ライフサイエンスコーパス: UDP-GlcNAc

1 UDP-GlcNAc 2-epimerase and GlcNAc 2-epimerase are two en

2 UDP-GlcNAc 2-epimerase enzymes have been shown to be req

3 UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) catalyzes the

4 UDP-GlcNAc acyltransferase (LpxA) catalyzes the first st

5 UDP-GlcNAc and UDP-ManNAcA biosynthesis evolved early in

6 UDP-GlcNAc is also utilized as substrate for the glycosy

7 UDP-GlcNAc is one such metabolite that acts as a substra

8 UDP-GlcNAc is the donor substrate used in multiple glyco

9 UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase

10 UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

11 UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

12 UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

13 diolabeled [3H]UDP-N-acetylglucosaminyl ([3H]UDP-GlcNAc).

14 rnative methods to rapidly separate free [3H]UDP-GlcNAc from 3H-p62ST acceptor peptide (trichloroacet

15 oli indicated that it does not function as a UDP-GlcNAc/UDP-GalNAc epimerase.

16 he (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved

17 n GPI anchors indicated that TbGT8 encodes a UDP-GlcNAc: beta-Gal-GPI beta1-3 GlcNAc transferase.

18 st, key catalytic domain residues and even a UDP-GlcNAc oxygen important for Ser/Thr glycosylation ar

19 recently shown, unexpectedly, to occur in a UDP-GlcNAc-dependent fashion within the transferase acti

20 nd GlcNAc2 as well, as GlcNAc acceptors in a UDP-GlcNAc-dependent glycosyltransfer reaction.

21 and CD II, contribute to the formation of a UDP-GlcNAc-binding pocket that catalyzes the transfer of

22 ticular, the E. coli encoded WecA protein, a UDP-GlcNAc: undecaprenylphosphate GlcNAc-1-phosphate tra

23 t Pel-dependent biofilm formation requires a UDP-GlcNAc C4-epimerase that generates the UDP-GalNAc pr

24 Transformation of these strains with a UDP-GlcNAc transporter and screening of a GnTI leader fu

25 ferase motif with alanine residues abolished UDP-GlcNAc binding and lymphostatin activity, although o

26 UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first s

27 UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first s

28 ized facilitator of UDP-N-acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc) t

29 ith uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) as a starting point, two enzymes of the gene

30 preferably utilizes UDP-N-acetylglucosamine (UDP-GlcNAc) as a sugar donor.

31 c pathway, increase UDP-N-acetylglucosamine (UDP-GlcNAc) availability, and lead to modification of cy

32 nds uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) but not UDP-glucose (UDP-Glc).

33 s a uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) C4 epimerase, only the second microbial enzy

34 d to be involved in UDP-N-acetylglucosamine (UDP-GlcNAc) donor specificity.

35 tes uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) for glycan synthesis and O-linked GlcNAc (O-

36 he sugar nucleotide UDP-N-acetylglucosamine (UDP-GlcNAc) is an essential metabolite in both prokaryot

37 Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) is the donor sugar substrate for OGT and its

38 The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modi

39 the HBP metabolite UDP-N-acetylglucosamine (UDP-GlcNAc) to CRPC-like cells significantly decreases c

40 tylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to serines and threonines of cytoplasmic, nu

41 ogenase, converting UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetyl-glucosaminuronic acid (UDP-G

42 g the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylglucosaminuronic acid (UDP-Gl

43 of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), a key precursor of LacNAc synthesis.

44 nal modification is UDP-N-acetylglucosamine (UDP-GlcNAc), a product of the hexosamine biosynthesis pa

45 of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a substrate for cellular glycosyltransferas

46 alactose (UDP-Gal), UDP-N-acetylglucosamine (UDP-GlcNAc), and UDP-glucuronic acid.

47 te uridine diphosphoryl-N-acetylglucosamine (UDP-GlcNAc), namely, a metal-binding site and glycosyl o

48 r, uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), to the 6 position of the alpha-1-6 linked M

49 or, uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), was monitored by recording mass spectra wit

50 ith the cosubstrate UDP-N-acetylglucosamine (UDP-GlcNAc),O-linked-GlcNAc transferase (OGT) catalyzes

51 cid (UDP-GlcUA) and UDP-N-acetylglucosamine (UDP-GlcNAc).

52 of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc).

53 ize uridine diphosphate N-acetylglucosamine (UDP-GlcNAc).

