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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.
dTDP-3-azido-3-deoxy-D-glucose
dTDP-3-azido-3,6-dideoxy-alpha-D-xylo-hexopyran-4-ulose
-
-
-
?
dTDP-3-deoxy-D-glucose
dTDP-3,6-dideoxy-alpha-D-erythro-hexopyran-4-ulose
-
-
-
?
dTDP-6-fluoro-6-deoxyglucose
dTDP-4-keto-6-deoxyglucose + F-
substrate undergoes fluoride ion elimination instead of dehydration
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
dUDP-glucose
dUDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
additional information
?
-
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
the enzyme is specifically active toward dTDP-Glc, showing little, if any, activity toward UDP-Glc and no activity toward other potential NDP-glucose substrates or toward several NDP-sugars that are abundant in Caenorhabditis elegans (e.g. GDP-Man, UDP-GlcNAc and UDPGal)
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
the enzyme is involved in the biosynthesis of the dTDP-3-amino-3,6-dideoxy-D-galactose and dTDP-3-amino-3,6-dideoxy-D-glucose
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
QM/MM investigation of the detailed mechanism of dTDP-glucose 4,6-dehydratase. The computational results demonstrate that the whole catalytic reaction contains four enzymatic elementary steps and one nonenzymatic enol-keto tautomerisation step. In the oxidation step, the NAD+ abstracts the hydride from glycosyl C4 and a conserved tyrosine residue removes a proton from the glycosyl C4-hydroxyl group. This oxidation step proceeds through a concerted asynchronous mechanism with a calculated free energy barrier of 21.1 kcal/mol, in which the hydride transfer lags behind the proton transfer. Different from the proposal based on experiments that the dehydration follows a concerted mechanism. The QM/MM calculation results show that the elimination of water is stepwise, in which two highly conserved residues are involved. Glu129 firstly deprotonates the glycosyl C5 and subsequently Asp128 protonates the leaving C6-hydroxyl group to give a water molecule and dTDP-4-dehydroglucose-5,6-ene intermediate. In the reduction step, NADH returns the hydride back to glycosyl C6 and the phenolic hydroxyl of Tyr151 spontaneously denotes its proton to C4-keto group, forming an enol
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-glucose
?
-
-
-
-
?
dTDP-glucose
?
-
key role in biosynthesis of macrolides and other types of antibiotics
-
-
?
dTDP-glucose
?
-
activity increases during stationary growth phase
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
the conversion takes place in three steps: dehydrogenation to dTDP-4-ketoglucose, dehydration to dTDP-4-ketoglucose-5,6-ene and rereduction of C6 to the methyl group
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
the conversion takes place in three steps: dehydrogenation to dTDP-4-ketoglucose, dehydration to dTDP-4-ketoglucose-5,6-ene and rereduction of C6 to the methyl group. Asp135 and Glu136 are the acid and base catalysts, respectively of the dehydration step
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
the single-turnover kinetic mechanism for the reaction is determined by rapid mix-chemical quench mass spectrometry. NAD+ initially oxidizes glucosyl C4 of dTDP-glucose to NADH and dTDP-4-ketoglucose. Next water is eliminated between C5 and C6 of dTDP-4-ketoglucose to form dTDP-4-ketoglucose-5,6-ene. Hydride transfer from NADH to C6 of dTDP-4-ketoglucose-5,6-ene regenerates NAD+ and produces the product dTDP-4-keto-4-deoxyglucose
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
second enzyme in the dTDP-L-rhamnose pathway
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
second enzyme of the dTDP-L-rhamnose synthesis pathway
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
enzyme consists of a C-terminal sugar-nucleotide binding domain and an N-terminal NAD+ cofactor-binding domain
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
involved in initial steps of glycan biosynthesis of bacterial cell surface layer (S-layer)
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
involved in initial steps of glycan biosynthesis of bacterial cell surface layer (S-layer)
-
-
?
UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
E3VXL5
-
-
-
?
UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
UDP-D-glucose
UDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
additional information
?
-
-
not: ADPglucose, CDPglucose, UDPglucose, GDPglucose, UDPgalactose, dTDPmannose, CTP and dTTP
-
-
?
additional information
?
-
-
enzyme of the 6-deoxyhexose biosynthetic pathway, that is also present in the aminoglycoside antibiotic biosynthetic pathway
-
-
?
additional information
?
-
-
not: ADPglucose, ADPmannose, GDPmannose, GDPglucose, UDPgalactose
-
-
?
additional information
?
