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D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
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D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
reaction mechanism
-
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
catalytic mechanism
-
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
catalytic mechanism
-
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
catalytic mechanism
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
active site and reaction mechanism, structure-function relationship, structural coordination spheres are important, residues of the first coordination sphere involved in metal binding are indispensable for catalytic activity, Glu185 is essential for catalytic activity
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
active site architecture
-
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
active site structure and catalytic mechanism, modeling of the substrate ribulose 5-phosphate bound in the active site with the phosphate group anchored at the sulfate site and the placement of the ribulose group guided by the glycerol site, the catalytic reaction involves residues Asp41, Cys66, and Glu174, and the Asp99-His136 dyad
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D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
catalytic reaction mechanism, substrate recognition and active site structure, active site consists of three glutamates, two aspartates, two histidines, and a cysteine which may provide the means for general acid and base catalysis and for coordinating the Mg2+ cofactor within the active site
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
reaction mechanism involving intramolecular skeletal rearrangement, a cluster of charged amino acid residues comprising Arg25, Glu26 and Glu28, Asp21 and Asp30 is essential for catalytic activity, as well as His164 and Glu185
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D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
reaction mechanism, the enzyme possesses an essential acidic active-site loop
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
RibA is a bifunctional enzyme possessing 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and GTP cyclohydrolase II activity, EC 3.5.4.25, of the C-terminal domain, overview
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D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
reaction mechanism, detailed overview
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate
reaction mechanism, detailed overview
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
additional information
?
-
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
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-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
rate-limiting step in riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is involved in riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
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-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
step in biosynthesis of vitamin B2, riboflavin
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the enzyme is important in riboflavin biosynthesis, overview
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the enzyme is involved in the pathway of riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is involved in the pathway of riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is involved in the pathway of riboflavin biosynthesis, overview
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
substrate preparation, overview
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is important in the riboflavin biosynthesis, the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, is formed by condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione (1) with 3,4-dihydroxy-2-butanone 4-phosphate, overview
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
step in biosynthesis of vitamin B2, riboflavin
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
DHBPS supplies the building blocks for the assembly of the xylene ring of the vitamin B2, riboflavin, all eight C atoms of the xylene moiety are derived from the product of the enzyme
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
step in the biosynthesis of riboflavin, vitamin B2, ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the enzyme is involved in the pathway of riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
a dimetal center is involved in substrate binding, structure-function relationship, overview
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
substrate binding structure involving a dimetal center, overview
the enzyme converts ribulose 5-phosphate into 3,4-dihydroxy-2-butanone 4-phosphate, while its C4 atom is released as formate
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the reaction involves an intramolecular skeletal rearrangement, NMR study
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
product identification by NMR and CD spectroscopy
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X, analysis of the riboflavin biosynthetic pathway, overview
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
carbon atoms 1-3 of the enzyme product correspond to carbon atoms 1-3 of the substrate, whereas C-4 of the product stems from C-6 of the substrate. Carbon atom 4 of the substrate is released as formate together with the hydrogen atom attached to it. The skeletal rearrangement which leads to the loss of C-4 and the direct linkage between C-3 and C-6 of the substrate is an intramolecular reaction, the hydrogen atom at C-3 of the enzyme product is introduced from solvent water
product identification by GC-MS
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
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-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
isozyme AtRIBA1
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
isozyme AtRIBA2
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
isozyme AtRIBA1
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
isozyme AtRIBA2
-
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?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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-
-
?
additional information
?
-
-
RibA is the rate limiting enzyme in an industrial riboflavin producing strain
-
-
?
additional information
?
-
-
RibA is a bifunctional enzyme possessing 3,4-dihydroxy-2-butanone 4-phosphate synthase activity located in the N-terminal half of the protein and GTP cyclohydrolase II activity, EC 3.5.4.25, of the C-terminal domain, overview
-
-
?
additional information
?
-
-
the position of the metal cofactors and the substrates phosphate group are further stabilized by an extensive hydrogen-bond and salt-bridge network, overview
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?
additional information
?
-
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the enzyme is involved in the riboflavin biosynthetic pathway, but has a second unrelated function in expression of mitochondrial respiration
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?
additional information
?
-
substrate binding structures, overview
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-
?
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
substrate binding structures, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
additional information
?