54 ase uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc).

55 nits in place of glucosamine, do not acylate UDP-GlcNAc.

56 E. coli LpxA acylates UDP-GlcNAc and UDP-GlcNAc3N at comparable rates in vitro

57 Using the method of standard addition, UDP-GlcNAc concentrations were measured in deproteinized

58 Thus, this Alg13-Alg14 UDP-GlcNAc transferase represents an unprecedented examp

59 pe N-glycan branching was impaired, although UDP-GlcNAc transport into Golgi vesicles was not decreas

60 ixed endpoint fluorometric method to analyze UDP-GlcNAc.

61 s and uses cytosolic UDP-glucuronic acid and UDP-GlcNAc as substrates.

62 s found to activate glutamine catabolism and UDP-GlcNAc-associated modules.

63 The K(m) values for UDP-GalNAc and UDP-GlcNAc are 131 microM and 137 microM, respectively.

64 it strongly reduced cellular UDP-GalNAc and UDP-GlcNAc pools.

65 erpart, can also interconvert UDP-GalNAc and UDP-GlcNAc.

66 Recently, cellular release of UDP-Glc and UDP-GlcNAc has been reported, but whether additional UDP

67 Gal and abnormally low levels of UDP-Glc and UDP-GlcNAc in the presence of galactose and that human G

68 s in the complex structures with UDP-Glc and UDP-GlcNAc.

69 uronan synthase (HAS) utilizes UDP-GlcUA and UDP-GlcNAc in the presence of Mg(2+) to form the GAG hya

70 hat utilizes UDP-glucuronic acid (GlcUA) and UDP-GlcNAc to synthesize HA.

71 abbit GlcNAc-TI complexed with manganese and UDP-GlcNAc.

72 mice, as well as glycolytic metabolites and UDP-GlcNAc levels in liver.

73 f the interaction was dependent on Mgat5 and UDP-GlcNAc levels.

74 e of human epimerase complexed with NADH and UDP-GlcNAc.

75 Coexpression of SAS and UDP-GlcNAc 2-epimerase/ManNAc kinase, the bifunctional e

76 rbon tunicamine sugar motif from uridine and UDP-GlcNAc via uridine-5'-aldehyde and UDP-4-keto-6-ene-

77 losed the following: (i) all variants act as UDP-GlcNAc/UMP antiporters; (ii) conservative substituti

78 ate a LC-MS method that assesses HBP flux as UDP-GlcNAc ((13)C)-molar percent enrichment (MPE) and co

79 EcLpxA does not discriminate between UDP-GlcNAc and UDP-GlcNAc3N; however, E. coli does not m

80 hat PelX catalyzes the epimerization between UDP-GlcNAc and UDP-GalNAc.

81 limiting enzyme of sialic acid biosynthesis, UDP-GlcNAc 2-epimerase/ManNAc kinase.

82 Gne can catalyze the interconversion of both UDP-GlcNAc/GalNAc and UDP-Glc/Gal almost equally well.

83 e activity of wtOGT and OGT(C917A) with both UDP-GlcNAc and UDP-GlcNDAz.

84 ide chain against the uracil moiety of bound UDP-GlcNAc in the X-ray structure of Chlamydia trachomat

85 that makes critical interactions with bound UDP-GlcNAc and Mn(2+) ion in rabbit GlcNAc-TI.

86 a recent 3.0-A structure of LpxA with bound UDP-GlcNAc.

87 GFAT2 was modestly inhibited (15%) by UDP-GlcNAc but not through detectable O-glycosylation.

88 cific recognition of lysosomal hydrolases by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

89 ltransferase-catalyzed reactions mediated by UDP-GlcNAc:GlcNAc-P-P-Dol N-acetylglucosaminyltransferas

90 sphorylation of N-linked oligosaccharides by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

91 s purified and shown to efficiently catalyze UDP-GlcNAc oxidation, forming one NADH equivalent.

92 In SLC35A3-knockout HEK293T cells, UDP-GlcNAc transport was significantly decreased but not

93 h-throughput analysis of changes in cellular UDP-GlcNAc concentrations in time series experiments or

94 coli O86:B7 to those of other characterized UDP-GlcNAc/Glc 4-epimerases indicated that it has relaxe

95 ly the BAS5304-encoded protein could convert UDP-GlcNAc to UDP-GalNAc, indicating that BAS5304 was th

96 even different enzymes that together convert UDP-GlcNAc to CMP-pseudaminic acid.

