ライフサイエンスコーパス: UDP-GalNAc

1 UDP-GalNAc could bind to either the N-terminal or C-term

2 UDP-GalNAc pyrophosphorylase (UDP-GalNAcPP; AGX1) cataly

3 UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans

4 UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltrans

5 UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans

6 a pentenary complex of bovine Gal-T1-Mn(2+)-UDP-GalNAc-Glc-alpha-lactalbumin.

7 tiated by a large family of approximately 20 UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans

8 gene from Caenorhabditis elegans encoding a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyl

9 A 4-epimerase and UDP-N-acetylgalactosamine (UDP-GalNAc) 4-epimerase activities.

10 (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-GalNAc) transport in Arabidopsis thaliana.

11 o uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc), irrespective of the initial substrate.

12 d, it resulted in a gain of activity against UDP-GalNAc by more than 230-fold.

13 wth on galactose, and (iii) both UDP-Gal and UDP-GalNAc 4-epimerase activities in cell extracts.

14 Thus, provision of both UDP-Gal and UDP-GalNAc for RPS production by S. gordonii 38 depends

15 ssayed for activity against both UDP-Gal and UDP-GalNAc.

16 otide-sugars UDP-glucose, UDP-galactose, and UDP-GalNAc.

17 zation reactions of UDP-Gal into UDP-Glc and UDP-GalNAc into UDP-GlcNAc with the same level of activi

18 binding of the donor substrates UDP-GlcA and UDP-GalNAc to purified K4CP protein and its mutants.

19 talyzed the synthesis of both UDP-GlcNAc and UDP-GalNAc from UTP and the appropriate HexNAc-1-P.

20 almost completely eliminated UDP-GlcNAc and UDP-GalNAc synthesis, while mutation of Gly(224) to Ala,

21 zes the epimerization between UDP-GlcNAc and UDP-GalNAc.

22 t UDP-Glc and UDP-Gal but not UDP-GlcNAc and UDP-GalNAc.

23 . coli enzyme to interconvert UDP-GlcNAc and UDP-GalNAc.

24 of Gne for UDP-Glc, UDP-Gal, UDP-GlcNAc, and UDP-GalNAc are 370, 295, 323, and 373 microM, respective

25 (polyprenyl-P-GalNAc) from polyprenyl-P and UDP-GalNAc.

26 idosalicylamido)-1-propenyl]-UDP-GlcNAc and -UDP-GalNAc, is described.

27 s was required to restore metabolic balance, UDP-GalNAc activity was not required for cell proliferat

28 undergoing conformational changes on binding UDP-GalNAc that arise from structuring the C terminus to

29 Rather, it strongly reduced cellular UDP-GalNAc and UDP-GlcNAc pools.

30 hat, indeed, this simple mutation did confer UDP-GalNAc/UDP-GlcNAc converting activity to the bacteri

31 r residues in a protein from the sugar donor UDP-GalNAc.

32 mine (GalNAc) from a nucleotide sugar donor (UDP-GalNAc) to Ser/Thr residues of an acceptor substrate

33 ly(224) to Ala, almost completely eliminated UDP-GalNAc synthesis, but UDP-GlcNAc was only diminished

34 the ganglioside-specific biosynthetic enzyme UDP-GalNAc:GM3/GD3 N-acetylgalactosaminyltransferase) re

35 d an apparent Km of 0.38 +/- 0.12 microM for UDP-GalNAc.

36 yltransferase with a 200-fold preference for UDP-GalNAc as substrate relative to UDP-Gal.

37 roup E which has a synthetic requirement for UDP-GalNAc.

38 Moreover, the calculated kcat/Km values for UDP-GalNAc and UDP-Gal are approximately 2-4 times highe

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

40 transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to fo

41 samine (GlcNAc) moiety is found cleaved from UDP-GalNAc and is placed 2.7A away from the O4 oxygen at

42 ine whether the enzymes transfer GalNAc from UDP-GalNAc or Gal from UDP-Gal to the H-antigen acceptor

43 Gal-T1 also transfers GalNAc from UDP-GalNAc to GlcNAc, but with only approximately 0.1% o

44 ppGalNAc Ts) that transfer alpha-GalNAc from UDP-GalNAc to Ser and Thr residues of polypeptide accept

45 ases (ppGalNAc Ts) that transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide ac

46 alyze the repetitive addition of sugars from UDP-GalNAc and UDP-GlcUA to chondroitin oligosaccharide

47 encoding Forssman glycolipid synthetase (FS; UDP-GalNAc:globoside alpha-1,3-N-acetylgalactosaminyltra

48 ly, those for formation of UDP-Glc, UDP-Gal, UDP-GalNAc, and dTDP-Rha.

49 ion of sugar nucleotides, including UDP-Gal, UDP-GalNAc, GDP-Fuc, and CMP-Neu5Ac.

50 mster ovary ldl-D cells defective in UDP-Gal/UDP-GalNAc 4-epimerase in which N- and O-linked glycosyl

51 synthesising UDP-Gal and UDP-galactosamine (UDP-GalNAc).

52 u5Ac, CMP-Neu5Gc, CMP-KDN, UDP-Gal, UDP-Glc, UDP-GalNAc, UDP-GlcNAc, GDP-Fuc, GDP-Man) and 12 nucleot

53 s GDP-Man, and TbNST4 transports UDP-GlcNAc, UDP-GalNAc, and GDP-Man.

54 ed that it does not function as a UDP-GlcNAc/UDP-GalNAc epimerase.