-
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
rate-limiting step in riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is involved in riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
step in biosynthesis of vitamin B2, riboflavin
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the enzyme is important in riboflavin biosynthesis, overview
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the enzyme is involved in the pathway of riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is involved in the pathway of riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is involved in the pathway of riboflavin biosynthesis, overview
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
the enzyme is important in the riboflavin biosynthesis, the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, is formed by condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione (1) with 3,4-dihydroxy-2-butanone 4-phosphate, overview
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
step in biosynthesis of vitamin B2, riboflavin
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
DHBPS supplies the building blocks for the assembly of the xylene ring of the vitamin B2, riboflavin, all eight C atoms of the xylene moiety are derived from the product of the enzyme
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
step in the biosynthesis of riboflavin, vitamin B2, ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
the enzyme is involved in the pathway of riboflavin biosynthesis
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
a step in the formation of the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione requiring a phosphorylated 4-carbon intermediate, designated as compound X, analysis of the riboflavin biosynthetic pathway, overview
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
-
-
?
additional information
?
-
-
RibA is the rate limiting enzyme in an industrial riboflavin producing strain
-
-
?
additional information
?
-
-
the enzyme is involved in the riboflavin biosynthetic pathway, but has a second unrelated function in expression of mitochondrial respiration
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abortion, Spontaneous
Chlorination disinfection byproducts in water and their association with adverse reproductive outcomes: a review.
Abortion, Spontaneous
DBPs not associated with miscarriage.
Abortion, Spontaneous
Identification of developmentally toxic drinking water disinfection byproducts and evaluation of data relevant to mode of action.
Abortion, Spontaneous
The DBP exposome: Development of a new method to simultaneously quantify priority disinfection by-products and comprehensively identify unknowns.
Acquired Immunodeficiency Syndrome
Impact of chitosan and polyacrylamide on formation of carbonaceous and nitrogenous disinfection by-products.
Acquired Immunodeficiency Syndrome
Occurrence of disinfection by-products in swimming pools and the estimated resulting cytotoxicity.
Adenocarcinoma
Differential Cytotoxicity of Haloaromatic Disinfection Byproducts and Lead Co-exposures against Human Intestinal and Neuronal Cells.
Asthma
Childhood asthma and environmental exposures at swimming pools: state of the science and research recommendations.
Asthma
Definition and quantification of initial anthropogenic pollutant release in swimming pools.
Asthma
Swimming pool water--fractionation and genotoxicological characterization of organic constituents.
Asthma
What's in the Pool? A Comprehensive Identification of Disinfection By-Products and Assessment of Mutagenicity of Chlorinated and Brominated Swimming Pool Water.
Carcinogenesis
Chemical and Toxicological Characterization of Halobenzoquinones, an Emerging Class of Disinfection Byproducts.
Carcinogenesis
Perturbation of xenobiotic metabolism in Dreissena polymorpha model exposed in situ to surface water (Lake Trasimene) purified with various disinfectants.
Carcinoma, Hepatocellular
Anion-exchange resin adsorption followed by electrolysis: A new disinfection approach to control halogenated disinfection byproducts in drinking water.
Carcinoma, Hepatocellular
Comparison of DNA damage in human-derived hepatoma line (HepG2) exposed to the fifteen drinking water disinfection byproducts using the single cell gel electrophoresis assay.
Cleft Palate
Associations Between Disinfection By-Product Exposures and Craniofacial Birth Defects.
Colonic Neoplasms
Induction of transitional cell hyperplasia in the urinary bladder and aberrant crypt foci in the colon of rats treated with individual and a mixture of drinking water disinfection by-products.
Colorectal Neoplasms
Disinfection by-products in drinking water and colorectal cancer: a meta-analysis.
Colorectal Neoplasms
Health impacts of long-term exposure to disinfection by-products in drinking water in Europe: HIWATE.
Colorectal Neoplasms
The epidemiology and possible mechanisms of disinfection by-products in drinking water.
Congenital Abnormalities
Analysis of nitrosamines by capillary electrospray-high-field asymmetric waveform ion mobility spectrometry-MS with programmed compensation voltage.
Congenital Abnormalities
Chlorination disinfection byproducts in water and their association with adverse reproductive outcomes: a review.
Congenital Abnormalities
Drinking water treatment is not associated with an observed increase in neural tube defects in mice.
Congenital Abnormalities
The DBP exposome: Development of a new method to simultaneously quantify priority disinfection by-products and comprehensively identify unknowns.
Congenital Abnormalities
The role of phytoplankton as pre-cursors for disinfection by-product formation upon chlorination.
Diabetes Mellitus
Seasonal variations of blood pressure in adults: Tehran lipid and glucose study.
Hypospadias
Maternal exposure to water disinfection by-products during gestation and risk of hypospadias.
Infections
Evidence of Dbps (decorin binding proteins) among European strains of Borrelia burgdorferi sensu lato and in the immune response of LB patient sera.
Infertility
Identification of endocrine active disinfection by-products (DBPs) that bind to the androgen receptor.
Intellectual Disability
Diagnostic Evaluation of Children with Autism Spectrum Disorders: Clinician Compliance with Published Guidelines.
Learning Disabilities
Management of Attention-Deficit/Hyperactivity Disorder by Developmental-Behavioral Pediatricians: A DBPNet Study.
