ライフサイエンスコーパス: UMP

1 UMP also significantly increased plasma and brain cytidi

2 UMP and CMP proved to be far better substrates than dCMP

3 UMP and GMP, accompanied by Mg2+, bind specifically to P

4 UMP and phosphoribosylpyrophosphate were shown by equili

5 UMP synthase, the bifunctional protein that catalyzes th

6 UMP was released from the enzyme concomitantly with CO(2

7 UMP, GMP, and CMP could not substitute for AMP as gamma-

8 UMP, which acted as a competitive inhibitor of UDP-Glc,

9 UMP/CMPK localized predominantly to the cytoplasm.

10 UMP/CMPK used all of the nucleoside triphosphates as pho

11 erase (E-His(166) + UDP-glucose = E-His(166)-UMP + glucose-1-P) is found to be 1.8 x 10(-4) at pH 7.0

12 ) for the hydrolyses of UMPIm and E-His(166)-UMP are -14.7 and -15.4 kcal mol(-1), respectively at pH

13 active site and the UMP group of E-His(166)-UMP provide little or no stabilization in the formation

14 3'-UMP binds to the variant protein with 5-fold weaker affi

15 66A RNase A and the K7A/R10A/K66A RNase A.3'-UMP complex were determined by X-ray diffraction analysi

16 and with bound 3'-uridine monophosphate (3'-UMP).

17 of 3'-UMP shows that a second molecule of 3'-UMP can bind to the enzyme.

18 Finally, the affinity of 3'-UMP for wild-type RNase A and the K7A/R10A/K66A variant

19 s consistent with the phosphoryl group of 3'-UMP interacting more strongly with the two active-site h

20 e presence of different concentrations of 3'-UMP shows that a second molecule of 3'-UMP can bind to t

21 e reaction product, uridine 3'-phosphate (3'-UMP), protonation of one active-site histidine residue f

22 f wild-type RNase A and the variants with 3'-UMP at pH 6.0 show that His12 and His119 contribute 1.4

23 te (5'-AMP) and uridine 5'-monophosphate (5'-UMP) are synthesized, and their structures are elucidate

24 Among aged animals consuming a UMP-containing diet (2.5%, w/w) for 1 or 6 weeks, baseli

25 In addition, 196-amino acid UMP/CMPK was the actual form of UMP/CMPK, rather than th

26 CMP, although with lower apparent affinity; UMP and the purine nucleotides are poor substrates.

27 d CDP-choline were all elevated 15 min after UMP (from 254 +/- 31.9 to 417 +/- 50.2, [P < 0.05]; 56.8

28 ornithine, which function as activators, and UMP, which acts as an inhibitor.

29 o be a competitive inhibitor of both ATP and UMP.

30 eeks, a diet containing choline chloride and UMP (a uridine source) and/or DHA by gavage.

31 mplates containing ribavirin support CMP and UMP incorporation with equivalent efficiency.

32 the release of the two products, Lipid I and UMP.

33 lated by the metabolites ornithine, IMP, and UMP.

34 Surprisingly, ornithine and UMP each had a significant effect on chCPS activity, and

35 When both ornithine and UMP were varied, models which presume a mutually exclusi

36 or the allosteric regulators, ornithine, and UMP.

37 o form 2,3-diacylglucosamine 1-phosphate and UMP by catalyzing the attack of water at the alpha-P ato

38 ducts, 2,3-diacylglucosamine 1-phosphate and UMP, by LpxH.

39 yield 2,3-diacylglucosamine 1-phosphate and UMP.

40 ndividually ornithine strongly promotes, and UMP strongly antagonizes, the binding of MgADP.

41 trations were required for the response, and UMP showed no stimulation at all.

42 Binding of PyrR to pyr RNA was specific and UMP-dependent with apparent Kd values of 10 and 220 nM i

43 ternary complex composed of UTP, TbTUT4, and UMP, which mimics an RNA substrate, and the postreaction

44 llular UTP or its breakdown products UDP and UMP act as mediators for hyaluronan synthase (HAS) activ

45 syltransferase activity of PyrR, antagonized UMP-dependent transcriptional termination, but uracil di

46 e slow deuridylylation of GlnK approximately UMP by the UTase/UR suggests that rapid interconversion

47 wed the deuridylylation of PII approximately UMP upon ammonia addition, showing that multiple PII int

48 ng enzyme (UTase/UR), only PII approximately UMP was effectively deuridylylated by the UR activity of

49 alidation of a new luminescence-based assay (UMP-Glo) for measuring activities of PGT enzymes.

