ライフサイエンスコーパス: mutase

1 then transfers it directly to the dependent mutase.

2 , which is a chaperone for methylmalonyl-CoA mutase.

3 l homology to the Escherchia coli chorismate mutase.

4 tributions of various residues in chorismate mutase.

5 ymes, methionine synthase and MMA-coenzyme A mutase.

6 he high value AdoCbl product to the acceptor mutase.

7 s, methionine synthase and methylmalonyl-CoA mutase.

8 with its partner protein, methylmalonyl-CoA mutase.

9 the B(12)-dependent enzyme methylmalonyl-CoA mutase.

10 also observed for AdoCbl bound to glutamate mutase.

11 by the radical B12 enzyme, methylmalonyl-CoA mutase.

12 approximately 100-fold by methylmalonyl-CoA mutase.

13 obalamin)-dependent enzyme methylmalonyl CoA mutase.

14 is modulated by the enzyme methylmalonyl-CoA mutase.

15 topyranose by the enzyme UDP-galactopyranose mutase.

16 rs, isocitrate lyase and phosphoenolpyruvate mutase.

17 ed to have only independent phosphoglycerate mutase.

18 t identified in Bacillus subtilis chorismate mutase.

19 e not converted to their beta-isomers by the mutase.

20 due to an inactive form of methylmalonyl-CoA mutase.

21 ma carboxylate of the substrate in glutamate mutase.

22 he amino group of the substrate in glutamate mutase.

23 s, methionine synthase and methylmalonyl-CoA mutase.

24 by methionine synthase and methylmalonyl-CoA mutase.

25 5'-deoxyadenosylcobalamin-dependent acyl-CoA mutase.

26 currently misannotated as methylmalonyl-CoA mutases.

27 it belongs to the *AroQ class of chorismate mutases.

28 a new subfamily of B(12)-dependent acyl-CoA mutases.

29 Phosphoglycerate mutase 1 (PGAM1) functions in glycolysis.

30 that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1) regulates anabolic biosynthesis by cont

31 that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated in human cancers

32 beled the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), resulting in enzyme inhibition.

33 acute mechanism underlying phosphoglycerate mutase 1 upregulation.

34 e 2) and Bevacizumab/PGAM1 (Phosphoglycerate mutase 1) are interactions found in this study with inde

35 that the glycolytic enzyme phosphoglycerate mutase-1 (PGAM1) is negatively regulated by Sirt1, a mem

36 ssing the glycolytic enzyme phosphoglycerate mutase-1 severely impaired the ability of CD8+ T cells t

37 ycolytic enzymes (aldolase, phosphoglycerate mutase 2, beta enolase and glycogen phosphorylase), tran

38 significant degradation of phosphoglycerate mutase 2, glycogen phosphorylase muscle form, pyruvate k

39 hila lifespan, and identify Phosphoglycerate Mutase 5 (PGAM5) as a mediator of this response.

40 Phosphoglycerate mutase 5 (PGAM5) is an atypical mitochondrial Ser/Thr ph

41 e mitochondrial phosphatase phosphoglycerate mutase 5 (PGAM5).

42 homology to members of the phosphoglycerate mutase/acid phosphatase (PGM/AcP) family of enzymes, wit

43 ncorrect oxidation state gains access to the mutase active site and is not released if generated duri

44 ypothesized that the loop serves to gate the mutase active site, interconverting between an open conf

45 nant enzymes showed typical phosphoglycerate mutase activities in both the glycolytic and gluconeogen

46 d interactions involved in inhibition of the mutase activity by vanadate and identifies a water molec

47 tely 240-fold decrease in the isobutyryl-CoA mutase activity compared with wild-type IcmF.

48 -pyruvate lyase with adventitious chorismate mutase activity from Pseudomonas aerugionsa (PchB) achie

49 y approximately 60-70%, and total chorismate mutase activity in corolla tissue is reduced by 80-85% c

50 nitric oxide (NO) inhibits methylmalonyl-CoA mutase activity in rodent cell extracts.

51 Ethylmalonyl-CoA mutase activity increased to a level sufficient for the

52 ce of Mg2+ MbtI has a promiscuous chorismate mutase activity similar to that of the isochorismate pyr

53 PGA mutase activity was dependent upon the presence of dival

54 Mutase activity was required for the incorporation of Ga

55 lar NO synthesis increased methylmalonyl-CoA mutase activity when measured subsequently in cell extra

56 or PCM-F displayed detectable isobutyryl-CoA mutase activity, demonstrating that PCM represents a nov

57 extorquens, which supports methylmalonyl-CoA mutase activity, serves dual functions; i.e., it tailors

58 amily, combined with the observed chorismate mutase activity, suggests that MbtI may exploit a sigmat

59 ed catalytic efficiency but loses detectable mutase activity.

60 g the eponymous activity and also chorismate mutase activity.

61 ylmalonyl-CoA mutase and stimulates in vitro mutase activity.

62 those measured in steady-state assays of PGA mutase activity.