-
-
not: ADPglucose, ADPmannose, GDPmannose, GDPglucose, UDPgalactose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
additional information
?
-
-
enzyme of the 6-deoxyhexose biosynthetic pathway, that is also present in the aminoglycoside antibiotic biosynthetic pathway
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
the enzyme is involved in the biosynthesis of the dTDP-3-amino-3,6-dideoxy-D-galactose and dTDP-3-amino-3,6-dideoxy-D-glucose
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-alpha-D-glucose
dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
-
-
-
-
?
dTDP-glucose
?
-
-
-
-
?
dTDP-glucose
?
-
key role in biosynthesis of macrolides and other types of antibiotics
-
-
?
dTDP-glucose
?
-
activity increases during stationary growth phase
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
second enzyme of the dTDP-L-rhamnose synthesis pathway
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
involved in initial steps of glycan biosynthesis of bacterial cell surface layer (S-layer)
-
-
?
dTDP-glucose
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
involved in initial steps of glycan biosynthesis of bacterial cell surface layer (S-layer)
-
-
?
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0.000064 - 0.053
dTDP-6-fluoro-6-deoxyglucose
466.6
dTDP-alpha-D-glucose
pH 7.5, 30°C
0.0089 - 6.08
dTDP-glucose
0.024
UDP-glucose
pH 7.5, 37°C, wild-type enzyme
0.000064
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme E136A
0.000065
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme K199R
0.00013
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme D135N/E136Q
0.00017
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme K199M
0.00023
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme E198Q
0.00064
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme E136Q
0.0014
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme Y301F
0.029
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme D135A
0.044
dTDP-6-fluoro-6-deoxyglucose
wild-type enzyme
0.053
dTDP-6-fluoro-6-deoxyglucose
mutant enzyme D135N
0.0089
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190A
0.011
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190D
0.017
dTDP-glucose
mutant enzyme E136A
0.017
dTDP-glucose
mutant enzyme K199R
0.017
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136A
0.017
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K199R
0.019
dTDP-glucose
mutant enzyme E198Q
0.019
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E198Q
0.0198
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y160A
0.0207
dTDP-glucose
pH 7.5, 37°C, mutant enzyme T134V
0.021
dTDP-glucose
pH 7.5, 37°C, mutant enzyme T134A
0.022
dTDP-glucose
mutant enzyme D135A
0.022
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135A
0.0226
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190H
0.024
dTDP-glucose
mutant enzyme D135N/E136Q
0.024
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N/E136Q
0.0258
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y160F
0.0395
dTDP-glucose
mutant enzyme D135N
0.0395
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N
0.042
dTDP-glucose
mutant enzyme Y301F
0.042
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y301F
0.0425
dTDP-glucose
mutant enzyme K199M
0.0425
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K199M
0.043
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232Q
0.051
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K164M
0.073
dTDP-glucose
mutant enzyme E136Q
0.073
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136Q
0.085
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232A
0.14
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K164A
0.52
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A
0.72
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232N
1.2
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187S
1.9
dTDP-glucose
pH 7.5, 18°C, wild-type enzyme
2.4
dTDP-glucose
pH 7.5, 37°C, mutant enzyme T134S
4.9
dTDP-glucose
wild-type enzyme
4.9
dTDP-glucose
pH 7.5, 37°C, wild-type enzyme
4.9
dTDP-glucose
-
pH 7.5, 37°C, wild-type enzyme
6.08
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A
6.08
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232N
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C187A
9.4fold decrease in turnover number for dTDP-glucose compared to wild-type value, 6fold decrease in KM-value for dTDP-glucose compared to wild-type value. 8% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
C187S
4.1fold decrease in turnover number for dTDP-glucose compared to wild-type value, 4fold decrease in KM-value for dTDP-glucose compared to wild-type value. 5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
D135135N/E136Q
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 340fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 204fold lower than that of the wild-type enzyme
D135N/E136Q
204fold decrease in turnover number for dTDP-glucose compared to wild-type value, 3.2fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
H232A
57.6fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.8fold decrease in KM-value for dTDP-glucose compared to wild-type value
H232N
6.8fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold decrease in KM-value for dTDP-glucose compared to wild-type value. 3% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
H232Q
114fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
K164A
15fold increase in Km-value for dTDP-glucose, 820fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 34fold decrease in turnover-number for dTDP-glucose
K164M
8.7fold increase in Km-value for dTDP-glucose, 837fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 96fold decrease in turnover-number for dTDP-glucose
N190A
551fold decrease in turnover number for dTDP-glucose compared to wild-type value, 0.92fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