97 s of the reaction showed that WbpM converted UDP-GlcNAc completely to what was shown to be its 4-keto

98 alic acid biosynthetic pathway by converting UDP-GlcNAc to N-acetylmannosamine are described in this

99 ty of SLC35A2 has been clearly demonstrated, UDP-GlcNAc delivery by SLC35A3 is not fully understood.

100 curs via nucleophilic attack of deprotonated UDP-GlcNAc on the acyl donor in a general base-catalyzed

101 pimerase assay, Lec3 cells had no detectable UDP-GlcNAc 2-epimerase activity, and Lec3 cells grown in

102 ains strongly bound NADP(+) and has distinct UDP-GlcNAc 4-oxidase, 5,6-dehydratase, and 4-reductase a

103 n mutant and that BRE-5 encodes the dominant UDP-GlcNAc:Man GlcNAc transferase activity in C. elegans

104 ine (GlcNAc) from the nucleotide sugar donor UDP-GlcNAc to serine or threonine residues of protein su

105 Escherichia coli hydrolyzed the sugar donor, UDP-GlcNAc, while the mutant OGTs that did not fully res

106 , ED(50) = 80 microm) could markedly elevate UDP-GlcNAc levels without increasing GlcN-6-P levels or

107 Only a Gne cDNA encoding UDP-GlcNAc 2-epimerase:ManNAc kinase rescued PSA synthes

108 specific knockout of the Mgat2 gene encoding UDP-GlcNAc:alpha-6-d-mannoside beta-1,2-N-acetylglucosam

109 d for the multistep conversion of endogenous UDP-GlcNAc to CMP-Neu5Ac.

110 NGc, which might compete with the endogenous UDP-GlcNAc for the sialic acid biosynthetic pathway.

111 by the inhibition of the bifunctional enzyme UDP-GlcNAc-2-epimerase/ManNAc kinase.

112 The Golgi enzyme UDP-GlcNAc:lysosomal enzymeN-acetylglucosamine-1-phospho

113 Yeast mutants lacking Yea4 (the ER UDP-GlcNAc transporter endogenously expressed in Sacchar

114 lase (UAP) is the final enzyme in eukaryotic UDP-GlcNAc biosynthesis, converting UTP and N-acetylgluc

115 Escherichia coli, recombinant GnT51 exhibits UDP-GlcNAc:hydroxyproline Skp1 GlcNAc-transferase activi

116 ly corrected UDP-Glc and, to a lesser extent UDP-GlcNAc depletion, enabled ldlD cells to proliferate

117 We describe the synthesis of two fluorescent UDP-GlcNAc analogues and their evaluation as chitin synt

118 nd approximately 20-fold higher affinity for UDP-GlcNAc than MGAT5, respectively, and increasing MGAT

119 A sensitive and highly selective assay for UDP-GlcNAc mass was developed using purified AGX2, an is

120 The genes for UDP-GlcNAc-2-epimerase/ManNAc kinase (EK), sialic acid 9

121 detection in negative mode was optimized for UDP-GlcNAc, UDP-MurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-A

122 ions in the de novo biosynthetic pathway for UDP-GlcNAc.

123 -acetylglucosamine (GlcNAc), a precursor for UDP-GlcNAc, to the media increased the levels of CMP-Neu

124 Roles for UDP-GlcNAc 2-epimerase/ManNAc 6-kinase (GNE) beyond cont

125 i (EcLpxA), an acyltransferase selective for UDP-GlcNAc and R-3-hydroxymyristoyl-acyl carrier protein

126 pproximately 2-4 times higher than those for UDP-GlcNAc and UDP-Glc, suggesting that Gne is slightly

127 The K(m) values of TviB for UDP-GlcNAc and NAD(+) are 77 +/- 9 microM and 276 +/- 52

128 by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 muM to over 20 mu

129 way (HBP) branches from glycolysis and forms UDP-GlcNAc, the moiety for O-linked beta-GlcNAc (O-GlcNA

130 ER, which catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the firs

131 Chitin synthases transfer GlcNAc from UDP-GlcNAc to preexisting chitin chains in reactions tha

132 -GlcNAc-T2 efficiently transfers GlcNAc from UDP-GlcNAc to synthetic peptides corresponding to mucin-

133 ansferring N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to N-glycan substrates produced by the sequen

134 ransfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to Ser/Thr residues of proteins.