Leiomyoma
Uterine fibroids increase the risk of hypertensive disorders of pregnancy: a prospective cohort study.
Lymphoma
Mutagenic analysis of six disinfection by-products in the Tk gene of mouse lymphoma cells.
Neoplasm Metastasis
Development of TMTP-1 targeted designer biopolymers for gene delivery to prostate cancer.
Neoplasms
Analysis of preneoplastic and neoplastic renal lesions in Tsc2 mutant Long-Evans (Eker) rats following exposure to a mixture of drinking water disinfection by-products.
Neoplasms
Blood transcriptional and microRNA responses to short-term exposure to disinfection by-products in a swimming pool.
Neoplasms
Chlorination disinfection by-products, public health risk tradeoffs and me.
Neoplasms
Cumulative health risk assessment of disinfection by-products in drinking water by different disinfection methods in typical regions of China.
Neoplasms
DBP-GAPred: An intelligent method for prediction of DNA-binding proteins types by enhanced evolutionary profile features with ensemble learning.
Neoplasms
Development of TMTP-1 targeted designer biopolymers for gene delivery to prostate cancer.
Neoplasms
Disinfection by-products in desalinated and blend water: formation and control strategy.
Neoplasms
Disinfection byproducts in Canadian provinces: associated cancer risks and medical expenses.
Neoplasms
DNA hypomethylation induced by drinking water disinfection by-products in mouse and rat kidney.
Neoplasms
DP-BINDER: machine learning model for prediction of DNA-binding proteins by fusing evolutionary and physicochemical information.
Neoplasms
EPA's Stage 2 Disinfection Byproducts Rules (DBPR) and Northern Kentucky Water: An Economic and Scientific Review.
Neoplasms
Epidemiological approaches in the investigation of environmental causes of cancer: the case of dioxins and water disinfection by-products.
Neoplasms
Evaluating gas chromatography with a halogen-specific detector for the determination of disinfection by-products in drinking water.
Neoplasms
Hazard assessment of three haloacetic acids, as byproducts of water disinfection, in human urothelial cells.
Neoplasms
Heterogeneity in the Relationship between Disinfection By-Products in Drinking Water and Cancer: A Systematic Review.
Neoplasms
NTP taps disinfection by-products for study.
Neoplasms
Occurrence and health risk assessment of halogenated disinfection byproducts in indoor swimming pool water.
Neoplasms
Potential health effects of drinking water disinfection by-products using quantitative structure toxicity relationship.
Neoplasms
Preliminary screening for the potential of drinking water disinfection byproducts to alter male reproduction.
Neoplasms
Reduction of DBPs in synthetic water by indoor techniques and its implications on exposure and health risk.
Neoplasms
The DBP exposome: Development of a new method to simultaneously quantify priority disinfection by-products and comprehensively identify unknowns.
Neoplasms
The epidemiology and possible mechanisms of disinfection by-products in drinking water.
Neoplasms
The role of phytoplankton as pre-cursors for disinfection by-product formation upon chlorination.
Neoplasms
Transcriptome analyses unravel CYP1A1 and CYP1B1 as novel biomarkers for disinfection by-products (DBPs) derived from chlorinated algal organic matter.
Neoplasms
Use of mechanism-based structure-activity relationships analysis in carcinogenic potential ranking for drinking water disinfection by-products.
Neural Tube Defects
Identification of developmentally toxic drinking water disinfection byproducts and evaluation of data relevant to mode of action.
Neuroblastoma
Differential Cytotoxicity of Haloaromatic Disinfection Byproducts and Lead Co-exposures against Human Intestinal and Neuronal Cells.
Obesity
The NIH National Center for Integrative Biomedical Informatics (NCIBI).
Pneumonia
[Cloning and characterization of a new antibacterial target, 3,4-dihydroxy-2-butanone-4-phosphate synthase].
Pregnancy Complications
Tap water use amongst pregnant women in a multi-ethnic cohort.
Premature Birth
Drinking water disinfection by-product exposure and duration of gestation.
Premature Birth
Health impacts of long-term exposure to disinfection by-products in drinking water in Europe: HIWATE.
Primary Dysautonomias
[OP.8D.02] FIRST IN MAN TREATMENT OF SEVERE BP VARIABILITY WITH BAROREFLEX ACTIVATION THERAPY.
Prostatic Neoplasms
The NIH National Center for Integrative Biomedical Informatics (NCIBI).
Rectal Neoplasms
Case control study of the geographic variability of exposure to disinfectant byproducts and risk for rectal cancer.
Sjogren's Syndrome
[OP.8D.02] FIRST IN MAN TREATMENT OF SEVERE BP VARIABILITY WITH BAROREFLEX ACTIVATION THERAPY.