N190D
441fold decrease in turnover number for dTDP-glucose compared to wild-type value, fold 4.2increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
N190H
217fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold increase in KM-value for dTDP-glucose compared to wild-type value
T134A
1.2fold increase in Km-value for dTDP-glucose, 283fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 233fold decrease in turnover-number for dTDP-glucose
T134S
3.7fold increase in Km-value for dTDP-glucose, 7.5fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 2fold decrease in turnover-number for dTDP-glucose
T134V
3.3fold increase in Km-value for dTDP-glucose, 788fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 237fold decrease in turnover-number for dTDP-glucose
Y160A
2.8fold increase in Km-value for dTDP-glucose, 683fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 247fold decrease in turnover-number for dTDP-glucose
Y160F
1.2fold increase in Km-value for dTDP-glucose, 234fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 190fold decrease in turnover-number for dTDP-glucose
D135A
222fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 30% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
D135A
-
switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5C6 bond rotation in the active site
D135A
the steady-state rate of conversion of dTDP-6-fluoro-6-deoxyglucose to dTDP-4-keto-6-deoxyglucose is identical to that of wild-type. The turnover number for dTDP-6-fluoro-6-deoxyglucose is 1.5fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 223fold lower than that of the wild-type enzyme
D135N
124fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. 9% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
D135N
-
switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5C6 bond rotation in the active site
D135N
the steady-state rate of conversion of dTDP-6-fluoro-6-deoxyglucose to dTDP-4-keto-6-deoxyglucose is identical to that of wild-type. The turnover number for dTDP-6-fluoro-6-deoxyglucose is 1.2fold higher than that of the wild-type enzyme, the turnover number for dTDP-glucose is 124fold lower than that of the wild-type enzyme
E136A
288fold decrease in turnover number for dTDP-glucose compared to wild-type value, 2fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
E136A
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 690fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 288fold lower than that of the wild-type enzyme
E136Q
67fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.5fold increase in KM-value for dTDP-glucose compared to wild-type value. 3% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
E136Q
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 69fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 67fold lower than that of the wild-type enzyme
E198Q
258fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.8fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
E198Q
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 190fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 258fold lower than that of the wild-type enzyme
K199M
115fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. 2% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
K199M
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 260fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 115fold lower than that of the wild-type enzyme
K199R
288fold decrease in turnover number for dTDP-glucose compared to wild-type value, 2.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 2% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
K199R
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 680fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 288fold lower than that of the wild-type enzyme
Y301F
117fold decrease in turnover number for dTDP-glucose compared to wild-type value, 5.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 39% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme
Y301F
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 31fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 117fold lower than that of the wild-type enzyme
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Vara, J.A.; Hutchinson, C.R.
Purification of thymidine-diphospho-D-glucose 4,6-dehydratase from an erythromycin-producing strain of Saccharospora erythraea by high resolution liquid chromatography
J. Biol. Chem.
263
14992-14995
1988
Saccharopolyspora erythraea
brenda
Matern, H.; Brillinger, G.U.; Pape, H.
Stoffwechselprodukte von Mikroorganismen. 114. Mitteilung. Thymidin-diphospho-D-glucose oxidoreduktase aus Streptomyces rimosus
Arch. Mikrobiol.
88
37-48
1973
Streptomyces rimosus
brenda
Glaser, L.; Zarkowsky, H.
Dehydration in nucleotide-linked deoxysugar synthesis
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
465-480
1971
Escherichia coli
-
brenda
Zarkowsky, H.; Lipkin, E.; Glaser, L.
The mechanism of 6-deoxyhexose synthesis. V. The relation of pyridine nucleotide to the structure of the deoxythymidine diphosphate-glucose oxidoreductase
J. Biol. Chem.
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6599-6606
1970
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brenda
Zarkowsky, H.; Lipkin, E.; Glaser, L.
The mechanism of 6-deoxyhexose synthesis. IV. The role of pyridine nucleotide in substrate release
Biochem. Biophys. Res. Commun.
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787-793
1970
Escherichia coli
brenda
Wang, S.F.; Gabriel, O.
Biological mechanisms involved in the formation of deoxysugars. VI. Role and function of enzyme-bound nicotinamide adenine dinucleotide in thymidine diphosphate D-glucose oxidoreductase
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245
8-14
1970
Escherichia coli
brenda
Zarkowsky, H.; Glaser, L.