55 howed that WT PaWaaG specifically hydrolyzes UDP-GalNAc and unlike EcWaaG, does not hydrolyze UDP-glu

56 -sugars inhibited enzyme activity, including UDP-GalNAc, UDP-Glc, UDP-Gal, UDP-GalUA, UMP, UDP, and U

57 lNAc contained protein complexes with intact UDP-GalNAc and two forms with hydrolysis products (UDP p

58 chia coli counterpart, can also interconvert UDP-GalNAc and UDP-GlcNAc.

59 e radioactivity incorporated from 3H-labeled UDP-GalNAc into a biotin-labeled acceptor peptide, as me

60 he cDNA for a fourth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

61 ene encoding a ninth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

62 erization of a novel member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

63 ression of the fifth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

64 c was not due to epimerase activity since no UDP-GalNAc could be detected when the enzyme was incubat

65 GalE2 contained UDP-Gal 4-epimerase but not UDP-GalNAc 4-epimerase activity.

66 factor type 1 associated protein and a novel UDP-GalNAc:poly-peptide N -acetylgalactosaminyltransfera

67 The binding affinity of UDP-GalNAc to a K4CP N-terminal fragment (residues 58-35

68 the K4CP molecule regulating the binding of UDP-GalNAc to only the N-terminal active site.

69 ssigned the gne gene for the biosynthesis of UDP-GalNAc.

70 htly more efficient for the epimerization of UDP-GalNAc and UDP-Gal.

71 n biosynthesis is regulated by the family of UDP-GalNAc polypeptide:N-acetylgalactosaminlytransfersas

72 sy la tion is initiated by a large family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans

73 A large family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans

74 The family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans

75 cosylation is initiated by a large family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

76 The family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

77 O-glycosylation is initiated by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

78 O-glycosylation is catalyzed by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

79 43), interact with the diphosphate moiety of UDP-GalNAc, but only Lys(231) interacts with the UDP pro

80 hod for quantitating the reaction product of UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferas

81 thesizes UDP-GlcNAc at about 25% the rate of UDP-GalNAc.

82 is regulated by the substrate specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferas

83 P-GalNAcPP; AGX1) catalyzes the synthesis of UDP-GalNAc from UTP and GalNAc-1-P.

84 y of the pyrophosphorylase from synthesis of UDP-GalNAc to synthesis of UDP-GlcNAc.

85 Starting with either UDP-GlcNAc or UDP-GalNAc, the synthesis involved the preparation of th

86 Ac probe was blocked by either UDP-GlcNAc or UDP-GalNAc.

87 -dependent manner by unlabeled UDP-GlcNAc or UDP-GalNAc.

88 azidosalicylamido)-1-propenyl]-UDP-GlcNAc or UDP-GalNAc.

89 d UDP-glucose, UDP-galactose, UDP-GlcNAc, or UDP-GalNAc.

90 n of the apoPSM tandem repeat by recombinant UDP-GalNAc:polypeptide alpha-GalNAc transferases (ppGalN

91 alicylate-allylamine-UDP-GlcNAc or a similar UDP-GalNAc photoaffinity probe, and either labeling was

92 lectin alpha site and a modeled active site UDP-GalNAc is consistent with the in vitro pattern of gl

93 tion of the synthesis of the donor substrate UDP-GalNAc and one or more polypeptide GalNAc-transferas

94 lNAc glycans in nuclei: the donor substrate (UDP-GalNAc), nuclear polypeptide GalNAc -transferase act

95 Giardia synthesizes UDP-GalNAc during cyst wall formation (encystment) via a

96 This activity for synthesizing UDP-GalNAc was not due to epimerase activity since no UD

97 cosyltransferase in complex with a synthetic UDP-GalNAc derivative.

98 The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

99 Both the UDP-GlcNAc and the UDP-GalNAc derivatives reacted in a concentration-depend

100 d subsequently in the Golgi apparatus by the UDP-GalNAc polypeptide N-acetylgalactosaminyltransferase

101 etailed transfer mechanism, catalyzed by the UDP-GalNAc polypeptide:N-acetyl-alpha-galactosaminyltran

102 o the previously reported K(m) value for the UDP-GalNAc transfer reaction that takes place at the N-t

103 a UDP-GlcNAc C4-epimerase that generates the UDP-GalNAc precursors required by the Pel synthase machi

104 Mutations in one member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

105 nal characterization of eight members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

106 tration that the activity of a member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

107 The crystal structure reveals that the UDP-GalNAc binding to Gal-T1 is similar to the binding o

108 Likewise, labeling with the UDP-GalNAc probe was blocked by either UDP-GlcNAc or UDP

109 In addition, we show that this UDP-GalNAc derivative in complex with the H-antigen acce

110 uman enzyme can also turn over UDP-GlcNAc to UDP-GalNAc and vice versa.

111 he TviB-catalyzed oxidation of UDP-GlcNAc to UDP-GalNAc, followed by the TviC-catalyzed epimerization

112 -encoded protein could convert UDP-GlcNAc to UDP-GalNAc, indicating that BAS5304 was the gene sought.

113 inhibiting 4-epimerization of UDP-GlcNAc to UDP-GalNAc, thereby depleting one of the substrates requ

114 shift the equilibrium of this pathway toward UDP-GalNAc synthesis.

115 elated to the catalytic domain of mucin-type UDP-GalNAc:Ser/Thr polypeptide alpha-GalNAc-transferases

116 by either unlabeled UDP-GlcNAc or unlabeled UDP-GalNAc.

117 expressed in CHO-Lec8 cells was active using UDP-GalNAc, but not UDP-Gal, as a donor toward a variety

118 higher substrate concentrations, it utilized UDP-GalNAc as a substrate as well as UDP-GlcNAc in the r

119 cture analysis of the Gal-T1.LA complex with UDP-GalNAc at 2.1-A resolution.

120 a low activity mutant of BoGT6a (E192Q) with UDP-GalNAc contained protein complexes with intact UDP-G