Stillbirth
Chlorination disinfection byproducts in water and their association with adverse reproductive outcomes: a review.
Stillbirth
Health impacts of long-term exposure to disinfection by-products in drinking water in Europe: HIWATE.
Stillbirth
The epidemiology and possible mechanisms of disinfection by-products in drinking water.
Stroke
Association of Blood Pressure With Stroke Risk, Stratified by Age and Stroke Type, in a Low-Income Population in China: A 27-Year Prospective Cohort Study.
Stroke
Optimal Blood Pressure in Patients after Stroke in Rural Areas of China.
Tuberculosis
Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis.
Tuberculosis
The crystal structure reveals the molecular mechanism of bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (Rv1415) from Mycobacterium tuberculosis.
Undifferentiated Connective Tissue Diseases
[OP.8D.02] FIRST IN MAN TREATMENT OF SEVERE BP VARIABILITY WITH BAROREFLEX ACTIVATION THERAPY.
Urinary Bladder Neoplasms
A review on the 40th anniversary of the first regulation of drinking water disinfection by-products.
Urinary Bladder Neoplasms
Biological and statistical approaches for modeling exposure to specific trihalomethanes and bladder cancer risk.
Urinary Bladder Neoplasms
Chemical and Toxicological Characterization of Halobenzoquinones, an Emerging Class of Disinfection Byproducts.
Urinary Bladder Neoplasms
Disinfection byproducts potentially responsible for the association between chlorinated drinking water and bladder cancer: A review.
Urinary Bladder Neoplasms
Drinking Water Disinfection Byproducts (DBPs) and Human Health Effects: Multidisciplinary Challenges and Opportunities.
Urinary Bladder Neoplasms
Energy of the Lowest Unoccupied Molecular Orbital, Thiol Reactivity, and Toxicity of Three Monobrominated Water Disinfection Byproducts.
Urinary Bladder Neoplasms
EPA's Stage 2 Disinfection Byproducts Rules (DBPR) and Northern Kentucky Water: An Economic and Scientific Review.
Urinary Bladder Neoplasms
Identification of endocrine active disinfection by-products (DBPs) that bind to the androgen receptor.
Urinary Bladder Neoplasms
Iodoacetic acid inhibits follicle growth and alters expression of genes that regulate apoptosis, the cell cycle, estrogen receptors, and ovarian steroidogenesis in mouse ovarian follicles.
Urinary Bladder Neoplasms
Nontargeted identification of peptides and disinfection byproducts in water.
Urinary Bladder Neoplasms
Occurrence and formation of halobenzoquinones in indoor and outdoor swimming pool waters of Nanning City, Southwest China.
Urinary Bladder Neoplasms
Occurrence, genotoxicity, and carcinogenicity of regulated and emerging disinfection by-products in drinking water: a review and roadmap for research.
Urinary Bladder Neoplasms
Occurrence, origin, and toxicity of disinfection byproducts in chlorinated swimming pools: An overview.
Urinary Bladder Neoplasms
Polymorphisms in GSTT1, GSTZ1, and CYP2E1, Disinfection Byproducts, and Risk of Bladder Cancer in Spain.
Urinary Bladder Neoplasms
The epidemiology and possible mechanisms of disinfection by-products in drinking water.
Urinary Bladder Neoplasms
Water disinfection by-products and bladder cancer: is there a European specificity? A pooled and meta-analysis of European case-control studies.
Urinary Bladder Neoplasms
What's in the Pool? A Comprehensive Identification of Disinfection By-Products and Assessment of Mutagenicity of Chlorinated and Brominated Swimming Pool Water.
Virus Diseases
Nuclear localization of the adenovirus DNA-binding protein: requirement for two signals and complementation during viral infection.
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evolution
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
-
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
-
malfunction
-
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
-
bleaching leaf phenotype of RIBA1 deficient plants, overview. The bleaching phenotype of the seedlings is not counterbalanced by the simultaneous AtRIBA2 and AtRIBA3 expression
-
metabolism
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
-
3,4-dihydroxy-2-butanone-4-phosphate synthase is one of the key enzymes in the biosynthesis of riboflavin
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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)
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physiological function
-
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
-
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
-
isozyme AtRIBA1 is required for pigmentation of the rosettes leaves
-
physiological function
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
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
-
3,4-dihydroxy-2-butanone 4-phosphate (DHBP) and GTP are the precursors for riboflavin biosynthesis
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physiological function
-
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
-
additional information
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
-
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
-
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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?
x * 42300, recombinant His-tagged N-terminally truncated AtRIBA2
?
x * 47600, recombinant His-tagged N-terminally truncated AtRIBA1
?
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x * 47600, recombinant His-tagged N-terminally truncated AtRIBA1
-
?
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x * 42300, recombinant His-tagged N-terminally truncated AtRIBA2
-
?
