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1 phate + UDP-glucose to glucose-1-phosphate + UDP-galactose.
2 dent upon the addition of both manganese and UDP-galactose.
3 th ADP-glucose, GDP-mannose, UDP-glucose, or UDP-galactose.
4 everely impair the enzyme's activity against UDP-galactose.
5 ly correlated with residual activity against UDP-galactose.
6 accumulation of the intermediary metabolite UDP-galactose.
7 ited an atypical concentration dependence on UDP-galactose.
8 en determined of a complex containing intact UDP-galactose.
9 degrees C with or without pretreatment with UDP-galactose.
10 ith ADP-glucose, UDP-glucose, UDP-GlcNAc, or UDP-galactose.
17 galactosemia results from the impairment of UDP-galactose 4'-epimerase (GALE), the third enzyme in t
18 address this knowledge gap, here we examined UDP-galactose 4'-epimerase (GALE), which interconverts t
19 Galactosemia III results from the loss of UDP-galactose 4'-epimerase (GALE), which interconverts U
21 pression of a gene encoding Escherichia coli UDP-galactose 4-epimerase and engineered to facilitate c
22 24, Tyr149, and Lys153 in the active site of UDP-galactose 4-epimerase are located in similar positio
23 richia coli dTDP-glucose 4,6-dehydratase and UDP-galactose 4-epimerase are members of the short-chain
30 meters for epimerization of UDP-galactose by UDP-galactose 4-epimerase from Escherichia coli (GalE),
36 ive site is reminiscent to that observed for UDP-galactose 4-epimerase, an enzyme that plays a key ro
37 mes of the pathway, galactose mutarotase and UDP-galactose 4-epimerase, are contained within a single
38 g of uridine diphosphogalactose 4-epimerase (UDP-galactose 4-epimerase, EC ) and alpha1, 3-galactosyl
39 o the roles of the corresponding residues in UDP-galactose 4-epimerase, which facilitate the ionizati
41 tural comparison of ADP-hep 6-epimerase with UDP-galactose 4-epimerase, which utilizes an NAD(+) cofa
53 in genes encoding phosphoglucomutase (pgm), UDP-galactose-4-epimerase, and two other NTHI sialyltran
56 n effort to prepare an abortive complex with UDP-galactose, a site-directed mutant protein was constr
58 ease of entropy, whereas the weak binding of UDP-galactose and -glucose, which occurred only in D2O s
59 rom sporophytic tissues, F3GalTase uses only UDP-galactose and flavonols to catalyze the formation of
60 with galactose 1-phosphate (Gal-1-P) to form UDP-galactose and glucose 1-phosphate (Glc-1-P) through
61 P-glucose with galactose 1-phosphate to form UDP-galactose and glucose 1-phosphate during normal cell
62 ersion of UDP-glucose and galactose-1-P with UDP-galactose and glucose-1-P by a double-displacement m
63 ose and galactose-1-phosphate (Gal-1-P) into UDP-galactose and glucose-1-phosphate (Glc-1-P) by a dou
64 ate that the cofactor is involved in binding UDP-galactose and has a crucial influence on catalytic e
65 myo-inositol to the reaction, which converts UDP-galactose and myo-inositol to galactinol is a contro
66 in yeast was severely reduced with regard to UDP-galactose and partially reduced with regard to UDP-N
67 consistent with the specificity of SRF-3 for UDP-galactose and strongly suggest that the above glycoc
68 s as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating th
69 4-epimerase catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose me
70 -galactose 4'-epimerase (GALE) interconverts UDP-galactose and UDP-glucose in the final step of the L
72 dylyltransferase is able to accommodate both UDP-galactose and UDP-glucose substrates by simple movem
73 cipates in catalyzing the interconversion of UDP-galactose and UDP-glucose through its redox properti
74 richia coli catalyzes the interconversion of UDP-galactose and UDP-glucose through the transient redu
75 rase (GALE) catalyzes the interconversion of UDP-galactose and UDP-glucose, an important step in gala
76 ose 4'-epimerase (GALE), which interconverts UDP-galactose and UDP-glucose, as well as UDP-N-acetylga
81 relative specificities for the sugar donors UDP-galactose and UDP-glucuronic acid, although UDP-gluc
89 ncoded for by the enzyme glucosyltransferase UDP galactose:beta-D-galactosyl-1, 4-N-acetyl-D-glucosam
90 cNAc-R (alphaGal), synthesized by the enzyme UDP galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosami
91 Here, we asked whether inactivation of the UDP-galactose:beta-galactoside-alpha1-3-galactosyltransf
93 y represents the first direct observation of UDP-galactose binding to epimerase and lends strong stru
94 donor substrate distortion, cleavage of the UDP-galactose bond, galactose transfer, and UDP release.
