copy of the ribA gene introduced into the sacBlocus of the riboflavin production strain and constitutive expression from the medium strength vegI promoter leads to improved riboflavin titers and yields of riboflavin on glucose of up to 25%, strain VB2XL1, both enzymatic activities of RibA, the 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and the GTP cyclohydrolase II activity of the C-terminal domain, are necessary for the improved riboflavin productivity, method, overview
additional information
engineering of Escherichia coli for increased riboflavin production: overexpression of gene ribB to increase the flux from ribulose 5-phosphate to 3,4-dihydroxybutan-2-one 4-phosphate. Then ndk and gmk genes are overexpressed to enhance GTP supply. Subsequently, a R419L mutation is introduced into purA to reduce the flux from IMP to AMP. Co-overexpression of mutant purF and prs genes further increased riboflavin production. The final strain RF18S produces 387.6 mg riboflavin per liter with a yield of 44.8 mg riboflavin per gram glucose in shake-flask fermentations. The final titer and yield are 72.2% and 55.6%. Mutant strain and method evaluation, overview
additional information
Escherichia coli K-12 / MG1655
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engineering of Escherichia coli for increased riboflavin production: overexpression of gene ribB to increase the flux from ribulose 5-phosphate to 3,4-dihydroxybutan-2-one 4-phosphate. Then ndk and gmk genes are overexpressed to enhance GTP supply. Subsequently, a R419L mutation is introduced into purA to reduce the flux from IMP to AMP. Co-overexpression of mutant purF and prs genes further increased riboflavin production. The final strain RF18S produces 387.6 mg riboflavin per liter with a yield of 44.8 mg riboflavin per gram glucose in shake-flask fermentations. The final titer and yield are 72.2% and 55.6%. Mutant strain and method evaluation, overview
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additional information
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construction of RIB3 disruption mutants, restoration by riboflavin of growth of a rib3 deletion mutant on glucose but not glycerol/ethanol, phenotype, overview