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x * 23177, mass spectrometry
?
x * 23251, recombinant enzyme, mass spectrometry
?
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x * 23177, mass spectrometry
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?
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x * 38600, SDS-PAGE, x * 25600, about, sequence calculation
?
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x * 28000, SDS-PAGE, x * 22500, about, sequence calculation
dimer
2 * 22530, mass spectrometry, 2 * 22658, full-length enzyme, sequence calculation
dimer
-
2 * 23000, SDS-PAGE, hydrodynamic analysis, NMR structure study, 2 * 23351, mass spectrometry
dimer
three-dimensional structure, structure-activity relationship study using NMR spectroscopy, residue-specific isotope labeling, and protein deuteration strategies, solution structure, overview
dimer
-
2 * 25799, recombinant enzyme, mass spectrometry and SDS-PAGE
dimer
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enzyme mutant H147S, crystal structure
dimer
-
three-dimensional structure, structure-activity relationship study using NMR spectroscopy, residue-specific isotope labeling, and protein deuteration strategies, solution structure, overview
dimer
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, isolated subunit Mtb-GCHII is a dimer while Mtb-DHBPS exists as amonomer in solution. The N-terminal DHBPS domain of Mtb-ribA2 shows an alpha + beta fold consisting of a central eight-stranded beta-sheet (beta1-beta8) surrounded by seven helices (alpha1-7alpha7)
dimer
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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, isolated subunit Mtb-GCHII is a dimer while Mtb-DHBPS exists as amonomer in solution. The N-terminal DHBPS domain of Mtb-ribA2 shows an alpha + beta fold consisting of a central eight-stranded beta-sheet (beta1-beta8) surrounded by seven helices (alpha1-7alpha7)
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dimer
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determination of the active sites in the homodimer, crystal structure, overview
dimer
DHBPS exists as a homodimer in solution, and the active sites are located at the dimeric interface formed by charged residues from two monomers
dimer
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DHBPS exists as a homodimer in solution, and the active sites are located at the dimeric interface formed by charged residues from two monomers
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dimer
the hydrophobic residues at the dimeric interface play a role in dimer formation, whereas some of the active site residues at the dimeric interface play a role in the catalytic activity of vDHBPS
dimer
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
the hydrophobic residues at the dimeric interface play a role in dimer formation, whereas some of the active site residues at the dimeric interface play a role in the catalytic activity of vDHBPS
-
homodimer
between pH 6.0-9.0, gel filtration
homodimer
gel filtration, 2 * 23310
monomer
-
1 * 24000, SDS-PAGE
monomer
below pH 5.0 enzyme forms an inactive monomer in solution, gel filtration
additional information
both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
additional information
both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
additional information
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both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
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additional information
the enzyme possesses an essential acidic active-site loop, active site structure, structure comparisons, overview
additional information
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hydrodynamic analysis, NMR structure study, isotope labeling, the homodimeric protein obeys strict C2 symmetry, overview
additional information
structure determination and analysis of functions of single residues, overview, dimer interface structure, localization of the active site, sequence and structure comparison
additional information
-
structure determination and analysis of functions of single residues, overview, dimer interface structure, localization of the active site, sequence and structure comparison
additional information
structure-function relationship, overview
additional information
the enzyme comprises one beta-sheet (five-stranded) and eight alpha-helices, adopting a three-layered alpha-beta-alpha sandwich fold
additional information
-
the enzyme comprises one beta-sheet (five-stranded) and eight alpha-helices, adopting a three-layered alpha-beta-alpha sandwich fold
additional information
-
the enzyme comprises one beta-sheet (five-stranded) and eight alpha-helices, adopting a three-layered alpha-beta-alpha sandwich fold
-
additional information
DHBPS enzyme structure comparisons
additional information
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
DHBPS enzyme structure comparisons
-
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purified recombinant apoenzyme in complex with the substrate ribulose 5-phosphate, sitting drop vapour diffusion method, 0.003 ml of 17-34 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml of reservoir solution containing 85 mM sodium citrate, pH 5.0, and 17% PEG 8000, with or without 5 mM EDTA, equilibration against 0.3 ml reservoir solution, 0.003 ml of the complex solution is mixed with 0.001 ml of 90 mM Mes/NaOH, pH 6.0, containing 18% PEG 8000, addition of 2 mM D-ribulose 5-phosphate, 20°C, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution, molecular replacement, modelling
reinterpretation of the space-group symmetry is reported for two crystal structures, PDB codes 1tks and 1tku
purified recombinant enzyme, hanging drop vapour diffusion method at room temperature, 4-5 days, 0.0022 ml of protein solution containing 24 mg/ml protein in 50 mM Tris-HCl pH 7.5, is mixed with 0.0007 ml of precipitating well solution containing 3 M CsCl, 3 M Cs-formate, 20 mM Bis-Tris-propane-NaOH, pH 6.9, or 6 M sodium formate, 25 mM HEPES-NaOH, pH 7.0, labeling with 1.5 mM Au(CN)2, X-ray diffraction structure determination and analysis at 1.4-2.4 A resolution, multiwavelength anomalous diffraction