95 . enterocolitica is not in the production of UDP galactose but, instead, some other nucleotide sugar
96 demonstrated normal activity with respect to UDP-galactose but complete loss of activity with respect
97 tate kinetic parameters for epimerization of UDP-galactose by UDP-galactose 4-epimerase from Escheric
99 kinetic isotope effects for epimerization of UDP-galactose-C-d(7) by these enzymes have also been mea
103 he gene that encodes the biosynthetic enzyme UDP-galactose:ceramide galactosyl transferase (CGT) are
104 P-glucose:ceramide glucosyltransferase or by UDP-galactose:ceramide galactosyltransferase (CGalT).
105 mice lacking the key enzyme to generate GCs, UDP-galactose:ceramide galactosyltransferase (CGT(-/-)),
107 We have generated mice lacking the enzyme UDP-galactose:ceramide galactosyltransferase (CGT), whic
108 l allele of the gene that encodes the enzyme UDP-galactose:ceramide galactosyltransferase (Cgt), whic
109 The structures of the enzyme/UDP-glucose and UDP-galactose complexes, in which the catalytic nucleoph
111 pendent (1-->4)-beta-D-mannan synthase and a UDP-galactose dependent (1-->6)-alpha-D-galactosyltransf
113 s D and D' contain an intact gene encoding a UDP-galactose epimerase (galE1) and a truncated remnant
114 he C-4'' position of sugar nucleotides, like UDP-galactose epimerase, dTDP-glucose-4,6-dehydratase, a
116 reens and identify SLC35A2 (a transporter of UDP-galactose expressed in target cells in blood and muc
117 pyrophosphorylase (UGP) alternatively makes UDP-galactose from uridine triphosphate and galactose-1-
118 curonic acid, UDP-N-acetylgalactosamine, and UDP-galactose (Gal) in a temperature-dependent and satur
119 pholino-1-propanol (D-PDMP), an inhibitor of UDP-galactose:glucosylceramide beta(1-->4)-galactosyltra
120 thesis by way of stimulating the activity of UDP-galactose:glucosylceramide beta(1-->4)-galactosyltra
121 e porcine salivary gland Core 1 transferase (UDP-galactose:glycoprotein-alpha-GalNAc beta3-galactosyl
124 fore interact with one or more phosphates of UDP-galactose in the Michaelis complex and in the transi
125 e specifically defective in the transport of UDP-galactose into the Golgi apparatus and of a mutant o
126 ransporter is rate-limiting in the supply of UDP-galactose into the Golgi lumen; this in turn results
127 CAr) with a 2% residual rate of transport of UDP-galactose into the lumen of Golgi vesicles was descr
128 xtract of the above protist, which transport UDP-galactose into their lumen with a K(m) of 2.7 microm
129 er in Saccharomyces cerevisiae; its K(m) for UDP-galactose is 2.9 microm; (b) characterized vesicles
130 s end, we further show that the galactose in UDP-galactose is incorporated into mature, de novo glyca
131 e (ADPG), kaempferol and UDPG, quercetin and UDP-galactose, isoliquiritigenin and UDPG, and luteolin
132 e intermediates', galactose 1-phosphate <--> UDP-galactose <--> UDP-glucose <--> glucose 1-phosphate
134 T-II encode an alpha-lactalbumin-responsive, UDP-galactose:N-acetylglucosamine beta4-galactosyltransf
136 displayed glycosyltransferase activity from UDP-galactose onto N-acetylgalactosamine but with a low
139 residues with uridine 5'-diphosphogalactose (UDP-galactose) results in the normal survival of short-t
141 the 4'-hydroxyl group of the UDP-glucose or UDP-galactose substrates during the course of the reacti
142 ation occurs about C-4 of the UDP-glucose or UDP-galactose substrates, in the reaction catalyzed by t