The mechanism of 6-deoxyhexose synthesis. III. Purification of deoxythymidine diphosphate-glucose oxidoreductase
J. Biol. Chem.
244
4750-4756
1969
Escherichia coli
brenda
Wang, S.F.; Gabriel, O.
Biological mechanisms involved in the formation of deoxysugars. V. Isolation and characterization of thymidine diphosphate D-glucose oxidoreductase from Escherichia coli B
J. Biol. Chem.
244
3430-3437
1969
Escherichia coli
brenda
Melo, A.; Elliott, W.H.; Glaser, L.
The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen transfer catalyzed by deoxythymidine diphosphate-D-glucose oxidoreductase
J. Biol. Chem.
243
1467-1474
1968
Escherichia coli
brenda
Gilbert, J.M.; Matsuhashi, M.; Strominger, J.L.
Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. II. Purification and properties of thymidine diphosphate D-glucose oxidoreductase
J. Biol. Chem.
240
1305-1308
1965
Escherichia coli
brenda
Romana, L.K.; Santiago, F.S.; Reeves, P.R.
High level expression and purification of dThymidine diphospho-D-glucose 4,6-dehydratase (rfbB) from Salmonella serovar typhimurium LT2
Biochem. Biophys. Res. Commun.
174
846-852
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Linton, K.J.; Jarvis, B.W.; Hutchinson, C.R.
Cloning of the genes encoding thymidine diphosphoglucose 4,6-dehydratase and thymidine diphospho-4-keto-6-deoxyglucose 3,5-epimerase from the erythomycin-producing Saccharopolyspora erythraea
Gene
153
33-40
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Saccharopolyspora erythraea
brenda
Naundorf, A.; Klaffke, W.
Substrate specificity of native dTDP-D-glucose-4,6-dehydratase. Chemo-enzymatic syntheses of artificial and naturally occuring deoxy sugars
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285
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1996
Escherichia coli
brenda
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Combined preparative enzymatic synthesis of dTDP-6-deoxy-4-keto-D-glucose from dTDP and sucrose
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15
139-145
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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Purification and characterization of TDP-D-glucose 4,6-dehydratase from anthracycline-producing streptomycetes
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138
779-786
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Streptomyces peucetius, Streptomyces sp. C5
brenda
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The purification, crystallization and structural elucidation of dTDP-D-glucose 4,6-dehydratase (RmlB), the second enzyme of the dTDP-L-rhamnose synthesis pathway from Salmonella enterica serovar typhimurium
Acta Crystallogr. Sect. D
56
222-225
2000
Salmonella enterica
brenda
Gross, J.W.; Hegeman, A.D.; Vestling, M.M.; Frey, P.A.
Characterization of enzymatic processes by rapid mix-quench mass spectrometry: the case of dTDP-glucose 4,6-dehydratase
Biochemistry
39
13633-13640
2000
Escherichia coli (P27830)
brenda
Gross, J.W.; Hegeman, A.D.; Gerratana, B.; Frey, P.A.
Dehydration is catalyzed by glutamate-136 and aspartic acid-135 active site residues in Escherichia coli dTDP-glucose 4,6-dehydratase
Biochemistry
40
12497-12504
2001
Escherichia coli (P27830), Escherichia coli
brenda
Hegeman, A.D.; Gross, J.W.; Frey, P.A.
Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site
Biochemistry
40
6598-6610
2001
Escherichia coli (P27830), Escherichia coli
brenda
Gerratana, B.; Cleland, W.W.; Frey, P.A.
Mechanistic roles of Thr134, Tyr160, and Lys 164 in the reaction catalyzed by dTDP-glucose 4,6-dehydratase
Biochemistry
40
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2001
Escherichia coli (P27830), Escherichia coli
brenda
Hegeman, A.D.; Gross, J.W.; Frey, P.A.
Concerted and stepwise dehydration mechanisms observed in wild-type and mutated Escherichia coli dTDP-glucose 4,6-dehydratase
Biochemistry
41
2797-2804
2002
Escherichia coli
brenda
Allard, S.T.; Cleland, W.W.; Holden, H.M.
High resolution X-ray structure of dTDP-glucose 4,6-dehydratase from Streptomyces venezuelae
J. Biol. Chem.
279
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Streptomyces venezuelae
brenda
Sohng, J.K.; Noh, H.R.; Lee, O.H.; Kim, S.J.; Han, J.M.; Nam, S.K.; Yoo, J.C.
Function of lysine-148 in dTDP-D-glucose 4,6-dehydratase from Streptomyces antibioticus Tue99
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12
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2002
Streptomyces antibioticus, Streptomyces antibioticus Tue99
-
brenda
Yoo, J.C.; Han, J.M.; Sohng, J.K.