purified enzyme mutant H147S in complex with substrate ribulose 5-phosphate, monoclinic crystal form, X-ray diffraction structure determination and analysis at 1.55-1.7 A resolution
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purified recombinant bifunctional enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 20-25 mg/ml protein in 20 mM Tris-HCl pH 8.0, 150 mM NaCl, 1 mM DTT, with 0.001 ml of reservoir solutioncontaining 0.1 M Na HEPES pH 7.5, 15%(w/v) PEG 8000, equilibration against 0.04 ml reservoir solution, 20°C, 2-4 days, X-ray diffraction structure determination and analysis at 3.0 A resolution
three crystal structures of Mtb-DHBPS domain in complex with phosphate and glycerol at pH 6.0, with sulfate at pH 4.0 and with zinc and sulfate at pH 4.0 are determined at 1.8, 2.06 and 2.06 A resolution, respectively
purified recombinant enzyme, crystallization of different enzyme complexes: E-SO42-, E-SO42-Mg2+, E-SO42-Mn2+, E-SO42-Mn2+-glycerol, and E-SO42-Zn2+ complexes with X-ray diffraction structure determination and and analysis at resolutions that extend to 1.55 A, 0.98 A, 1.60 A, 1.16 A, and 1.00 A, respectively, divalent cation-free enzyme from 24-30% PEG 5000 monomethyl ether, 0.2 M Li2SO4, and 0.1 M MES-NaOH, pH 6.0-6.5, by the hanging drop vapor diffusion method, to prepare divalent cation-containing crystals, 200 mM MgCl2, 200 mM MnCl2, or 200 mM zinc acetate are added to the crystals for 8-16 h in soaking solutions of the well solutions omitting Li2SO4 and 4% higher in the concentration of PEG 5000 monomethyl ether
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purified recombinnat enzyme divalent cation free, soaked in Zn2+ or soaked in Mg2+, hanging drop vapor diffusion method, room temperature, 0.001 ml of 7 mg/ml protein in 50 mM Tris-HCl, pH 7.5, is mixed with 0.001 ml well solution containing 24-30% PEG monomethyl ether, 0.2 M Li2SO4, and 0.1 M MES-NaOH, pH 6.0-6.5, 1 week-3 months, rectangular plates, X-ray diffraction structure determination and analysis at 1.5 A, 1.0 A, and 1.8 A resolution, respectively
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the crystal structures of Salmonella DHBPS in complex with sulfate, D-ribulose 5-phosphate and sulfate-zinc ion is determined at a resolution of 2.80, 2.52, and 1.86 A, respectively. Analysis of these crystal structures reveals that the acidic loop (residues 34-39) responsible for the acid-base catalysis is disordered in the absence of substrate or metal ion at the active site. Upon binding either substrate or sulfate and metal ions, the acidic loop becomes stabilized, adopts a closed conformation and interacts with the substrate
purified recombinant His-tagged enzyme, hanging-drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 5 mM Tris-HCl, pH 8.0, and 50 mM NaCl, with 0.001 ml of reservoir solution containing ammonium sulfate 2.0 M and 0.1 M BisTris pH7.02, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified enzyme in apoform or in complex with inhibitor 4-phospho-D-erythronohydroxamic acid, or substrate and substrate plus metal ions, sitting drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 25 mM Tris-HCl, pH 8.0, with 0.01 ml crystallization solution, containing for the apo form enzyme 0.2 M Na2HPO4, pH 9.1, and 20% PEG 3350, for phosphate-bound enzyme 0.2 M NaH2PO4, pH 4.5 and 20% PEG 3350, the Ru5P and 4PEH complex crystals are obtained by mixing vDHBPS with 10 mM Ru5P or 4PEH and incubation for 30 min at 20°C, grown in 0.2 M Na2HPO4, pH 9.1 and 20% PEG3350, the enzyme-Ru5P-Zn2+ and enzyme-4PEH-Zn2+ complex crystals are obtained by soaking complex crystals in 100 mM ZnCl2 for 12 h at 20°C, X-ray diffraction structure determination and analysis at 1.96 A, 1.86 A, 1.59 A, and 2.04 A resolution, respectively, modelling
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C59A
site-directed mutagenesis, the mutant shows 70% of wild-type enzyme activity
D92A
site-directed mutagenesis, inactive mutant
E166A
site-directed mutagenesis, inactive mutant
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
D21E
-
site-directed mutagenesis, inactive mutant
D21N
-
site-directed mutagenesis, inactive mutant
D30E
-
site-directed mutagenesis, inactive mutant
E185D
-
site-directed mutagenesis, inactive mutant
E185X
site-directed mutagenesis, inactive mutant
E26D
-
site-directed mutagenesis, inactive mutant
E26Q
-
site-directed mutagenesis, inactive mutant
E28D
-
site-directed mutagenesis, inactive mutant
H164N
-
site-directed mutagenesis, inactive mutant
E154D
-
DBPS activity is abolished
A137T
-
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
-
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
-
E39A
site-directed mutagenesis, inactive mutant
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
H154A
site-directed mutagenesis, inactive mutant
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
-
site-directed mutagenesis, inactive mutant
-
F139A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme
-
H154A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
site-directed mutagenesis, inactive mutant
-
N89A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
-
S64A
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
H147S
site-directed mutagenesis, the mutant enzyme shows about 10% of the wild-type enzyme activity
H147S
-
site-directed mutagenesis, the mutant shows about 10% of wild-type enzyme activity, crystal structure determination with bound substrate
additional information
-
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
-
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
-
construction of RIB3 disruption mutants, restoration by riboflavin of growth of a rib3 deletion mutant on glucose but not glycerol/ethanol, phenotype, overview
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Liao, D.I.; Viitanen, P.V.; Jordan, D.B.
