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1 dent upon the addition of both manganese and UDP-galactose.
2 everely impair the enzyme's activity against UDP-galactose.
3 th ADP-glucose, GDP-mannose, UDP-glucose, or UDP-galactose.
4 ly correlated with residual activity against UDP-galactose.
5  accumulation of the intermediary metabolite UDP-galactose.
6 ited an atypical concentration dependence on UDP-galactose.
7 en determined of a complex containing intact UDP-galactose.
8  degrees C with or without pretreatment with UDP-galactose.
9 phate + UDP-glucose to glucose-1-phosphate + UDP-galactose.
10 ith ADP-glucose, UDP-glucose, UDP-GlcNAc, or UDP-galactose.
11                 The product of this gene has UDP galactose 4-epimerase activity in both E. coli and Y
12                                   The enzyme UDP-galactose 4'-epimerase (GALE) catalyses the reversib
13                                              UDP-galactose 4'-epimerase (GALE) catalyzes the final st
14                                              UDP-galactose 4'-epimerase (GALE) catalyzes the final st
15                                              UDP-galactose 4'-epimerase (GALE) catalyzes the intercon
16                                              UDP-galactose 4'-epimerase (GALE) interconverts UDP-gala
17  galactosemia results from the impairment of UDP-galactose 4'-epimerase (GALE), the third enzyme in t
18    Galactosemia III results from the loss of UDP-galactose 4'-epimerase (GALE), which interconverts U
19                                              UDP-galactose 4'-epimerase (TbGalE), an enzyme of the Le
20 pression of a gene encoding Escherichia coli UDP-galactose 4-epimerase and engineered to facilitate c
21 24, Tyr149, and Lys153 in the active site of UDP-galactose 4-epimerase are located in similar positio
22 richia coli dTDP-glucose 4,6-dehydratase and UDP-galactose 4-epimerase are members of the short-chain
23                                              UDP-galactose 4-epimerase catalyzes the conversion of UD
24                                              UDP-galactose 4-epimerase catalyzes the interconversion
25                                              UDP-galactose 4-epimerase catalyzes the interconversion
26                                              UDP-galactose 4-epimerase catalyzes the interconversion
27                                              UDP-galactose 4-epimerase catalyzes the interconversion
28                                              UDP-galactose 4-epimerase contains the coenzyme NAD+ bou
29 der can occur due to either galactokinase or UDP-galactose 4-epimerase deficiencies.
30 meters for epimerization of UDP-galactose by UDP-galactose 4-epimerase from Escherichia coli (GalE),
31                                              UDP-galactose 4-epimerase from Escherichia coli catalyze
32                                              UDP-galactose 4-epimerase from Escherichia coli contains
33                                              UDP-galactose 4-epimerase is one of three enzymes in the
34                                              UDP-galactose 4-epimerase plays a critical role in sugar
35                                       Unlike UDP-galactose 4-epimerase where the conversion of config
36 ive site is reminiscent to that observed for UDP-galactose 4-epimerase, an enzyme that plays a key ro
37 mes of the pathway, galactose mutarotase and UDP-galactose 4-epimerase, are contained within a single
38 g of uridine diphosphogalactose 4-epimerase (UDP-galactose 4-epimerase, EC ) and alpha1, 3-galactosyl
39 o the roles of the corresponding residues in UDP-galactose 4-epimerase, which facilitate the ionizati
40        We characterized mutants defective in UDP-galactose 4-epimerase, which produced a defective li
41 tural comparison of ADP-hep 6-epimerase with UDP-galactose 4-epimerase, which utilizes an NAD(+) cofa
42 nase, galactose-1-P uridylyltransferase, and UDP-galactose 4-epimerase.
43 ound structural homology in Escherichia coli UDP-galactose 4-epimerase.
44 DR) family, with the closest relationship to UDP-galactose 4-epimerase.
45 ical bilobal topology observed for all other UDP-galactose 4-epimerases studied thus far.
46               Mechanistically, we identified UDP-galactose-4-epimerase (GalE) as a direct transcripti
47                                              UDP-galactose-4-epimerase (GALE) is a highly conserved e
48  results from impairment of the human enzyme UDP-galactose-4-epimerase (hGALE).