Expression of orf7(oxi III) as dTDP-glucose 4,6-dehydratase gene cloned from Streptomyces antibioticus Tu99 and biochemical characteristics of expressed protein
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1999
Streptomyces antibioticus, Streptomyces antibioticus Tu99
-
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The crystal structure of dTDP-D-glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar typhimurium, the second enzyme in the dTDP-l-rhamnose pathway
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2001
Salmonella enterica
brenda
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Identification and functional analysis of dTDP-glucose-4,6-dehydratase gene and its linked gene cluster in an aminoglycoside antibiotics producer of Streptomyces tenebrarius H6
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2004
Streptoalloteichus tenebrarius
brenda
Pfoestl, A.; Zayni, S.; Hofinger, A.; Kosma, P.; Schaeffer, C.; Messner, P.
Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha -D-glucose
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410
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2008
Thermoanaerobacterium thermosaccharolyticum (Q6TFC2), Thermoanaerobacterium thermosaccharolyticum E207-71 (Q6TFC2)
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Precursor for biosynthesis of sugar moiety of doxorubicin depends on rhamnose biosynthetic pathway in Streptomyces peucetius ATCC 27952
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85
1565-1574
2010
Streptomyces peucetius (C5J046), Streptomyces peucetius
brenda
Parakkottil Chothi, M.; Duncan, G.; Armirotti, A.; Abergel, C.; Gurnon, J.; Van Etten, J.; Bernardi, C.; Damonte, G.; Tonetti, M.
Identification of an L-rhamnose synthetic pathway in two nucleocytoplasmic large DNA viruses
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84
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2010
Acanthocystis turfacea chlorella virus 1 (A7K9F4), Acanthamoeba polyphaga Mimivirus (E3VXL5)
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Distribution of dTDP-glucose-4,6-dehydratase gene and diversity of potential glycosylated natural products in marine sediment-derived bacteria
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90
1347-1359
2011
Bacillus sp. (in: Bacteria), Streptomyces sp., Micromonospora sp., Nocardia sp., Pseudomonas sp., Rhodococcus sp., Streptosporangium sp., Ensifer sp. AS08, Dietzia sp. 3149, Shimazuella sp. 3435, Rhodospirillaceae bacterium 5305, Glycomyces sp. 3338, Verrucosispora sp. 3133, Filomicrobium sp. 454, Prauseria sp. 3425, Saccharothrix sp. 5133, Streptosporangium sp. 5322, Micromonospora sp. 3437-1, Micromonospora sp. 3387, Micromonospora sp. 3372-2, Streptomyces sp. 5320, Streptomyces sp. 5311, Streptomyces sp. 3419, Micromonospora sp. 114, Micromonospora sp. 5297, Ensifer sp. AS08 448, Micromonospora sp. 282, Rhodococcus sp. 3376-1, Streptomyces sp. 3127, Streptomyces sp. 5191, Dietzia sp. DQ12-45-1b 3149, Streptomyces sp. SCC 2136, Micromonospora sp. 3134, Micromonospora sp. 3137, Micromonospora sp. 3113, Micromonospora sp. 3191, Streptomyces sp. 5175, Streptomyces sp. 568, Nocardia sp. 5314, Pseudomonas sp. 5302, Bacillus sp. (in: Bacteria) 5187
brenda
Wu, C.; Tan, Y.; Gan, M.; Wang, Y.; Guan, Y.; Hu, X.; Zhou, H.; Shang, X.; You, X.; Yang, Z.; Xiao, C.
Identification of elaiophylin derivatives from the marine-derived actinomycete Streptomyces sp. 7-145 using PCR-based screening
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76
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2013
Streptomyces sp., Streptomyces sp. 7-145
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Shi, X.; Sha, S.; Liu, L.; Li, X.; Ma, Y.
A 96-well microtiter plate assay for high-throughput screening of Mycobacterium tuberculosis dTDP-D-glucose 4,6-dehydratase inhibitors
Anal. Biochem.
498
53-58
2016
Mycobacterium tuberculosis (P9WN65), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WN65)
brenda
Feng, L.; Shou, Q.; Butcher, R.A.
Identification of a dTDP-rhamnose biosynthetic pathway that oscillates with the molting cycle in Caenorhabditis elegans
Biochem. J.
473
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2016
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Campylobacter jejuni (Q6EB26)
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Streptomyces venezuelae (Q9ZGH3)
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