143 -P, as well as the levels of UDP-glucose and UDP-galactose, the nucleotide sugars that are required f
145 stead, the enzyme transferred galactose from UDP-galactose to acceptors containing a terminal beta-li
146 GT) catalyzes the transfer of galactose from UDP-galactose to beta-linked galactosides with retention
147 GT) catalyzes the transfer of galactose from UDP-galactose to form an alpha 1-3 link with beta-linked
150 ase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues o
152 ment of alpha1, 3-galactosyltransferase from UDP-galactose to UDP-glucose and decreased the cost for
153 tose 4-epimerase catalyzes the conversion of UDP-galactose to UDP-glucose through a mechanism involvi
154 richia coli, and has been shown to epimerize UDP-galactose to UDP-glucose without the addition of NAD
155 a manganese ion, it transfers galactose from UDP-galactose to xylose on a proteoglycan acceptor subst
156 ar site where galactose is transferred, from UDP-galactose, to the oligosaccharide chains of glycopro
162 (a) cloned and expressed the E. histolytica UDP-galactose transporter in Saccharomyces cerevisiae; i
163 results demonstrate that the Golgi membrane UDP-galactose transporter is rate-limiting in the supply
164 The CMP-sialic acid transporter SLC35A1 and UDP-galactose transporter SLC35A2 are two well-character
165 identified mutations in the Golgi-localized UDP-galactose transporter SLC35A2 that define an undiagn
168 mino acid sequence identity to the mammalian UDP-galactose transporters and 40% to the CMP-sialic aci
169 he YEA4 UDP- N-acetylglucosamine or the HUT1 UDP-galactose transporters, and overexpression of YEA4 o
170 for 48 hours at 4 degrees C and showed that UDP-galactose treatment of murine platelets also did not
171 luorogalactose or the native donor substrate UDP-galactose (UDP-Gal) and several glycan acceptors at
172 G patients had higher UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal) and UDP-Glucuronic levels, lower
173 mplex of a low-activity mutant alpha3GT with UDP-galactose (UDP-gal) exhibiting a bent configuration
174 n, galactose-1-phosphate (gal-1-P) is bound, UDP-galactose (UDP-Gal) is released, and the free enzyme
175 ce of manganese ion transfers galactose from UDP-galactose (UDP-Gal) to N-acetylglucosamine (GlcNAc)
176 n to be either mono-functional, synthesising UDP-galactose (UDP-Gal), or bi-functional, synthesising
177 potently activated by UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal), UDP-N-acetylglucosamine (UDP-Gl
179 Golgi apparatus transporter for UDP-glucose, UDP-galactose, UDP- N-acetylglucosamine, and UDP- N-acet
180 complex containing an inhibitory analogue of UDP-galactose, UDP-2F-galactose, in a complex with the A
182 ly enriched metabolites in colostrum such as UDP-galactose, UDP-glucose play crucial roles in cell gr
183 The multivariate analysis revealed that UDP-galactose, UDP-glucose, citrate, creatine phosphate,
184 ied and quantified the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and
185 umen of the above vesicles with the K(m) for UDP-galactose, using endogenous acceptors, being 93 micr
186 ed, however, in that UDP-glucose rather than UDP-galactose was observed binding in the active site.
187 rt induction was specific as no transport of UDP-galactose was observed even though the latter putati
188 nds uridine 5'-diphosphate (UDP)-glucose and UDP-galactose were enriched in hepatocytes and were rele
189 two reversible reactions: interconversion of UDP-galactose with UDP-glucose and interconversion of UD