135 charide beta-N-GlcNAc (O-GlcNAcylation) from UDP-GlcNAc by the enzyme O-GlcNAc transferase.

136 acNAc) units within N-glycans initiated from UDP-GlcNAc by the medial-Golgi branching enzymes as well

137 a-d-glucosaminyl l-malate (GlcN-malate) from UDP-GlcNAc and l-malate.

138 wo enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc, respectively.

139 that catalyzes the formation of ManNAc from UDP-GlcNAc via a 2-acetamidoglucal intermediate.

140 for transferring a single GlcNAc moiety from UDP-GlcNAc to specific serine/threonine residues of hund

141 e polymerization of the monosaccharides from UDP-GlcNAc and UDP-GlcUA.

142 eucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.

143 ond step in the synthesis of UDP-QuiNAc from UDP-GlcNAc.

144 and WbpI) in a stepwise manner starting from UDP-GlcNAc.

145 P-4-amino-sugar was readily synthesized from UDP-GlcNAc in a coupled reaction using PglF and PglE.

146 of the fungal cell wall, is synthesized from UDP-GlcNAc produced in the hexosamine biosynthetic pathw

147 The Km values of Gne for UDP-Glc, UDP-Gal, UDP-GlcNAc, and UDP-GalNAc are 370, 295, 323, and 373 mi

148 TbNST1/2 transports UDP-Gal/UDP-GlcNAc, TbNST3 transports GDP-Man, and TbNST4 transp

149 ed with NADH and UDP-glucose, UDP-galactose, UDP-GlcNAc, or UDP-GalNAc.

150 u5Gc, CMP-KDN, UDP-Gal, UDP-Glc, UDP-GalNAc, UDP-GlcNAc, GDP-Fuc, GDP-Man) and 12 nucleotides (AMP, A

151 , this simple mutation did confer UDP-GalNAc/UDP-GlcNAc converting activity to the bacterial enzyme w

152 mately 2-5% of the total glucose, generating UDP-GlcNAc as the end product.

153 e acetylation of UDP-GlcNAc(3NH(2))A to give UDP-GlcNAc(3NAc)A.

154 glucosamine uridyltransferase (GlmU) to give UDP-GlcNAc/GalNAc.

155 G-and 5 'metabolite' caps-NAD, FAD, UDP-Glc, UDP-GlcNAc, and dpCoA.

156 structures in humans and mice (FAD, UDP-Glc, UDP-GlcNAc, and m7Gpppm6A), cell- and tissue-specific va

157 nucleotide-sugar uridine-diphosphate-GlcNAc (UDP-GlcNAc) by deletion of the essential gene GNA1.

158 he condensation of UDP-N-acetyl glucosamine (UDP-GlcNAc) and phosphoenolpyruvate catalyzed by UDP-N-a

159 e uridine 5'-diphospho-N-acetyl-glucosamine (UDP-GlcNAc) pathway, which provides intermediates for pe

160 uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc) in human prostate cancer LnCaP-LN3 cells, we

161 6-dehydration of UDP-N-acetyl-d-glucosamine (UDP-GlcNAc) to UDP-2-acetamido-2,6-dideoxy-d-xylo-4-hexu

162 uridine diphosphate N-acetyl-D-glucosamine (UDP-GlcNAc), forming a 3-hexulose sugar nucleotide.

163 ivity is seen with ADP-glucose, UDP-glucose, UDP-GlcNAc, or UDP-galactose.

164 GNE (UDP-GlcNAc 2-epimerase/ManNAc kinase) myopathy is a rare

165 d using purified AGX2, an isoenzyme of human UDP-GlcNAc pyrophosphorylase.

166 The human UDP-GlcNAc transporter HFRC1 was overexpressed in human

167 UCE also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyl

168 ) and gneZ (BAS5117) encode nearly identical UDP-GlcNAc 2-epimerase enzymes that catalyze the reversi

169 titutions (E47D, E47Q, K50R, or K50H) impair UDP-GlcNAc uptake; and (iii) substitutions of Glu-47 and

170 onjugates than WT cells, indicating impaired UDP-GlcNAc transport activity of these two variants.

171 e previously reported that mice deficient in UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase

172 served a concentration-dependent increase in UDP-GlcNAc levels and MPE, with the latter reaching a pl

173 ile and that Cys301 has an important role in UDP-GlcNAc binding by Gpi3ps.