49                       Homology modeling with UDP-galactose-4-epimerase predicts that Asp36 is respons
50  in genes encoding phosphoglucomutase (pgm), UDP-galactose-4-epimerase, and two other NTHI sialyltran
51 ormation with the 3-dimensional structure of UDP-galactose-4-epimerase.
52                         Uridine diphosphate (UDP) galactose, a pivotal compound in the metabolism of
53 n effort to prepare an abortive complex with UDP-galactose, a site-directed mutant protein was constr
54           Attempts to prepare an enzyme/NADH/UDP-galactose abortive complex always failed, however, i
55 ease of entropy, whereas the weak binding of UDP-galactose and -glucose, which occurred only in D2O s
56 rom sporophytic tissues, F3GalTase uses only UDP-galactose and flavonols to catalyze the formation of
57 with galactose 1-phosphate (Gal-1-P) to form UDP-galactose and glucose 1-phosphate (Glc-1-P) through
58 P-glucose with galactose 1-phosphate to form UDP-galactose and glucose 1-phosphate during normal cell
59 ersion of UDP-glucose and galactose-1-P with UDP-galactose and glucose-1-P by a double-displacement m
60 ose and galactose-1-phosphate (Gal-1-P) into UDP-galactose and glucose-1-phosphate (Glc-1-P) by a dou
61 ate that the cofactor is involved in binding UDP-galactose and has a crucial influence on catalytic e
62 myo-inositol to the reaction, which converts UDP-galactose and myo-inositol to galactinol is a contro
63 in yeast was severely reduced with regard to UDP-galactose and partially reduced with regard to UDP-N
64 consistent with the specificity of SRF-3 for UDP-galactose and strongly suggest that the above glycoc
65 s as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating th
66 4-epimerase catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose me
67 4-epimerase catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose me
68 -galactose 4'-epimerase (GALE) interconverts UDP-galactose and UDP-glucose in the final step of the L
69                    The nucleotide portion of UDP-galactose and UDP-glucose participates in the epimer
70 dylyltransferase is able to accommodate both UDP-galactose and UDP-glucose substrates by simple movem
71 cipates in catalyzing the interconversion of UDP-galactose and UDP-glucose through its redox properti
72 richia coli catalyzes the interconversion of UDP-galactose and UDP-glucose through the transient redu
73 rase (GALE) catalyzes the interconversion of UDP-galactose and UDP-glucose, an important step in gala
74 ose 4'-epimerase (GALE), which interconverts UDP-galactose and UDP-glucose, as well as UDP-N-acetylga
75 abolism by catalyzing the interconversion of UDP-galactose and UDP-glucose.
76 enzyme that catalyzes the interconversion of UDP-galactose and UDP-glucose.
77 this enzyme catalyzes the interconversion of UDP-galactose and UDP-glucose.
78 way of galactose metabolism, interconverting UDP-galactose and UDP-glucose.
79  relative specificities for the sugar donors UDP-galactose and UDP-glucuronic acid, although UDP-gluc
80 talyses the reversible epimerisation of both UDP-galactose and UDP-N-acetyl-galactosamine.
81          Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine (GalNAc) and
82 zed in terms of activity with regard to both UDP-galactose and UDP-N-acetylgalactosamine.
83 ies included elevated galactose-1P, elevated UDP-galactose, and deficient UDP-glucose.
84 eversibly glycosylated using UDP-glucose and UDP-galactose as substrates.
85         Herein, we describe the cloning of a UDP-galactose: beta-d-galactosyl-1,4-glucosylceramide al
86 ncoded for by the enzyme glucosyltransferase UDP galactose:beta-D-galactosyl-1, 4-N-acetyl-D-glucosam
87 cNAc-R (alphaGal), synthesized by the enzyme UDP galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosami
88   Here, we asked whether inactivation of the UDP-galactose:beta-galactoside-alpha1-3-galactosyltransf
89                                              UDP-galactose:beta-galactosyl-alpha1,3-galactosyltransfe
90 y represents the first direct observation of UDP-galactose binding to epimerase and lends strong stru
91  donor substrate distortion, cleavage of the UDP-galactose bond, galactose transfer, and UDP release.
