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
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General Information
General Information on EC 4.1.99.12 - 3,4-dihydroxy-2-butanone-4-phosphate synthase
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evolution
malfunction
metabolism
physiological function
additional information
angiosperms share a small RIBA gene family consisting of three members. The monofunctional, bipartite RIBA3 proteins AtRIBA2, and AtRIBA3, which have lost DHBPS activity, evolved early in tracheophyte evolution, phylogenetic analysis, overview. While AtRIBA2 is lacking GCHII activity, AtRIBA3 does not display DHBPS function
evolution
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angiosperms share a small RIBA gene family consisting of three members. The monofunctional, bipartite RIBA3 proteins AtRIBA2, and AtRIBA3, which have lost DHBPS activity, evolved early in tracheophyte evolution, phylogenetic analysis, overview. While AtRIBA2 is lacking GCHII activity, AtRIBA3 does not display DHBPS function
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silencing NbRibA compromises hypersensitive response cell death, NO and ROS production, and induced high susceptibility to oomycete Phytophthora infestans and ascomycete Colletotrichum orbiculare. Compromised radical production and hypersensitive response cell death induced by INF1 in NbRibA-silenced leaves is rescued by adding riboflavin, FMN or FAD
malfunction
bleaching leaf phenotype of RIBA1 deficient plants, overview. The bleaching phenotype of the seedlings is not counterbalanced by the simultaneous AtRIBA2 and AtRIBA3 expression
malfunction
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bleaching leaf phenotype of RIBA1 deficient plants, overview. The bleaching phenotype of the seedlings is not counterbalanced by the simultaneous AtRIBA2 and AtRIBA3 expression
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3,4-dihydroxy-2-butanone-4-phosphate synthase is one of the key enzymes in the biosynthesis of riboflavin
metabolism
the enzyme is involved in biosynthesis of riboflavin, overview. Riboflavin is the precursor for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential cofactors for numerous enzymes (e.g., dehydrogenases, oxidases, reductases)
metabolism
the bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase (LcRIBA) catalyzes 2 initial reactions in riboflavin biosynthetic pathway
metabolism
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3,4-dihydroxy-2-butanone-4-phosphate synthase is one of the key enzymes in the biosynthesis of riboflavin
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metabolism
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the enzyme is involved in biosynthesis of riboflavin, overview. Riboflavin is the precursor for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential cofactors for numerous enzymes (e.g., dehydrogenases, oxidases, reductases)
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the enzyme is involved in riboflavin biosynthesis. Up-regulation of DHBP synthase is evidenced as one of the first line strategies to cope with imbalance of energy production and vital adaptation
physiological function
isozyme AtRIBA1 is required for pigmentation of the rosettes leaves
physiological function
3,4-dihydroxy-2-butanone 4-phosphate (DHBP) and GTP are the precursors for riboflavin biosynthesis
physiological function
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3,4-dihydroxy-2-butanone 4-phosphate synthase is associated with riboflavin biosynthesis. The enzyme belongs to the proteins of great potential as Fusarium oxysporum f. sp. fragariae (Fof) virulence factors
physiological function
enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase (DHBPS) catalyzes one of the two committed steps in the riboflavin pathway and converts D-ribulose 5-phosphate (Ru5P) to L-3,4-dihydroxy-2-butanone 4-phosphate and formate
physiological function
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isozyme AtRIBA1 is required for pigmentation of the rosettes leaves
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physiological function
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase (DHBPS) catalyzes one of the two committed steps in the riboflavin pathway and converts D-ribulose 5-phosphate (Ru5P) to L-3,4-dihydroxy-2-butanone 4-phosphate and formate
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physiological function
Escherichia coli K-12 / MG1655
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3,4-dihydroxy-2-butanone 4-phosphate (DHBP) and GTP are the precursors for riboflavin biosynthesis
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physiological function
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the enzyme is involved in riboflavin biosynthesis. Up-regulation of DHBP synthase is evidenced as one of the first line strategies to cope with imbalance of energy production and vital adaptation
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an essential bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (DHBPS/GCHII) enzyme from Mycobacterium tuberculosis, Mtb-ribA2. The enzyme is composed of two conformationally different molecules of Mtb-ribA2 in the asymmetric unit that form a dimer via their GCHII domains. DHBPS and GCHII functional homodimers form a long helical-like oligomer, but the enzyme exists as a dimer in solution. The DHBPS subunit possesses an active-site loop1, a substrate channelling loop2, and a pH-sensitive loop3, structure comparisons, overview
additional information
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an essential bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (DHBPS/GCHII) enzyme from Mycobacterium tuberculosis, Mtb-ribA2. The enzyme is composed of two conformationally different molecules of Mtb-ribA2 in the asymmetric unit that form a dimer via their GCHII domains. DHBPS and GCHII functional homodimers form a long helical-like oligomer, but the enzyme exists as a dimer in solution. The DHBPS subunit possesses an active-site loop1, a substrate channelling loop2, and a pH-sensitive loop3, structure comparisons, overview
additional information
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
additional information
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
additional information
the two key enzymes of the riboflavin biosynthetic pathway, DHBPS and GTP cyclohydrolaseII (GCHII), EC 3.5.4.25,are fused together into the bifunctional enzyme encoded by Sp0176 gene of Streptococcus pneumoniae strain TIGR 4, DHBPS active site architecture, overview
additional information
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the two key enzymes of the riboflavin biosynthetic pathway, DHBPS and GTP cyclohydrolaseII (GCHII), EC 3.5.4.25,are fused together into the bifunctional enzyme encoded by Sp0176 gene of Streptococcus pneumoniae strain TIGR 4, DHBPS active site architecture, overview
additional information
DHBPS enzyme structure comparisons, active site architecture of enzyme vDHBPS
additional information
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the two key enzymes of the riboflavin biosynthetic pathway, DHBPS and GTP cyclohydrolaseII (GCHII), EC 3.5.4.25,are fused together into the bifunctional enzyme encoded by Sp0176 gene of Streptococcus pneumoniae strain TIGR 4, DHBPS active site architecture, overview
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additional information
Mycobacterium tuberculosis H37Ra / ATCC 25177
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an essential bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (DHBPS/GCHII) enzyme from Mycobacterium tuberculosis, Mtb-ribA2. The enzyme is composed of two conformationally different molecules of Mtb-ribA2 in the asymmetric unit that form a dimer via their GCHII domains. DHBPS and GCHII functional homodimers form a long helical-like oligomer, but the enzyme exists as a dimer in solution. The DHBPS subunit possesses an active-site loop1, a substrate channelling loop2, and a pH-sensitive loop3, structure comparisons, overview
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additional information
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in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
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additional information
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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DHBPS enzyme structure comparisons, active site architecture of enzyme vDHBPS
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