ライフサイエンスコーパス: UDP-Glc

1 UDP-Glc also stimulated keratinocyte migration, prolifer

2 UDP-Glc was the preferred hexose donor, but TDP-glucose

3 photoaffinity labeling with azido-[beta-32P]UDP-Glc.

4 A UDP-Glc:glycoprotein glucosyltransferase glucosylates N-

5 beta-Glc, a high-energy molecule formed by a UDP-Glc dependent reaction.

6 Glc(1)Man(5)GlcNAc(2), which is made by a UDP-Glc: glycoprotein glucosyltransferase that is part o

7 sibility, we generated mice overexpressing a UDP-Glc PPL transgene in skeletal muscle.

8 stead, these LpxA acyltransferases require a UDP-Glc-NAc derivative (designated UDP 2-acetamido-3-ami

9 ive beta-glycosyltransferase, and requires a UDP-Glc dehydrogenase for conversion of UDP-Glc to UDP-G

10 catalyzes the interconversion of UDP-Gal and UDP-Glc during normal galactose metabolism.

11 on of the crystal structures of UDP-Gal- and UDP-Glc-bound beta4Gal-T1 reveals that the O4 hydroxyl g

12 nterconversion of both UDP-GlcNAc/GalNAc and UDP-Glc/Gal almost equally well.

13 elative binding orientations of UDP-Galp and UDP-Glc were compared using saturation transfer differen

14 4 times higher than those for UDP-GlcNAc and UDP-Glc, suggesting that Gne is slightly more efficient

15 regulated by two enzymes, glucosidase II and UDP-Glc:glycoprotein:glycosyltransferase (GT), which cyc

16 Specificity of binding to UDP and UDP-Glc indicates a properly folded protein, and binding

17 ar, we observed a strong correlation between UDP-Glc concentration and the development of AKI in card

18 in the hydrogen bonding interactions between UDP-Glc and Gal-T1.

19 structure is isomorphous to our previous BGT UDP-Glc structure.

20 fragment that spans these domains and binds UDP-Glc, while a similar fragment having one of these do

21 The transgene increased both UDP-Glc PPL activity and levels of UDP-Glc in skeletal m

22 to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase.

23 blocked the induction of HAS2 expression by UDP-Glc, the latter inhibitor suggesting that the signal

24 lypeptide (RGP1) that can be glycosylated by UDP-Glc, UDP-Xyl, or UDP-Gal, and isolated a cDNA encodi

25 UDP-GlcUA-actuated release was inhibited by UDP-Glc with an approximate K(i) of 5 micrometer.

26 Arabidopsis AtUGlcAE1 is not inhibited by UDP-Glc, UDP-Gal, or UMP.

27 The enzyme was competitively inhibited by UDP-Glc, with a Ki of 733 microM.

28 , we discuss its proposed role in channeling UDP-Glc to cellulose synthase during secondary wall depo

29 ical data however, shows that BGT can cleave UDP-Glc in the absence of DNA acceptor, which probably a

30 ic amino-terminal portion of HUGT1 conferred UDP-Glc binding and transfer of glucose that was specifi

31 ystals grown in ammonium sulphate containing UDP-Glc.

32 supplementation, which essentially corrected UDP-Glc and, to a lesser extent UDP-GlcNAc depletion, en

33 ct on UDP-Glc in Type I fibers but decreased UDP-Glc by 35-40% in Type IIA/D and Type IIB fibers.

34 am enzymes (UDP-glucose [Glc] dehydrogenase, UDP-Glc pyrophosphorylase, and UDP-GlcA decarboxylase) a

35 to the increase of specific UDP-derivatives (UDP-Glc, UDP-Gal and UDP-Glucuronic), also potentially e

36 cleotides, e.g. uridine 5'-diphosphoglucose (UDP-Glc), but the metabolic pathways that produce sugar-

37 glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-st

38 e of enzyme-bound polysaccharide when either UDP-Glc or UDP-GlcUA alone was present in the reaction.

39 two genes, UGT80A2 and UGT80B1, that encode UDP-Glc:sterol glycosyltransferases, enzymes that cataly

40 nosoma brucei and is initiated by the enzyme UDP-Glc 4'-epimerase.

41 he present study, we overproduced the enzyme UDP-Glc pyrophosphorylase to test whether the overproduc

42 new cap structures in humans and mice (FAD, UDP-Glc, UDP-GlcNAc, and m7Gpppm6A), cell- and tissue-sp

43 2,2,7GpppG-and 5 'metabolite' caps-NAD, FAD, UDP-Glc, UDP-GlcNAc, and dpCoA.

44 , a phenylalanine (Phe-391) in UGT3A2 favors UDP-Glc use.

45 N-glycan-dependent QC of folding (UDP-Glc:glycoprotein glucosyltransferase, calreticulin,

46 The Km values of Gne for UDP-Glc, UDP-Gal, UDP-GlcNAc, and UDP-GalNAc are 370, 29

47 acid (UDP-GlcA) and display specificity for UDP-Glc.