92 . enterocolitica is not in the production of UDP galactose but, instead, some other nucleotide sugar
93 demonstrated normal activity with respect to UDP-galactose but complete loss of activity with respect
94 tate kinetic parameters for epimerization of UDP-galactose by UDP-galactose 4-epimerase from Escheric
95                             Epimerization of UDP-galactose-C-d(7) by S124A-GalE proceeds with a pH-in
96 kinetic isotope effects for epimerization of UDP-galactose-C-d(7) by these enzymes have also been mea
97                             Epimerization of UDP-galactose-C-d(7) by Y149F-GalE proceeds with a pH-de
98 um kinetic isotope effect in the reaction of UDP-galactose-C-d(7).
99                                              UDP-galactose ceramide galactosyltransferase-deficient (
100 he gene that encodes the biosynthetic enzyme UDP-galactose:ceramide galactosyl transferase (CGT) are
101 P-glucose:ceramide glucosyltransferase or by UDP-galactose:ceramide galactosyltransferase (CGalT).
102 mice lacking the key enzyme to generate GCs, UDP-galactose:ceramide galactosyltransferase (CGT(-/-)),
103                                              UDP-galactose:ceramide galactosyltransferase (CGT) (EC 2
104    We have generated mice lacking the enzyme UDP-galactose:ceramide galactosyltransferase (CGT), whic
105 l allele of the gene that encodes the enzyme UDP-galactose:ceramide galactosyltransferase (Cgt), whic
106 The structures of the enzyme/UDP-glucose and UDP-galactose complexes, in which the catalytic nucleoph
107 lacturonate was not formed by a hypothetical UDP-galactose dehydrogenase.
108 pendent (1-->4)-beta-D-mannan synthase and a UDP-galactose dependent (1-->6)-alpha-D-galactosyltransf
109 lyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism.
110 s D and D' contain an intact gene encoding a UDP-galactose epimerase (galE1) and a truncated remnant
111 he C-4'' position of sugar nucleotides, like UDP-galactose epimerase, dTDP-glucose-4,6-dehydratase, a
112                               ArnA resembles UDP-galactose epimerase, dTDP-glucose-4,6-dehydratase, a
113  pyrophosphorylase (UGP) alternatively makes UDP-galactose from uridine triphosphate and galactose-1-
114 curonic acid, UDP-N-acetylgalactosamine, and UDP-galactose (Gal) in a temperature-dependent and satur
115 pholino-1-propanol (D-PDMP), an inhibitor of UDP-galactose:glucosylceramide beta(1-->4)-galactosyltra
116 thesis by way of stimulating the activity of UDP-galactose:glucosylceramide beta(1-->4)-galactosyltra
117 e porcine salivary gland Core 1 transferase (UDP-galactose:glycoprotein-alpha-GalNAc beta3-galactosyl
118 alactose transfer and for the low endogenous UDP-galactose hydrolase activity.
119 fore interact with one or more phosphates of UDP-galactose in the Michaelis complex and in the transi
120 e specifically defective in the transport of UDP-galactose into the Golgi apparatus and of a mutant o
121 ransporter is rate-limiting in the supply of UDP-galactose into the Golgi lumen; this in turn results
122 CAr) with a 2% residual rate of transport of UDP-galactose into the lumen of Golgi vesicles was descr
123 xtract of the above protist, which transport UDP-galactose into their lumen with a K(m) of 2.7 microm
124 er in Saccharomyces cerevisiae; its K(m) for UDP-galactose is 2.9 microm; (b) characterized vesicles
125 e (ADPG), kaempferol and UDPG, quercetin and UDP-galactose, isoliquiritigenin and UDPG, and luteolin
126 e intermediates', galactose 1-phosphate <--> UDP-galactose &lt;--> UDP-glucose <--> glucose 1-phosphate
127        In the presence of GDP-mannose and/or UDP-galactose, membranes of R. leguminosarum first trans
128 T-II encode an alpha-lactalbumin-responsive, UDP-galactose:N-acetylglucosamine beta4-galactosyltransf
129                                      Neither UDP-galactose nor GDP-mannose was active as a sugar dono
130 ne-containing acceptors, and utilizes either UDP-galactose or UDP-glucose as donor substrates.
131 h the uridine nucleotide may be UDP-glucose, UDP-galactose, or UDP.
132 residues with uridine 5'-diphosphogalactose (UDP-galactose) results in the normal survival of short-t
133 o investigate the structural determinants of UDP-galactose selectivity.