63 roxyl by the enzyme phosphoacetylglucosamine mutase (AGM1).

64 Five of these (phosphoglycerate mutase, alcohol dehydrogenase, thioredoxin peroxidase, c

65 tly characterized archaeal methylmalonyl-CoA mutase, allowed demonstration of its robust PCM activity

66 al B(12)-dependent enzyme, methylmalonyl-CoA mutase, although its precise role is not understood.

67 structures are similar to that of chorismate mutase, although there is little sequence homology and n

68 ganization similar to that of isobutyryl-CoA mutase and a recently characterized archaeal methylmalon

69 In the presence of methylmalonyl-CoA mutase and ATP, AdoCbl is transferred from ATR to the ac

70 ial enzymes, mitochondrial methylmalonyl-CoA mutase and cytosolic methionine synthase, respectively.

71 balamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have both medical and b

72 n skeleton rearrangements, methylmalonyl-CoA mutase and isobutyryl-CoA mutase (ICM).

73 s in the closely related phosphoenolpyruvate mutase and isocitrate lyase enzymes.

74 n protein of AdoCbl-dependent isobutyryl-CoA mutase and its corresponding G-protein chaperone, which

75 p, known to play a catalytic role in the PEP mutase and lyase branches of the superfamily, adopts an

76 on constant for binding of methylmalonyl-CoA mutase and MeaB ranges from 34 +/- 4 to 524 +/- 66 nm, d

77 between the radical enzyme methylmalonyl-CoA mutase and MeaB, which are discussed.

78 the reaction catalyzed by methylmalonyl-CoA mutase and on the thermodynamics of cofactor binding.

79 New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all th

80 d with the axoneme, whereas phosphoglycerate mutase and pyruvate kinase primarily reside in the deter

81 MeaB forms a complex with methylmalonyl-CoA mutase and stimulates in vitro mutase activity.

82 -dependent assembly of holomethylmalonyl-CoA mutase and subsequent protection of radical intermediate

83 nverted to phosphonopyruvate (Ppyr) with PEP mutase and then to Pald with Ppyr decarboxylase.

84 cificity and the catalytic scope of acyl-CoA mutases and could benefit engineering efforts for biotec

85 main forms an ACT (aspartokinase, chorismate mutase, and TyrA) fold and contains the tetrameric inter

86 Thus, NO inhibition of methylmalonyl-CoA mutase appeared to be from the reaction of NO with both

87 Acyl-CoA mutases are a growing class of adenosylcobalamin-depende

88 Coenzyme B(12)-dependent acyl-CoA mutases are radical enzymes catalyzing reversible carbon

89 esent study, the DAHPS (aroA) and chorismate mutase (aroQ) activities of B. subtilis DAHPS are separa

90 with UDP-[14C]Galp and recombinant UDP-Galp mutase as the source of [14C]Galf for galactan biosynthe

91 ble mutant (Y89F/R207Q) of methylmalonyl-CoA mutase as well as of the single mutants (Y89F and R207Q)

92 Methylmalonyl-CoA mutase belongs to the class of adenosylcobalamin (AdoCbl

93 group of cofactor-dependent phosphoglycerate mutase/bisphosphoglycerate mutase enzymes (PGM/bPGM; EC

94 ection against oxidative inactivation of the mutase by MeaB is dependent upon the presence of nucleot

95 The inhibition of methylmalonyl-CoA mutase by NO was likely of physiological relevance becau

96 Phosphoglycerate mutases catalyze the interconversion of 2- and 3-phospho

97 bond homolysis rate in the methylmalonyl-CoA mutase-catalyzed reaction has been evaluated by site-dir

98 the initial stages of the methylmalonyl-CoA-mutase-catalyzed reaction.

99 site residue, R207, in the methylmalonyl-CoA mutase-catalyzed reaction.

100 bstrate specificity and predict new acyl-CoA mutase-catalyzed reactions.

101 Methylmalonyl-CoA mutase catalyzes the adenosylcobalamin-dependent rearran

102 denosylcobalamin-dependent methylmalonyl-CoA mutase catalyzes the interconversion of methylmalonyl-Co

103 Methylmalonyl-CoA mutase catalyzes the isomerization of methylmalonyl-CoA

104 Previous work has indicated that PEP mutase catalyzes the rearrangement of phosphoenolpyruvat

105 Class I PurE (N5-carboxyaminoimidazole mutase) catalyzes a chemically unique mutase reaction.

106 (N(5)-CAIR) synthetase (PurK) and N(5)-CAIR mutase (class I PurE).

107 ex formed by two pathway enzymes: chorismate mutase (CM) and 3-deoxy-d-arabino-heptulosonate 7-phosph

108 tein is a homodimer that exhibits chorismate mutase (CM) and prephenate dehydrogenase (PDH) activitie

109 one to flavanone, whereas E. coli chorismate mutase (CM) catalyzes the pericyclic rearrangement of ch

110 rate enhancement provided by the chorismate mutase (CM) enzyme for the Claisen rearrangement of chor

111 ivo selection to the evolution of chorismate mutase (CM) enzymes.