50 revented by phosphorothioate substitution at UMP residues in the nascent RNA.

51 nstant = 23.2 microm), and the T-state binds UMP exclusively (dissociation constant = 0.49 microm).

52 the behavior of bisalanyl-AMP and bisalanyl-UMP in the presence of model nucleophiles.

53 We further found that sCPS bound both UMP and IMP and that chCPS bound IMP, although none of t

54 However, both UMP (Km = 153 microM) and CMP (Km = 266 microM) were equ

55 ers for deuterium exchange into enzyme-bound UMP and F-UMP of 1.2 x 10(-5) and 0.041 s(-1), respectiv

56 The 3' hydroxyl of the bound UMP is poised for in-line nucleophilic attack while cont

57 active triphosphate metabolite, PSI-7409, by UMP-CMP kinase and nucleoside diphosphate kinase, respec

58 terminator structures, and that PyrR acts by UMP-dependent binding to and stabilization of the anti-a

59 This band is partially bleached by UMP and almost totally abolished by UDP, indicating that

60 steps in de novo synthesis are catalysed by UMP synthase (UMPS) - a bifunctional enzyme comprising o

61 w kinetic studies on UTP binding followed by UMP incorporation into an EC as monitored by alterations

62 yrimidines, and its activity is inhibited by UMP and activated by 5-phospho-alpha-D-ribosyl diphospha

63 lites from both pathways, with inhibition by UMP and activation by IMP and ornithine.

64 ressed as a bifunctional gene product called UMP synthase (UMPS), with OPRT at the N terminus and OMP

65 ) is responsible for phosphorylation of CMP, UMP, and deoxycytidine monophosphate (dCMP) and also pla

66 aker substrate for purified enzyme than CMP, UMP, or dCMP.

67 e, T-maze, and Y-maze tests; coadministering UMP further enhanced these increases.

68 from 137 to 680 fmol/min in those consuming UMP (P<0.05).

69 phosphate) versus their ribose-counterparts (UMP and 5-fluorouridine monophosphate), in a similar man

70 cement, with the participation of a covalent UMP-His 166-enzyme intermediate in the Escherichia coli

71 en atoms of the substrate in the crystalline UMP-enzyme and in the crystalline complex of H166G-GalT

72 88 reduces hydrogen bonding and destabilizes UMP-GALT.

73 Dietary UMP (0.5%, 1 week) also amplified the increase in ACh ca

74 tate based on the structure of D. discoideum UMP/CMP kinase aids to rationalize the substrate specifi

75 ted for the similar Dictyostelium discoideum UMP/CMP kinase reveals the conformational changes that o

76 al was obtained by the co-addition of either UMP or cytidine.

77 activation dominates the effects when either UMP or IMP is also bound.

78 synthase protein levels as well as elevated UMP synthase mRNA levels.

79 enzyme activity was correlated with elevated UMP synthase protein levels as well as elevated UMP synt

80 ate formation of a covalent uridylyl-enzyme (UMP enzyme).

81 ate formation of a covalent uridylyl-enzyme (UMP-enzyme).

82 ate formation of a covalent uridylyl-enzyme (UMP-enzyme).

83 inase has 50% identity with other eukaryotic UMP/CMP kinase proteins.

84 uterium exchange into enzyme-bound UMP and F-UMP of 1.2 x 10(-5) and 0.041 s(-1), respectively, so th

85 The binding of UMP and F-UMP to ScOMPDC results in 0.5 and 1.4 unit decreases, re

86 The binding of UMP and F-UMP to ScOMPDC results in a greater than 5 x 10(9)-fold

87 or k(cat)/K(m) for deuterium exchange into F-UMP gives the intrinsic second-order rate constant for e

88 UMP) and 5-fluorouridine 5'-monophosphate (F-UMP) catalyzed by yeast orotidine 5'-monophosphate decar

89 -fluorouracil (5-FU) and further to 5-fluoro-UMP, respectively.

90 levels; however, both basally and following UMP, these levels were much lower than those of uridine.

91 4) and 1.28 x 10(4) microM(-)(1) s(-)(1) for UMP and GMP, respectively.

92 rification scheme, in which the affinity for UMP was markedly reduced, CP rate curves showed no sigmo

93 monoesterase activity, with a preference for UMP > TMP > AMP >> CMP.

