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1 we show that the loss of Drosophila TDP-43 (dTDP-43) results in an increased production of sensory b
5 Escherichia coli gene wbbL, which encodes a dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-
7 ing that the enzyme encoded by the gene is a dTDP-beta-L-rhamnose alpha-1,3-L-rhamnosyl transferase t
13 -deoxysugar donors, dTDP-L-2-deoxyfucose and dTDP-L-daunosamine, and the monoglycosyl aglycone, rhodo
14 phosphorylation of dGMP and dTMP to dGDP and dTDP, respectively, by using either GTP, dGTP or dTTP as
17 irement for GDP-d-mannose, UDP-d-glucose and dTDP-l-rhamnose in Psl production and surface attachment
20 etic mechanism for the reaction catalyzed by dTDP-glucose 4,6-dehydratase (4,6-dehydratase) has been
23 DP-4-keto-6-deoxyglucose by Escherichia coli dTDP-glucose 4,6-dehydratase (4,6-dehydratase) takes pla
27 tep in d-kijanose biosynthesis by converting dTDP-3-amino-2,3,6-trideoxy-4-keto-3-methyl-d-glucose in
28 and purified from, Escherichia coli converts dTDP-4-keto-6-deoxy-Glc to dTDP-beta-l-rhamnose in the p
29 ction mixtures containing recombinant Cps2T, dTDP-rhamnose, and the Cps2E product (undecaprenyl pyrop
30 ive substrate, dTDP-6-fluoro-6-deoxyglucose (dTDP-6FGlc), which undergoes fluoride ion elimination in
31 sphate)(dTMP-PCP), thymidine 5'-diphosphate (dTDP), adenosine 5'-triphosphate (ATP), and adenosine 5'
33 e preparation of dTDP-L-2-deoxysugar donors, dTDP-L-2-deoxyfucose and dTDP-L-daunosamine, and the mon
34 complexes of the enzyme with CoA and either dTDP-D-Quip3N or dTDP-3-amino-3,6-didexoy-alpha-D-galact
36 r nucleotides, like UDP-galactose epimerase, dTDP-glucose-4,6-dehydratase, and UDP-xylose synthase.
46 dTTP; 6 x 10(-7) M, dTMP-PCP; 4 x 10(-6) M, dTDP; 3 x 10(-5) M, ATP; 2 x 10(-6) M, ATP gamma S), whi
52 enzymes are required for the biosynthesis of dTDP-desosamine in Streptomyces venezuelae, with the las
53 the enzymes involved in the biosynthesis of dTDP-Fucp3NAc is a 3,4-ketoisomerase, hereafter referred
54 d a four-gene operon for the biosynthesis of dTDP-L-rhamnose, an essential precursor for the sphingan
55 lar to genes involved in the biosynthesis of dTDP-rhamnose, glycosyltransferases, and ABC transporter
57 xt, water is eliminated between C5 and C6 of dTDP-4-ketoglucose to form dTDP-4-ketoglucose-5,6-ene.
59 nospora chalcea, catalyzes the conversion of dTDP-3-amino-2,3,6-trideoxy-4-keto-D-glucose to dTDP-3-a
62 cose 4,6-dehydratase catalyzed conversion of dTDP-glucose to dTDP-4-keto-6-deoxyglucose occurs in thr
63 e, transient appearance and disappearance of dTDP-hexopyranose-5,6-ene (the reductively stabilized dT
64 he phosphotransfer reaction for formation of dTDP from dTMP is a new strategy for anticancer treatmen
68 pimerization of the C3' and C5' positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-l
69 enzymes, AknK, as well as the preparation of dTDP-L-2-deoxysugar donors, dTDP-L-2-deoxyfucose and dTD
70 , the 4A' hexamers formed in the presence of dTDP with or without Mg2+ did not bind DNA, indicating t
71 stals of KijD3 were grown in the presence of dTDP, and the structure was solved to 2.05-A resolution.
81 growth of mycobacteria and the targeting of dTDP-rhamnose synthesis for new tuberculosis drugs is su
83 enzyme with CoA and either dTDP-D-Quip3N or dTDP-3-amino-3,6-didexoy-alpha-D-galactose (dTDP-D-Fucp3
85 e synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wal
87 DesI was solved in complex with its product, dTDP-4-amino-4,6-dideoxyglucose, to a nominal resolution
88 crystallized in the presence of its product, dTDP-Quip3N, and the structure was solved and refined to
90 glycosyl transferase, and orfde6, a putative dTDP-rhamnose biosynthesis gene, generated two OG1RF mut
91 the fraction of NADH formed with saturating dTDP-xylose show shifts in the pK(a) assigned to Tyr160
92 pyranose-5,6-ene (the reductively stabilized dTDP-4-ketoglucose-5,6-ene), and the appearance of produ
94 he glycosyltransferases, the donor substrate dTDP-rhamnose was first synthesized using recombinant S.
95 zed as a complex with NAD+ and the substrate dTDP-glucose and its structure determined to 1.35 A reso
97 as performed using an alternative substrate, dTDP-6-fluoro-6-deoxyglucose (dTDP-6FGlc), which undergo
98 P-benzene binding mode, the DesVI substrate, dTDP-3-(methylamino)-3,4,6-trideoxyglucose, has been mod
99 AknK also accepts an alternate dTDP-L-sugar, dTDP-L-daunosamine, and other monoglycosylated anthracyc
100 -vancosamine from the chemically synthesized dTDP-4-epi-vancosamine to the beta-OH-Tyr6 residue of th
101 tion studies further support the notion that dTDP-43 acts through miR-9a to control the precision of
105 ino acid side chains involved in binding the dTDP-sugar into the active site include Tyr 183, His 309
107 either of two mechanisms, enolization of the dTDP-4-ketoglucose intermediate, followed by elimination
108 es in the first hydride transfer step of the dTDP-glucose 4,6-dehydratase mechanism has been studied
111 ble for anchoring the hexose moieties of the dTDP-sugars to the protein include Glu 141, Asn 159, and
115 dy-state rate of conversion of dTDP-6FGlc to dTDP-4-keto-6-deoxyglucose by each Asp135 variant was id
117 nation to dTDP-4-ketoglucose, dehydration to dTDP-4-ketoglucose-5,6-ene, and rereduction of C6 to the
118 tive site in three steps: dehydrogenation to dTDP-4-ketoglucose, dehydration to dTDP-4-ketoglucose-5,
119 The enzyme phosphorylates dTMP and dGMP to dTDP and dGDP, respectively, in the presence of a phosph
122 P-3-amino-2,3,6-trideoxy-4-keto-D-glucose to dTDP-3-amino-2,3,6-trideoxy-4-keto-3-methyl-D-glucose.
123 tase catalyzed conversion of dTDP-glucose to dTDP-4-keto-6-deoxyglucose occurs in three sequential ch
124 the subunit-subunit interfaces, and the two dTDP-sugar ligands employed in this study bind to the pr
126 tion of the second sugar to the chain, using dTDP-L-2-deoxyfucose and rhodosaminyl aklavinone, to cre
127 to that of wt, in contrast to turnover using dTDP-glucose where differences in rates of up to 2 order
130 ip between dGDP and both dGTP, dGMP, whereas dTDP appears to have a mixed type of inhibition of dTMP
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