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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

93 The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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