94 ion suggests that exogenous Up4A first forms UMP and ATP in the human colon and UDP and ADP in the mu

95 Furthermore, UMP/CMPK was able to phosphorylate all of the deoxycytid

96 mensional model of the Escherichia coli GALT-UMP protein crystal.

97 ing UDP-GalNAc, UDP-Glc, UDP-Gal, UDP-GalUA, UMP, UDP, and UTP.

98 Here, the roles of GlnK and GlnK-UMP in A. vinelandii were studied to determine whether t

99 inhibited by NH(4)(+), suggesting that GlnK-UMP is required to signal adenylyltransferase/adenylyl-r

100 stringent with a preference of CMP > AMP >> UMP > GMP.

101 AMP, ADP, ATP, CMP, CDP, CTP, GMP, GDP, GTP, UMP, UDP, and UTP) was examined by reversed-phase HPLC a

102 Human UMP synthase is a bifunctional protein containing two se

103 Human UMP/CMP kinase (cytidylate kinase; EC 2.7.4.14) is respo

104 Human UMP/CMP kinase plays a crucial role in supplying precurs

105 data suggest that the active sites of human UMP/CMP kinase for dCMP and for CMP cannot be identical.

106 dels for the phosphorylation action of human UMP/CMP kinase.

107 re of the substrate-free, open form of human UMP/CMP kinase.

108 a using recombinant or highly purified human UMP/CMP kinase showed that dCMP, as well as pyrimidine a

109 ction conditions for human recombinant human UMP/CMP kinase to phosphorylate dCMP and CMP (referred a

110 Thus, we cloned the human UMP/CMPK gene, expressed it in Escherichia coli, and pur

111 The reactivities of the mutants in UMP-dependent reductive inactivation by glucose are simi

112 s, we hypothesize that the covalent union in UMP synthase stabilizes the domains containing the respe

113 at the active site compared to the inactive UMP/UDP-enzyme complex reported previously.

114 ases (TUTases) catalyze template-independent UMP addition to the 3' hydroxyl of RNA.

115 osteric activator ornithine or the inhibitor UMP despite the substantial and opposing effects these l

116 for V(max) (pK(a) values = 5.5, 9.0) and V/K(UMP)(-)(NeuAc) (pK(a)values = 6.2, 9.0).

117 er, as a non-heme, Fe(II)-dependent alpha-KG:UMP dioxygenase that produces uridine-5'-aldehyde to ini

118 eoside monophosphate kinase [UMP/CMP kinase (UMP/CMPK);EC 2.7.4.14] plays a crucial role in the forma

119 Pyrimidine nucleoside monophosphate kinase [UMP/CMP kinase (UMP/CMPK);EC 2.7.4.14] plays a crucial r

120 PRPP, which like UMP is a substrate for the uracil phosphoribosyltransfer

121 eaction in which the enzyme covalently links UMP to the hydroxyl group of tyrosine in the terminal pr

122 ermined to be K(m)(alpha-KG) = 7.5 muM, K(m)(UMP) = 14 muM, and k(cat) approximately 80 min(-1).

123 This assay measures UMP, the by-product of PGT reactions, in a sensitive and

124 When 10 or 100 microM UMP was added to reaction mixtures containing D39 membra

125 the C-6 protons of uridine 5'-monophosphate (UMP) and 5-fluorouridine 5'-monophosphate (F-UMP) cataly

126 o steps of de novo uridine 5'-monophosphate (UMP) biosynthesis are catalyzed by orotate phosphoribosy

127 the uridine source uridine-5'-monophosphate (UMP) can significantly increase levels of the phosphatid

128 hways whereby oral uridine-5'-monophosphate (UMP) increases membrane phosphatide synthesis in brains

129 phosphate (CP) and uridine 5'-monophosphate (UMP), showed pronounced sigmoidicity, each in the presen

130 a uridine source, uridine-5'-monophosphate (UMP), which increases brain levels of the rate-limiting

131 phosphate (OMP) to uridine 5'-monophosphate (UMP).