174 tation is a novel mechanism for inactivating UDP-GlcNAc 2-epimerase activity.

175 e even in the presence of GlcN and increased UDP-GlcNAc.

176 Ac modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylat

177 As expected, GlcN and glucose increased UDP-GlcNAc levels (t((1/2)) approximately 14-18 min), bu

178 Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, inc

179 bility of the E. coli enzyme to interconvert UDP-GlcNAc and UDP-GalNAc.

180 of UDP-Gal into UDP-Glc and UDP-GalNAc into UDP-GlcNAc with the same level of activity that is requi

181 h, converting D-glucosamine 1-phosphate into UDP-GlcNAc via acetylation and subsequent uridyl transfe

182 et al. report that increasing intracellular UDP-GlcNAc leads to increased branching of N-glycans, in

183 The method enabled mapping the (13)C-labeled UDP-GlcNAc in fungal mycelium and recording its redistri

184 ation and relative placement of its ligands, UDP-GlcNAc and beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->

185 inhibits beta1,6GlcNAc branching by limiting UDP-GlcNAc supply to MGAT5, suggesting that restricted c

186 x and hybrid N-glycosylation requires MGAT1 (UDP-GlcNAc:alpha-3-D-mannoside-beta1,2-N-acetylglucosami

187 rocedure had a detection limit of 0.2 microM UDP-GlcNAc in a 1-ml sample.

188 zymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), to

189 are engineered to produce diazirine-modified UDP-GlcNAc (UDP-GlcNDAz), and the diazirine-modified Glc

190 residues involved in the activity of a mouse UDP-GlcNAc transporter, murine solute carrier family 35

191 ee ternary complex forms: NAD(+)/UDP, NAD(+)/UDP-GlcNAc, and NAD(+)/UDP-Glc.

192 Lec3 mutants with no UDP-GlcNAc 2-epimerase activity represent sensitive host

193 can interconvert UDP-Glc and UDP-Gal but not UDP-GlcNAc and UDP-GalNAc.

194 competitive with respect to acyl-ACP but not UDP-GlcNAc.

195 ll incorporated in patches in the absence of UDP-GlcNAc.

196 nfirm that WbpD catalyzes the acetylation of UDP-GlcNAc(3NH(2))A to give UDP-GlcNAc(3NAc)A.

197 t the enzyme also catalyzes the acylation of UDP-GlcNAc at a slow rate.

198 or R-3-hydroxylauroyl-ACP and an analogue of UDP-GlcNAc, designated UDP-GlcNAc3N, in which NH(2) repl

199 ated cells serves to enhance availability of UDP-GlcNAc to MGAT5.

200 e to accommodate the N-acetyl group on C2 of UDP-GlcNAc so that the anomeric carbon atom (C1) is opti

201 ely 50% lower intracellular concentration of UDP-GlcNAc and conferred a fivefold increase in the leve

202 hat a reduction in cellular concentration of UDP-GlcNAc and the resulting increased expression of Rra

203 d T cells contained higher concentrations of UDP-GlcNAc and increased intracellular protein O-GlcNAcy

204 and High Five cells showed concentrations of UDP-GlcNAc, UDP-Gal, UDP-Glc, GDP-Fuc, and GDP-Man equal

205 o fluctuations in cellular concentrations of UDP-GlcNAc, which result from nutrients entering the hex

206 s that catalyze the reversible conversion of UDP-GlcNAc and UDP-ManNAc.

207 mbiguously the dual enzymatic conversions of UDP-GlcNAc to UDP-GlcNAcA and subsequently to UDP-XylNAc

208 Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O

209 S synthesis by inhibiting 4-epimerization of UDP-GlcNAc to UDP-GalNAc, thereby depleting one of the s

210 5 protein catalyzed the C-2 epimerization of UDP-GlcNAc, and the MMP0706 protein used NAD(+) to oxidi

211 fied O-GlcNAc by expressing a mutant form of UDP-GlcNAc pyrophosphorylase and subsequently culturing

212 GlcNAc, in the form of UDP-GlcNAc, and galactose, as UDP-Gal, are delivered int

213 ase, interacts with the 3'-hydroxyl group of UDP-GlcNAc to generate the nucleophile.

