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 the donor substrate used in multiple glyco

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

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

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

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

12 tein still cross-linked the radioactive N(3)-UDP-GlcNAc although not nearly as well as the wild type.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

56 ixed endpoint fluorometric method to analyze UDP-GlcNAc.

57 d Cap5O was assessed by incubating Cap5P and UDP-GlcNAc (to produce UDP-ManNAc), together with Cap5O,

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

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

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

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

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

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

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

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

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

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

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

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

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

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

72 can be prepared from commercially available UDP-GlcNAc by enzymatic conversion to UDP-MurNAc, which

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

74 tudied here, each of which nonetheless binds UDP-GlcNAc.

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

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

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

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

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

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

81 pletely eliminated UDP-GalNAc synthesis, but UDP-GlcNAc was only diminished by 50%.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

100 in the peptide almost completely eliminated UDP-GlcNAc and UDP-GalNAc synthesis, while mutation of G

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

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

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

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

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

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

107 diphosphate-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) by cytidine monophosphate-N-acet

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

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

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

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

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

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

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

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

116 1.2 microM for Nup 62; K(m) = 0.5 microM for UDP-GlcNAc) are nearly identical to purified mammalian O

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

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

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

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

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

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

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

124 inant OGT has three distinct K(m) values for UDP-GlcNAc and that UDP-GlcNAc concentrations modulates

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

152 the conversion of UDP-N-acetyl glucosamine (UDP-GlcNAc) to UDP-N-acetylmannosamine (UDP-ManNAc).

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

154 6-dehydration of UDP-N-acetyl-d-glucosamine (UDP-GlcNAc) to UDP-2-acetamido-2,6-dideoxy-d-xylo-4-hexu

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

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

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

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

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

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

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

162 an Escherichia coli rffE mutant defective in UDP-GlcNAc 2-epimerase activity.

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

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

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

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

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

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

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

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

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

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

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

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

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

176 assay condition, the decrease in k(cat)/K(m,UDP-GlcNAc) mainly reflects an increased K(m,UDP-GlcNAc)

177 activity corresponds to decreased k(cat)/K(m,UDP-GlcNAc) values for all the mutants.

178 UDP-GlcNAc) mainly reflects an increased K(m,UDP-GlcNAc).

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

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

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

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

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

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

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

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

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

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

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

190 The availability of UDP-GlcNAc correlates with glycosylation levels of intra

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

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

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

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

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

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

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

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

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

200 g the PKA activation results in depletion of UDP-GlcNAc for O-glycosylation.

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

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

203 5 protein catalyzed the C-2 epimerization of UDP-GlcNAc, and the MMP0706 protein used NAD(+) to oxidi

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

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

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

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

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

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

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

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

212 GT is exquisitely regulated by the levels of UDP-GlcNAc within the nucleus and cytoplasm.

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

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

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

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

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

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

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

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

221 Redundancy of UDP-GlcNAc 2-epimerase function in S. aureus was demonst

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

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

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

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

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

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

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

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

230 ia coli, the human enzyme can also turn over UDP-GlcNAc to UDP-GalNAc and vice versa.

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

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

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

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

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

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

237 ylyltransferase reaction with UTP to produce UDP-GlcNAc.

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

239 -6-P in addition to the pathway end product, UDP-GlcNAc.

240 to GlcNAc-1-PO(4) to form the final products UDP-GlcNAc and pyrophosphate.

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

242 iochemical characterization of a recombinant UDP-GlcNAc 2-epimerase encoded by S. aureus cap5P.

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

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

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

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

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

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

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

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

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

252 by GlcNAc-P-P-dolichol toward the substrate UDP-GlcNAc and non-competitive inhibition toward dolicho

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

254 istoyl)-GlcNAc and an alternative substrate, UDP-GlcNAc, demonstrates that the ester-linked R-3-hydro

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

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

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

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

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

260 id protein (57 kDa protein) also synthesizes UDP-GlcNAc at about 25% the rate of UDP-GalNAc.

261 distinct K(m) values for UDP-GlcNAc and that UDP-GlcNAc concentrations modulates the affinity of OGT

262 Previously, we reported that UDP-GlcNAc: Galbeta1-3GalNAcalphaRbeta1-6-N-acetylglucos

263 The UDP-GlcNAc glycosyltransferase catalyzing the second sug

264 e reduced affinity of GlcNAc-TI for both the UDP-GlcNAc and Man(5)GlcNAc(2)Asn substrates.

265 viously characterized MNN2 gene encoding the UDP-GlcNAc Golgi transporter.

266 ously shown to contain the gene encoding the UDP-GlcNAc transporter; transformants were isolated, and

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

293 ure of Escherichia coli GlmU in complex with UDP-GlcNAc and CoA has been determined to 2.1 A resoluti

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

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

296 a broad area influence the interaction with UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosph

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 way, the reaction of dolichol phosphate with UDP-GlcNAc to form N-acetylglucosaminylpyrophosphoryldol

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