132 abidopsis thaliana uridine 5'-monophosphate (UMP)/cytidine 5'-monophosphate (CMP) kinase was isolated

133 Uridine monophosphate (UMP) kinase is a conserved enzyme that catalyzes the ATP

134 hosphate (AMP) and 5'-uridine monophosphate (UMP) molecules confined in multi-lamellar phospholipid b

135 the conversion of 5'-uridine monophosphate (UMP) to UMP-NeuAc, which was found to be an inactive sia

136 nophosphate (IMP) and uridine monophosphate (UMP) were only 30% of those found in the wild-type cells

137 y annotating N-methyl-uridine monophosphate (UMP), lysomonogalactosyl-monopalmitin, N-methylalanine,

138 nversion of uracil to uridine monophosphate (UMP).

139 supplemental uridine (as its monophosphate, UMP; 0.5%) and choline (0.1%) via the diet, and docosahe

140 for the pyrimidine nucleoside monophosphates UMP and CMP.

141 s have activities very similar to the native UMP synthase, but unlike the bifunctional protein, the d

142 In the absence of UMP, initial-rate curves for CP are hyperbolic.

143 10 and 220 nM in the presence and absence of UMP, respectively.

144 By contrast, the actions of UMP and IMP together must be explained with a competitiv

145 otide metabolism, namely the ODC activity of UMP synthase.

146 espect to uptake of orotic acid, affinity of UMP synthase for its substrates, or UMP synthase gene-co

147 inities that surpass the binding affinity of UMP.

148 anionic substituents at the 6-carbon atom of UMP.

149 s is initiated by the covalent attachment of UMP to the terminal protein VPg, yielding VPgpU and VPgp

150 The binding of UMP and F-UMP to ScOMPDC results in 0.5 and 1.4 unit dec

151 The binding of UMP and F-UMP to ScOMPDC results in a greater than 5 x 1

152 The binding of UMP to the allosteric domain inhibits the dimerization o

153 The concentration of UMP required for half-maximal effect was 2.5 microM.

154 The concentration of UMP required for half-maximal stimulation of binding of

155 effective at 100 times the concentration of UMP.

156 n vitro, at physiological concentrations, of UMP synthase, the two isolated catalytic domains prepare

157 id synthesis by catalyzing the conversion of UMP, CMP, and dCMP into their diphosphate form.

158 diastereomer mixture prepared by coupling of UMP-morpholidate with fluoromethylenebis(phosphonic acid

159 liganded conformation before dissociation of UMP and were inconsistent with several other kinetic mec

160 6-amino acid UMP/CMPK was the actual form of UMP/CMPK, rather than the 228-amino acid form as suggest

161 UDP-GlcNAc, with the resulting generation of UMP, a potent and competitive inhibitor of GnT-IX.

162 sphoenolpyruvate to the 3'-hydroxyl group of UMP.

163 this investigation were the imidazolides of UMP, xanthosine 5'-monophosphate, the bis-monophosphates

164 oriI, templates processive incorporation of UMP into VPg by using a "slide-back" mechanism.

165 Through inhibition of UMP synthase, 5-AzaC also strongly induced expression of

166 e HIV protease and the unfolding kinetics of UMP/CMP kinase, a globular protein from Dictyostelium di

167 lines), showed an unexpected, high level of UMP synthase and was therefore analyzed in detail.

168 of these cell lines showed reduced levels of UMP synthase.

169 s 2 (HRV2) catalyzes the covalent linkage of UMP to the terminal protein (VPg) using poly(A) as a tem

170 PV) RNA synthesis is the covalent linkage of UMP to the terminal protein VPg.

171 The mechanism of UMP attachment at the active site of the transferase is

172 Whereas the enzymatic mechanism of UMP kinase (UK) is well-characterized, the molecular bas

173 replication is initiated when a molecule of UMP is covalently linked to the hydroxyl group of a tyro

174 replication is initiated when a molecule of UMP is covalently linked to the hydroxyl group of a tyro

175 ins prepared by site-directed mutagenesis of UMP synthase, and the yeast ODCase.

176 hydrogen bonds to the phosphoryl oxygens of UMP with lengths of 2.52 and 2.82 A.

177 the nucleophile and the alpha-phosphorus of UMP.

178 The role of UMP/CMPK for the phosphorylation of nucleoside analogues

179 A series of UMP-NeuAc radioisotopomers were prepared by chemical dea

180 ckettsial CTP appears to be the transport of UMP followed by its phosphorylation and the amination of

181 tes, were much poorer substrates than CMP or UMP for this enzyme.

182 mented with uracil, uridine, deoxyuridine or UMP.