214 e acylation of the glucosamine 3-OH group of UDP-GlcNAc, using R-3-hydroxymyristoyl-acyl carrier prot

215 ier protein to the glucosamine 3-OH group of UDP-GlcNAc.

216 carrier protein to the 3'-hydroxyl group of UDP-GlcNAc.

217 otein (ACP) to the glucosamine 3-OH group of UDP-GlcNAc.

218 l carrier protein (ACP) to the 3-OH group of UDP-GlcNAc.

219 ugh the enzyme facilitated the hydrolysis of UDP-GlcNAc.

220 lcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.

221 GNE deficiency may affect levels of UDP-GlcNAc, a key metabolite in the nutrient-sensing hex

222 of Neu5Ac to CMP-Neu5Ac at higher levels of UDP-GlcNAc.

223 c transporter and/or different mechanisms of UDP-GlcNAc transport into the Golgi apparatus may exist.

224 pendent oxidation of the glucosamine 3-OH of UDP-GlcNAc, and the 369-residue GnnB protein was propose

225 this catalytically productive orientation of UDP-GlcNAc but allows a more optimal alignment of UDP-Gl

226 initiated by the TviB-catalyzed oxidation of UDP-GlcNAc to UDP-GalNAc, followed by the TviC-catalyzed

227 ns-Golgi network may ensure that the pool of UDP-GlcNAc in the Golgi stack is not depleted, thereby m

228 both derived from the same metabolic pool of UDP-GlcNAc, without significant differential metabolic p

229 brium reaction resulting in a 70:30 ratio of UDP-GlcNAc to uridine diphosphate-N-acetylgalactosamine

230 Robust constitutive release of UDP-GlcNAc was observed in yeast as well as in well diff

231 e and hypotonic stress-stimulated release of UDP-GlcNAc.

232 ed by mutations in the alphabeta subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

233 cted by the lack of ROCK1-mediated supply of UDP-GlcNAc.

234 ucose and glutamine for de novo synthesis of UDP-GlcNAc, a sugar-nucleotide that inhibits receptor en

235 s and studied the mitochondrial transport of UDP-GlcNAc.

236 ce of UGT3A1 is necessary for utilization of UDP-GlcNAc.

237 Other UDP-GlcNAc/GalNAc analogues can also be prepared dependi

238 required for the conversion of [alpha-(32)P]UDP-GlcNAc to a novel, less negatively charged sugar nuc

239 ent sensing hexosamine biosynthetic pathway, UDP-GlcNAc, as its substrate donor.

240 of hGFAT1 by the end product of the pathway, UDP-GlcNAc, was competitive with a K(i) of 4 microm.

241 wn structure such as glycogen phosphorylase, UDP-GlcNAc 2-epimerase, and the glycosyl transferase Mur

242 Chitin synthase (CS) polymerizes UDP-GlcNAc to form chitin (poly-beta(1,4)-GlcNAc), a key

243 Chitin synthase polymerizes UDP-GlcNAc to form chitin (poly-beta(1,4)-GlcNAc) and is

244 suggest that SLC35A3 may not be the primary UDP-GlcNAc transporter and/or different mechanisms of UD

245 ylyltransferase reaction with UTP to produce UDP-GlcNAc.

246 tor pyridoxal 5'-phosphate (PLP) and product UDP-GlcNAc(3NH(2))A as the external aldimine at 1.9 A re

247 -6-P in addition to the pathway end product, UDP-GlcNAc.

248 strates of Eogt, that mutation of a putative UDP-GlcNAc binding DXD motif greatly reduces enzyme acti

249 sis and glutaminolysis co-operatively reduce UDP-GlcNAc biosynthesis and N-glycan branching in mouse

250 in Saccharomyces cerevisiae) showed reduced UDP-GlcNAc release.

251 formation of spores in mother cells required UDP-GlcNAc 2-epimerase activity.

252 The structure revealed that PelX resembles UDP-GlcNAc C4-epimerases.

253 w that it encodes a Golgi apparatus resident UDP-GlcNAc:alpha3-D-mannoside beta1-2-N-acetylglucosamin

254 of endoplasmic reticulum (ER)/Golgi-resident UDP-GlcNAc transporters to the cellular release of their

255 rsor despite detection of only this enzyme's UDP-GlcNAc hydrolase activity.

256 eficient cells complemented with Yea4 showed UDP-GlcNAc release rates at levels similar to or higher

257 of the enzyme in complex with its substrate UDP-GlcNAc at 2.8 A resolution.