Cloning, expression, purification and crystallization of dihydroxybutanone phosphate synthase from Magnaporthe grisea
Acta Crystallogr. Sect. D
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Pyricularia grisea
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Steinbacher, S.; Schiffmann, S.; Bacher, A.; Fischer, M.
Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate
Acta Crystallogr. Sect. D
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Methanocaldococcus jannaschii
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Picollelli, M.A.; Viitanen, P.V.; Jordan, D.B.
Spectrophotometric determination of 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Anal. Biochem.
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Escherichia coli, Escherichia coli W3110 / ATCC 27325
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Liao, D.I.; Zheng, Y.J.; Viitanen, P.V.; Jordan, D.B.
Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase
Biochemistry
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Pyricularia grisea
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Richter, G.; Kelly, M.; Krieger, C.; Yu, Y.; Bermel, W.; Karlsson, G.; Bacher, A.; Oschkinat, H.
NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling
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Escherichia coli
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Volk, R.; Bacher, A.
Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3,4-dihydroxy-2-butanone-4-phosphate synthase
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Meyerozyma guilliermondii
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Volk, R.; Bacher, A.
Biosynthesis of riboflavin. Studies on the mechanism of L-3,4-dihydroxy-2-butanone 4-phosphate synthase
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Meyerozyma guilliermondii
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Fischer, M.; Romisch, W.; Schiffmann, S.; Kelly, M.; Oschkinat, H.; Steinbacher, S.; Huber, R.; Eisenreich, W.; Richter, G.; Bacher, A.
Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii
J. Biol. Chem.
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Methanocaldococcus jannaschii
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Jin, C.; Barrientos, A.; Tzagoloff, A.
Yeast dihydroxybutanone phosphate synthase, an enzyme of the riboflavin biosynthetic pathway, has a second unrelated function in expression of mitochondrial respiration
J. Biol. Chem.
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Saccharomyces cerevisiae
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Steinbacher, S.; Schiffmann, S.; Richter, G.; Huber, R.; Bacher, A.; Fischer, M.
Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: implications for the catalytic mechanism
J. Biol. Chem.
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Methanocaldococcus jannaschii (Q60364)
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Huembelin, M.; Griesser, V.; Keller, T.; Schurter, W.; Haiker, M.; Hohmann, H.P.; Ritz, H.; Richter, G.; Bacher, A.; Van Loon, A.P.G.M.
GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase are rate-limiting enzymes in riboflavin synthesis of an industrial Bacillus subtilis strain used for riboflavin production
J. Indust. Microbiol. Biotechnol.
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Bacillus subtilis
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Echt, S.; Bauer, S.; Steinbacher, S.; Huber, R.; Bacher, A.; Fischer, M.
Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans
J. Mol. Biol.
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Candida albicans (Q5A3V6)
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Goetze, E.; Kis, K.; Eisenreich, W.; Yamauchi, N.; Kakinuma, K.; Bacher, A.
Biosynthesis of riboflavin. Stereochemistry of the 3,4-dihydroxy-2-butanone 4-phosphate synthase reaction
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Escherichia coli
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Richter, G.; Krieger, C.; Volk, R.; Kis, K.; Ritz, H.; Gotze, E.; Bacher, A.
Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase
Methods Enzymol.
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Escherichia coli K-12 (P0A7J0)
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Kelly, M.J.; Ball, L.J.; Krieger, C.; Yu, Y.; Fischer, M.; Schiffmann, S.; Schmieder, P.; Kuhne, R.; Bermel, W.; Bacher, A.; Richter, G.; Oschkinat, H.