183 and in each major phosphatide; giving DHA or UMP (plus choline) produced smaller increases in some of

184 AE1 is not inhibited by UDP-Glc, UDP-Gal, or UMP.

185 upling between MgADP and either ornithine or UMP.

186 inity of UMP synthase for its substrates, or UMP synthase gene-copy number.

187 These results show that oral UMP, a uridine source, enhances the synthesis of CDP-cho

188 All three allosteric ligands, ornithine, UMP, and IMP, act by modifying the affinity of CPS for t

189 habeta)2 dimer in the presence of ornithine, UMP, or IMP.

190 The amounts of [(32)P]UMP incorporated into VPgpUpU(OH) and negative-strand RN

191 the ubiquitin-mediated proteolysis pathway (UMP).

192 case, one would expect uridine 5'-phosphate (UMP) derivatives with bulky anionic substituents at C6 t

193 oy the communication between the PII and PII-UMP binding sites and the AT and AR active sites.

194 educed by PII-UMP, whereas glutamine and PII-UMP competed for the enzyme.

195 gulation of ATase by glutamine, PII, and PII-UMP consistent with all data is presented.

196 we observed that essentially all PII and PII-UMP interactions were influenced by ADP.

197 and PII-UMP, these domains bound PII and PII-UMP significantly better when linked to the central regi

198 he binding of these effectors to PII and PII-UMP was characterized.

199 ent with the protein activators (PII and PII-UMP) binding to the enzyme domain with the opposing acti

200 clusively through its binding to PII and PII-UMP, did not alter the binding of PII or PII-UMP to the

201 polypeptides were indifferent to PII and PII-UMP, or their ATase activity was inhibited by either PII

202 domains of ATase bound poorly to PII and PII-UMP, these domains bound PII and PII-UMP significantly b

203 which did so by binding only to PII and PII-UMP.

204 sensors of 2-ketoglutarate were PII and PII-UMP.

205 ha-ketoglutarate, which binds to PII and PII-UMP.

206 o contain two distinct sites for PII and PII-UMP.

207 ultiple sites for the binding of PII and PII-UMP.

208 and pyrophosphate (PPi) released before PII-UMP.

209 g (AR) activity of ATase is activated by PII-UMP and inhibited by unmodified PII and by glutamine.

210 l-removing (AR) reaction is activated by PII-UMP and is inhibited by glutamine and by PII.

211 ed by glutamine and its level reduced by PII-UMP, whereas glutamine and PII-UMP competed for the enzy

212 transduction protein and is inhibited by PII-UMP.

213 UMP, did not alter the binding of PII or PII-UMP to the enzyme.

214 on or inhibition of the enzyme by PII or PII-UMP.

215 le not eliminating the binding of PII or PII-UMP.

216 activity was inhibited by either PII or PII-UMP.

217 Our results were consistent with PII, PII-UMP, and glutamine shifting the enzyme among at least si

218 The PII, PII-UMP, and glutamine sites were in communication so that t

219 hibited by the uridylylated form of PII, PII-UMP.

220 The deduced amino acid sequence of the plant UMP/CMP kinase has 50% identity with other eukaryotic UM

221 Following proteolytic digestion, the plant UMP/CMP kinase was purified and analyzed for its structu

222 Addition of the PyrR regulatory protein plus UMP led to greatly increased termination.

223 Transcriptional attenuation by PyrR plus UMP was also demonstrated in vitro with templates from t

224 gly promoted by the combination of PyrR plus UMP.

225 ate, uracil (2.2 A resolution), its product, UMP (2.5 A resolution), and the prodrug, 5-fluorouracil

226 e of the LdUMPS in complex with its product, UMP.

227 were measured using mixtures of radiolabeled UMP-NeuAc's as the donor substrate and N-acetyllactosami

228 In the present study, adult gerbils received UMP (1 mmol/kg), a constituent of human breast milk and

229 reiterative transcription (i.e., repetitive UMP addition) within the 8-bp T.

230 In particular, positions of the respective UMP alpha-phosphoryl groups differ by approximately 4 A.

231 5-fold tighter in the presence of saturating UMP or UDP and 150- fold tighter with saturating UTP, su

232 for the linkage of both the first and second UMPs to VPg, 3) VPgpUpU is synthesized by a "slide-back"

233 The smallest UMP dose that significantly increased brain CDP-choline

234 f the novel sugar-nucleotide donor substrate UMP-NeuAc.

235 anished with use of the slow donor substrate UMP-NeuAc.