48 or substrate is reduced 30-fold, whereas for UDP-Glc it is reduced only 5-fold.

49 osphate (GCP) was proposed to be formed from UDP-Glc breakdown and subsequently transferred, thus pro

50 ck the epimerase to make UDP-Gal/GalNAc from UDP-Glc/GlcNAc.

51 (Gal-T activity) and also transfers Glc from UDP-Glc to GlcNAc (Glc-T activity), albeit at only 0.3%

52 It also transfers glucose (Glc) from UDP-Glc to GlcNAc, constituting the glucosyltransferase

53 ramide synthase (GCS) transfers glucose from UDP-Glc to ceramide, catalyzing the first glycosylation

54 no electron density for the Glc moiety from UDP-Glc similar to previous observations.

55 cus pneumoniae catalyzes sugar transfer from UDP-Glc and UDP-glucuronic acid (GlcUA) to a polymer wit

56 es catalyze the formation of xyloglucan from UDP-Glc and UDP-Xyl by cooperative action of alpha-xylos

57 tion in complex with natural donors UDP-Gal, UDP-Glc and, in an attempt to overcome one of the common

58 howed concentrations of UDP-GlcNAc, UDP-Gal, UDP-Glc, GDP-Fuc, and GDP-Man equal to or higher than th

59 s (CMP-Neu5Ac, CMP-Neu5Gc, CMP-KDN, UDP-Gal, UDP-Glc, UDP-GalNAc, UDP-GlcNAc, GDP-Fuc, GDP-Man) and 1

60 bited enzyme activity, including UDP-GalNAc, UDP-Glc, UDP-Gal, UDP-GalUA, UMP, UDP, and UTP.

61 Uridine-5'-diphospho-1-alpha-d-glucose (UDP-Glc) is a common substrate used by glucosyltransfera

62 alyze the conversion of UDP-alpha-d-glucose (UDP-Glc) to the key metabolic precursor UDP-alpha-d-gluc

63 from SG and uridine 5'-diphosphate-glucose (UDP-Glc) under conditions that also favor cellulose synt

64 sed from keratinocytes and that UDP-glucose (UDP-Glc) added into keratinocyte cultures induced a spec

65 UDP-glucose (UDP-Glc) and glycogen levels in skeletal muscle fibers o

66 reptococcus pneumoniae requires UDP-glucose (UDP-Glc) and UDP-glucuronic acid (UDP-GlcUA) for product

67 lc-(1-3)-beta-d-GlcUA-(1-] from UDP-glucose (UDP-Glc) and UDP-glucuronic acid (UDP-GlcUA) is catalyse

68 on of the P2Y14 receptor ligand UDP-glucose (UDP-Glc) was higher in urine samples from intensive care

69 e bound to the substrate analog UDP-glucose (UDP-Glc) was solved by X-ray crystallographic methods an

70 ymes can use both UDP-GlcUA and UDP-glucose (UDP-Glc), leading to the formation of glucuronide and gl

71 of PMM2-CDG patients had higher UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal) and UDP-Glucuronic lev

72 ceptor is potently activated by UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal), UDP-N-acetylglucosami

73 lucosamine (UDP-GlcNAc) but not UDP-glucose (UDP-Glc).

74 and/or binding of the substrate UDP-glucose (UDP-Glc).

75 lucose-6-phosphate (Glc-6-P) --> Glc-1-P --> UDP-Glc --> UDP-glucuronic acid (UDP-GlcUA) --> (GlcUA-G

76 ter ovary mutant cell line ldlD deficient in UDP-Glc 4-epimerase and expressing CD82 or CD9 by cDNA t

77 e modelled the position of the Glc moiety in UDP-Glc.

78 The reduction in UDP-Glc suggested that UDP-Glc pyrophosphorylase (PPL) a

79 is-193 of rat GCS as an important residue in UDP-Glc and GCS inhibitor binding; however, little else

80 Other enzymes emphasized include UDP-Glc pyrophosphorylase and sucrose phosphate synthase

81 imerase is a homodimer that can interconvert UDP-Glc and UDP-Gal but not UDP-GlcNAc and UDP-GalNAc.

82 yzes epimerization reactions of UDP-Gal into UDP-Glc and UDP-GalNAc into UDP-GlcNAc with the same lev

83 the 2' and 3' isomers of methylanthraniloyl-UDP-Glc (MUG).

84 Strains containing mutant UDP-Glc dehydrogenases exhibited reduced levels of UDP-G

85 s: NAD(+)/UDP, NAD(+)/UDP-GlcNAc, and NAD(+)/UDP-Glc.

86 Using a competition assay, the affinity of UDP-Glc was determined to be 45+/-10 microm in the absen

87 lcNAc but allows a more optimal alignment of UDP-Glc for sugar donation.