The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site
Proc. Natl. Acad. Sci. USA
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2001
Methanocaldococcus jannaschii, Escherichia coli (P0A7J0), Escherichia coli
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Liao, D.I.; Calabrese, J.C.; Wawrzak, Z.; Viitanen, P.V.; Jordan, D.B.
Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis
Structure
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11-18
2001
Escherichia coli (P0A7J0), Escherichia coli
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Le Trong, I.; Stenkamp, R.E.
Alternative models for two crystal structures of Candida albicans 3,4-dihydroxy-2-butanone 4-phosphate synthase
Acta Crystallogr. Sect. D
64
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2008
Candida albicans (Q5A3V6)
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Isarankura-Na-Ayudhya, P.; Isarankura-Na-Ayudhya, C.; Treeratanapaiboon, L.; Kasikun, K.; Thipkeaw, K.; Prachayasittikul, V.
Proteomic profiling of Escherichia coli in response to heavy metals stress
Eur. J. Sci. Res.
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2009
Escherichia coli, Escherichia coli TG1
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Singh, M.; Kumar, P.; Karthikeyan, S.
Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis
J. Struct. Biol.
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Mycobacterium tuberculosis (A5U2B7), Mycobacterium tuberculosis
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Asai, S.; Mase, K.; Yoshioka, H.
A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance
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Nicotiana benthamiana
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Kumar, P.; Singh, M.; Gautam, R.; Karthikeyan, S.
Potential anti-bacterial drug target: structural characterization of 3,4-dihydroxy-2-butanone-4-phosphate synthase from Salmonella typhimurium LT2
Proteins
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3292-3303
2010
Salmonella enterica subsp. enterica serovar Typhimurium (P66032)
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Singh, M.; Kumar, P.; Yadav, S.; Gautam, R.; Sharma, N.; Karthikeyan, S.
The crystal structure reveals the molecular mechanism of bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (Rv1415) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
69
1633-1644
2013
Mycobacterium tuberculosis (A5U2B7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Ra / ATCC 25177 (A5U2B7)
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Hiltunen, H.M.; Illarionov, B.; Hedtke, B.; Fischer, M.; Grimm, B.
Arabidopsis RIBA proteins: two out of three isoforms have lost their bifunctional activity in riboflavin biosynthesis
Int. J. Mol. Sci.
13
14086-14105
2012
Arabidopsis thaliana (P47924), Arabidopsis thaliana (Q6NLQ7), Arabidopsis thaliana Col-0 (P47924), Arabidopsis thaliana Col-0 (Q6NLQ7)
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Li, J.; Hua, Z.; Miao, L.; Jian, T.; Wei, Y.; Shasha, Z.; Shaocheng, Z.; Zhen, G.; Hongpeng, Z.; Ailong, H.; Deqiang, W.
The crystal structure and biochemical properties of DHBPS from Streptococcus pneumoniae, a potential anti-infective target for Gram-positive bacteria
Protein Expr. Purif.
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161-168
2013
Streptococcus pneumoniae (A0A0H2UN41), Streptococcus pneumoniae, Streptococcus pneumoniae TIGR 4 (A0A0H2UN41)
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Xu, Z.; Lin, Z.; Wang, Z.; Chen, T.
Improvement of the riboflavin production by engineering the precursor biosynthesis pathways in Escherichia coli
Chin. J. Chem. Engin.
23
1834-1839
2015
Escherichia coli (P0A7J0), Escherichia coli K-12 / MG1655 (P0A7J0)
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Islam, Z.; Kumar, A.; Singh, S.; Salmon, L.; Karthikeyan, S.
Structural basis for competitive inhibition of 3,4-dihydroxy-2-butanone-4-phosphate synthase from Vibrio cholerae
J. Biol. Chem.
290
11293-11308
2015
no activity in Homo sapiens, Vibrio cholerae serotype O1 (Q9KKP2), Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961 (Q9KKP2)
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Fang, X.; Barbetti, M.J.
Differential protein accumulations in isolates of the strawberry wilt pathogen Fusarium oxysporum f. sp. fragariae differing in virulence
J. Proteomics
108
223-237
2014
Fusarium oxysporum f. sp. fragariae
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Tuan, P.A.; Zhao, S.; Kim, J.K.; Kim, Y.B.; Yang, J.; Li, C.H.; Kim, S.J.; Arasu, M.V.; Al-Dhabi, N.A.; Park, S.U.
Riboflavin accumulation and molecular characterization of cDNAs encoding bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase, lumazine synthase, and riboflavin synthase in different organs of Lycium chinense plant
Molecules
19
17141-17153
2014
Lycium chinense (W0FER2), Lycium chinense
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