236 In the absence of the prime substrate UMP, LipL is able to catalyze oxidative decarboxylation

237 PyrR, but concentrations 10-fold higher than UMP were required; UDP was only effective at 100 times t

238 model, consistent with previous reports that UMP and IMP bind to the same site.

239 The UMP pyrimidine ring stacks against the uracil base of th

240 interactions between the active site and the UMP group of E-His(166)-UMP provide little or no stabili

241 kage is a phosphoramidate formed between the UMP moiety and the His 166 N(epsilon)(2) of GalT, with H

242 ption whereby termination is governed by the UMP-dependent binding of PyrR to pyr RNA and provide pur

243 Young rats eating the UMP-containing diet exhibited similar increases in basal

244 onclusion derives from studies employing the UMP synthesis inhibitor N-phosphonacetyl-L-aspartate (PA

245 None of the variants formed the UMP-enzyme in detectable amounts upon reaction with UDP-

246 ferase (OMP synthase, EC 2.4.2.10) forms the UMP precursor orotidine 5'-monophophate (OMP) from orota

247 glucose-1-phosphate (glu-1-P), and forms the UMP-GALT intermediate.

248 However, the UMP . GCP complex was 4.8 degrees less closed than the g

249 n bonding with the phosphoryl oxygens of the UMP moiety, which is bonded to His 166 in the intermedia

250 (31)P NMR studies of the UMP product generated from UDP-2,3-diacylglucosamine in

251 (ScOMPDC) catalyze the exchange of H6 of the UMP product with solvent deuterium allows an estimate of

252 tidylate decarboxylase (ODC) activity of the UMP synthase enzyme complex that catalyzes an early even

253 n authentic and well conserved member of the UMP/CMP kinase group while EhAK is the most divergent me

254 hat glutamine at position 188 stabilizes the UMP-GALT intermediate through hydrogen bonding and enabl

255 Kinetic analysis revealed that the UMP/CMP kinase preferentially uses ATP (Michaelis consta

256 hat delivers a solvent-derived proton to the UMP product; the active site of KGPDC contains a homolog

257 active sites underwent uridylylation to the UMP-enzyme, similar to wild-type GalT, upon reaction wit

258 the presence of SII, incorporation of 4-thio-UMP into RNA, and irradiation and was sensitive to treat

259 e EhUK was more similar (48-49% identity) to UMP/CMP kinases.

260 al ion-independent decarboxylation of OMP to UMP and CO(2).

261 he enzyme-catalyzed transformation of OMP to UMP may have less of an energetic impact than commonly t

262 led to uracil and then phosphoribosylated to UMP in the parasite by LdUPRT.

263 atives by spontaneous addition of sulfite to UMP and to OMP.

264 ENTPD5 hydrolyzes UDP to UMP to promote protein N-glycosylation and folding in ER

265 lucosyltransferase inhibitory product UDP to UMP, and that the latter product then exits the lumen of

266 ation of an ER enzyme that hydrolyzes UDP to UMP.

267 version of 5'-uridine monophosphate (UMP) to UMP-NeuAc, which was found to be an inactive sialyl dono

268 sted the kinetic competence of the wild-type UMP-enzyme.

269 The unstable UMP-GALT allows single displacement of glu-1-P with rele

270 examined, but no catalysis of [(14)C]uracil-UMP and [(32)P]PP(i)-phosphoribosylpyrophosphate exchang

271 These KIEs observed using UMP-NeuAc are much larger than those previously measured

272 When UMP or UTP is bound to the PyrR regulatory protein, it b

273 TP (Michaelis constant [Km] = 29 microM when UMP is the other substrate and Km = 292 microM when CMP

274 hine and IMP function as activators, whereas UMP is an inhibitor.

275 oline (ACh) synthesis, we determined whether UMP administration also affects ACh levels in striatum a

276 CP rate curves showed no sigmoidicity, while UMP rate curves had sigmoidicity exaggerated by a low ma

277 formation of an (alphabeta)4 tetramer while UMP favors the formation of an (alphabeta)2 dimer.

278 pses, particularly when co-administered with UMP.

279 uents at C6 to be bound weakly compared with UMP, which is unsubstituted at C6.

280 0-A resolution structure of the complex with UMP/GCP and a 2.8-A resolution structure of the complex

281 nor are they removed from an FAD resin with UMP (which shares a pattern of hydrogen bond donors and