88 Fluorescent analogs of UDP-Glc have been prepared for use in our studies of the

89 The binding of UDP-Glc and Mg2+ are highly coupled with Mg2+ affinities

90 ructures reveal that although the binding of UDP-Glc is quite similar to UDP-Gal, there are few signi

91 saturable with increasing concentrations of UDP-Glc or UDP-GlcUA, with respective apparent K(m) valu

92 es a UDP-Glc dehydrogenase for conversion of UDP-Glc to UDP-GlcUA.

93 biosynthesis, namely, those for formation of UDP-Glc, UDP-Gal, UDP-GalNAc, and dTDP-Rha.

94 The generation of UDP-Glc proceeds by conversion of Glc-6-P to Glc-1-P to

95 P, which acted as a competitive inhibitor of UDP-Glc, also stimulated Cps2E to catalyze the reverse r

96 1-P and UDP-Gal and abnormally low levels of UDP-Glc and UDP-GlcNAc in the presence of galactose and

97 ased both UDP-Glc PPL activity and levels of UDP-Glc in skeletal muscles by approximately 3-fold.

98 serve electron density for the Glc moiety of UDP-Glc nor for two large surface loop regions (residues

99 However, overexpression of UDP-Glc PPL was without effect on either the levels of s

100 We found that overproduction of UDP-Glc did not cause any alterations in Ca(2+) uptake o

101 Recently, cellular release of UDP-Glc and UDP-GlcNAc has been reported, but whether ad

102 NMR studies of UDP-Glc hydrolysis by yeast glycogen synthase were used

103 lyze the reverse reaction, with synthesis of UDP-Glc from the polyprenyl pyrophosphate Glc.

104 affinity of UDP-GlcUA is higher than that of UDP-Glc.

105 Insulin was without effect on UDP-Glc in Type I fibers but decreased UDP-Glc by 35-40%

106 bably accounts for the absence of Glc in our UDP-Glc substrate structures.

107 with a >15-fold preference for TDP-Glc over UDP-Glc.

108 lar levels of glucose-6-P (G-6-P), GlcN-6-P, UDP-Glc-NAc, and ATP.

109 sent a method for solubilizing and purifying UDP-Glc:ceramide glucosyltransferase (EC 2.4.1.80; gluco

110 In both the parent and mutant strains, UDP-Glc levels far exceeded UDP-GlcUA levels, which were

111 of UDP product (form I) and donor substrate UDP-Glc (form II), respectively.

112 erization reaction, these data indicate that UDP-Glc and UDP-GlcUA bind to the same synthase sites in

113 The results indicate that UDP-Glc PPL activity is not limiting for glycogen synthe

114 tion is consistent with data indicating that UDP-Glc is not a substrate for UGM.

115 nd IL-8 expression, supporting a notion that UDP-Glc signals for epidermal inflammation, enhanced hya

116 The reduction in UDP-Glc suggested that UDP-Glc pyrophosphorylase (PPL) activity might limit gly

117 The UDP-Glc dehydrogenase and synthase necessary for the lat

118 The UDP-Glc-actuated reaction was inhibited by UDP-GlcUA wit

119 Our study identifies the UDP-Glc/P2Y14 receptor axis as a potential target for th

120 s thaliana) lines carrying insertions in the UDP-Glc:sterol glucosyltransferase genes, UGT80A2 and UG

121 g UDP, which is an inhibitory product of the UDP-Glc:glycoprotein glucosyltransferase, it is likely t

122 ceeds by conversion of Glc-6-P to Glc-1-P to UDP-Glc and is mediated by a phosphoglucomutase (PGM) an

123 TcdA binds MUG competitively with respect to UDP-Glc with an affinity of 15 +/- 2 microm in the absen

124 by increased activity of core 2 transferase (UDP-Glc:Galbeta1-3GalNAcalphaRbeta-N-acetylglucoaminyltr

125 NAc as preferred sugar donor and UGT3A2 uses UDP-Glc.

126 p dye-agarose chromatography procedure using UDP-Glc to elute the enzyme.

127 was monitored throughout purification using UDP-Glc and a fluorescent ceramide analog as substrates.

128 he in UGT3A1 enhances its ability to utilize UDP-Glc and completely inhibits its ability to use UDP-G

129 tion of GlcUA to the chain terminus, whereas UDP-Glc drives chain termination when inadequate levels

130 ction of excess methylisatoic anhydride with UDP-Glc in aqueous solution yields primarily the 2' and

131 tal structures of the Gal-T1.LA complex with UDP-Glc x Mn(2+) and with N-butanoyl-glucosamine (N-buta

132 The apparent V(max) was 48-fold greater with UDP-Glc compared with UDP-GlcUA.

133 yme in detectable amounts upon reaction with UDP-Glc in the absence of Gal-1-P.

134 imilar to wild-type GalT, upon reaction with UDP-Glc.

135 conformations in the complex structures with UDP-Glc and UDP-GlcNAc.