134  the 4'-hydroxyl group of the UDP-glucose or UDP-galactose substrates during the course of the reacti
135 ation occurs about C-4 of the UDP-glucose or UDP-galactose substrates, in the reaction catalyzed by t
136                                    UGT8 uses UDP galactose to galactosidate ceramide, a key step in t
137 stead, the enzyme transferred galactose from UDP-galactose to acceptors containing a terminal beta-li
138 GT) catalyzes the transfer of galactose from UDP-galactose to beta-linked galactosides with retention
139 GT) catalyzes the transfer of galactose from UDP-galactose to form an alpha 1-3 link with beta-linked
140  epimerase in the presence of UDP-glucose or UDP-galactose to high resolution.
141 ed a similar glycosylation process by adding UDP-galactose to human apheresis platelets.
142 ase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues o
143 ) catalyzes the transfer of a galactose from UDP-galactose to N-acetylglucosamine.
144 ment of alpha1, 3-galactosyltransferase from UDP-galactose to UDP-glucose and decreased the cost for
145 tose 4-epimerase catalyzes the conversion of UDP-galactose to UDP-glucose through a mechanism involvi
146 richia coli, and has been shown to epimerize UDP-galactose to UDP-glucose without the addition of NAD
147 a manganese ion, it transfers galactose from UDP-galactose to xylose on a proteoglycan acceptor subst
148 ar site where galactose is transferred, from UDP-galactose, to the oligosaccharide chains of glycopro
149                        Each mutation reduced UDP-galactose transport, leading to galactose-deficient
150 nes, an acetyl-CoA transporter (pfact) and a UDP-galactose transporter (pfugt).
151                                              UDP-galactose transporter (UGT; SLC35A2) and UDP-N-acety
152 ajor mutant, which is inactivated in the two UDP-galactose transporter genes LPG5A and LPG5B.
153  (a) cloned and expressed the E. histolytica UDP-galactose transporter in Saccharomyces cerevisiae; i
154  results demonstrate that the Golgi membrane UDP-galactose transporter is rate-limiting in the supply
155  identified mutations in the Golgi-localized UDP-galactose transporter SLC35A2 that define an undiagn
156  of PHB, PDK2, a speckle-type protein, and a UDP-galactose transporter.
157 ansported into the Golgi lumen by a specific UDP-galactose transporter.
158 mino acid sequence identity to the mammalian UDP-galactose transporters and 40% to the CMP-sialic aci
159 he YEA4 UDP- N-acetylglucosamine or the HUT1 UDP-galactose transporters, and overexpression of YEA4 o
160  for 48 hours at 4 degrees C and showed that UDP-galactose treatment of murine platelets also did not
161 mplex of a low-activity mutant alpha3GT with UDP-galactose (UDP-gal) exhibiting a bent configuration
162 n, galactose-1-phosphate (gal-1-P) is bound, UDP-galactose (UDP-Gal) is released, and the free enzyme
163 ce of manganese ion transfers galactose from UDP-galactose (UDP-Gal) to N-acetylglucosamine (GlcNAc)
164 n to be either mono-functional, synthesising UDP-galactose (UDP-Gal), or bi-functional, synthesising
165 potently activated by UDP-glucose (UDP-Glc), UDP-galactose (UDP-Gal), UDP-N-acetylglucosamine (UDP-Gl
166 thesize UDP-galacturonic acid (UDP-GalA) and UDP-galactose (UDP-Gal).
167 Golgi apparatus transporter for UDP-glucose, UDP-galactose, UDP- N-acetylglucosamine, and UDP- N-acet
168 complex containing an inhibitory analogue of UDP-galactose, UDP-2F-galactose, in a complex with the A
169 imerase complexed with NADH and UDP-glucose, UDP-galactose, UDP-GlcNAc, or UDP-GalNAc.
170 ied and quantified the pools of UDP-glucose, UDP-galactose, UDP-N-acetylglucosamine, GDP-mannose, and
171 umen of the above vesicles with the K(m) for UDP-galactose, using endogenous acceptors, being 93 micr
172 ed, however, in that UDP-glucose rather than UDP-galactose was observed binding in the active site.
173 rt induction was specific as no transport of UDP-galactose was observed even though the latter putati

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