258 se WbpM had acted on the precursor substrate UDP-GlcNAc.

259 ion, which was assigned a role in substrate (UDP-GlcNAc) binding.

260 sis of the nucleotide sugar donor substrate, UDP-GlcNAc, with the resulting generation of UMP, a pote

261 li MurG in complex with its donor substrate, UDP-GlcNAc.

262 nzyme (wtOGT) prefers the natural substrate, UDP-GlcNAc, over the unnatural UDP-GlcNDAz.

263 t it only polymerizes the native substrates, UDP-GlcNAc and UDP-GlcUA.

264 ors for the hexosamine pathway that supplies UDP-GlcNAc for synthesis of complex oligosaccharides.

265 The UDP-GlcNAc glycosyltransferase catalyzing the second sug

266 imilar approaches, we identified WbmV as the UDP-GlcNAc transferase and noted that WbmW represents a

267 hat coordinates a Mg(2+) ion for binding the UDP-GlcNAc sugar donor.

268 d effect on catalysis when inserted into the UDP-GlcNAc donor, with the UDP(5-F)-GlcNAc serving as a

269 Saccharomyces cerevisiae Gpi3p is the UDP-GlcNAc-binding and presumed catalytic subunit of the

270 nally, we identify several residues near the UDP-GlcNAc-binding site, which are specifically permissi

271 Modeling of the UDP-GlcNAc donor supports a direct displacement invertin

272 hibits the human ManNAc kinase domain of the UDP-GlcNAc-2-epimerase/ManNAc kinase.

273 fects enzyme activity and is proximal to the UDP-GlcNAc binding site.

274 in the second Rossmann domain points to the UDP-GlcNAc donor binding site.

275 s to increased GlcNH(2) 6-phosphate and then UDP-GlcNAc levels.

276 acetylglucosamine-1-phosphate (GlcNAc-1P) to UDP-GlcNAc.

277 ransferase pair that converts UDP-GlcNAcA to UDP-GlcNAc(3NH(2))A in a coupled reaction via a unique N

278 at5 expression and GlcNAc supplementation to UDP-GlcNAc, the donor substrate shared by Mgat branching

279 T cells is dependent on metabolite supply to UDP-GlcNAc biosynthesis (hexosamine pathway) and in turn

280 te, which are specifically permissive toward UDP-GlcNAc utilization.

281 vitro assay, we showed that TbGnTI transfers UDP-GlcNAc to biantennary Man3GlcNAc2, but not to triant

282 r, pyrimidine nucleotide carrier, transports UDP-GlcNAc from the cytosol to the inside of the mitocho

283 T3 transports GDP-Man, and TbNST4 transports UDP-GlcNAc, UDP-GalNAc, and GDP-Man.

284 Our results indicate that, unlike UDP-GlcNAc 2-epimerase, which promotes biosynthesis of s

285 ion is triggered by redistribution of unused UDP-GlcNAc from the medial to trans-Golgi via inter-cist

286 hown to undergo a conformational change upon UDP-GlcNAc binding, the kinetic data are inconsistent wi

287 rom two non-human primates were found to use UDP-GlcNAc, whereas UGT3A isoforms from non-primates cou

288 c and completely inhibits its ability to use UDP-GlcNAc.

289 transgenic overexpression of an enzyme using UDP-GlcNAc to modify proteins with O-GlcNAc produces the

290 rate analog for diverse enzymes that utilize UDP-GlcNAc.

291 O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis,

292 ed with a rat Gne cDNA had restored in vitro UDP-GlcNAc 2-epimerase activity and cell surface PSA exp

293 In an in vitro UDP-GlcNAc 2-epimerase assay, Lec3 cells had no detectab

294 cNAcase) this sugar or by loading cells with UDP-GlcNAc.

295 ure of Escherichia coli LpxA in complex with UDP-GlcNAc reveals details of the substrate-binding site

296 osaccharides were efficiently elongated with UDP-GlcNAc as the donor substrate, confirming that CsaA

297 termination but rather by interference with UDP-GlcNAc synthesis.

298 Similarly, cells loaded with UDP-GlcNAc had an attenuated response to uncaging of Ins

299 N-acetylglucosaminyltransferase (Mgat4) with UDP-GlcNAc.

300 and catalytic domains, which, together with UDP-GlcNAc, are required for both glycosylation and prot