112 7-phosphate synthase (DAH7PS) and chorismate mutase (CM) from Geobacillus sp.

113 The catalytic reaction of chorismate mutase (CM) has been the subject of major current attent

114 paradigm has been challenged for chorismate mutase (CM), a well-characterized metabolic enzyme that

115 cted from the crystal structure of glutamate mutase complexed with the substrate.

116 Chorismate mutase converts chorismate into prephenate for aromatic

117 s lanosterol synthase ((S)-2,3-epoxysqualene mutase (cyclizing, lanosterol forming), EC 5.4.99.7).

118 expected from previously reported chorismate mutase data.

119 to a growth based selection in a chorismate mutase deficient strain.

120 lity to complement an auxotrophic chorismate mutase deletion strain.

121 butable to modulation of bisphosphoglycerate mutase, direct inhibition of GEs by pervanadate, or oxid

122 c pathways can be predicted by examining PEP mutase diversity.

123 The C-terminal phosphoglycerate mutase domain of PGAM5 shares homology with the catalyti

124 n six positions of the engineered chorismate mutase domain of the Escherichia coli chorismate mutase-

125 vity and the cofactor- and substrate-binding mutase domains with isomerase activity.

126 and at the active site of E. coli chorismate mutase (EcCM) have been compared.

127 interface of the Escherichia coli chorismate mutase (EcCM) homodimer to be dependent on incorporation

128 e lower half of glycolysis (phosphoglycerate mutase, enolase, and pyruvate kinase).

129 phosphoglycerate mutase/bisphosphoglycerate mutase enzymes (PGM/bPGM; EC 5.4.2.1/5.4.2.4).

130 A definitive mechanism for the chorismate mutase enzymes is provided.

131 ee of hydrogen tunneling occurs in glutamate mutase, even though the intrinsic kinetic isotope effect

132 ding that an engineered monomeric chorismate mutase exhibits catalytic efficiency similar to the natu

133 Here we show that phosphoglycerate mutase family 5 (PGAM5) functions as a phosphohistidine

134 vidence that members of the phosphoglycerate mutase family 5 (PGAM5) proteins are involved in the INr

135 e mitochondrial phosphatase phosphoglycerate mutase family member 5 (PGAM5), a putative downstream ef

136 the mitochondrial protein, phosphoglycerate mutase family member 5 (PGAM5), displayed a Parkinson's-

137 und in other members of the phosphoglycerate mutase family, including a conserved histidine that is a

138 identified a member of the phosphoglycerate mutase family, PGAM5, as a novel substrate for Keap1.

139 la tertiaricarbonis as a novel member of the mutase family.

140 units of the AdoCbl-dependent isobutyryl-CoA mutase flanking a G-protein chaperone and named it isobu

141 e has a modest effect on the affinity of the mutase for the 5'-deoxyadenosylcobalamin (AdoCbl) cofact

142 pending on the combination of nucleotide and mutase form.

143 tes that MeaB is necessary for protection of mutase from inactivation during catalysis.

144 MeaB functions to protect methylmalonyl-CoA mutase from irreversible inactivation.

145 MeaB and methylmalonyl-CoA mutase from M. extorquens were cloned and purified in th

146 The crystal structure of PEP mutase from Mytilus edulis in complex with a substrate-a

147 ed recombinant, independent phosphoglycerate mutases from C. elegans and the human-parasitic nematode

148 lyzed by evolutionarily unrelated chorismate mutases from Escherichia coli and Bacillus subtilis.

149 Comparisons of chorismate mutases from multiple plants suggest that subtle differe

150 rotein chaperone and named it isobutyryl-CoA mutase fused (IcmF).

151 this fusion protein as IcmF (isobutyryl-CoA mutase fused).

152 aracterized and homologous methylmalonyl-CoA mutase/G-protein chaperone system.

153 cific 16S rDNA, H. pylori phosphoglucosamine mutase (glmM) and urease B (ureB) gene of H. heilmannii

154 Glutamate mutase (GM) is a cobalamin-dependent enzyme that catalyz

155 essential glycolytic enzyme phosphoglycerate mutase (Gpm).

156 The recombinant mutase has a pH optimum of 8.5, a k(cat) value of 0.015

157 ecent spate of discoveries of novel acyl-CoA mutases has engendered a growing appreciation for the di

158 (AdoCbl)-dependent enzyme, methylmalonyl-CoA mutase, has been studied.

159 Nucleotide sugar mutases have been demonstrated to interconvert UDP-Larab

160 Here, we describe 2-hydroxyisobutyryl-CoA mutase (HCM) found in the bacterium Aquincola tertiarica

161 enzyme B12-dependent 2-hydroxyisobutyryl-CoA mutase (HCM) is a radical enzyme catalyzing the stereosp

162 Like isobutyryl-CoA mutase, HCM consists of a large substrate- and a small B

163 reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery of 1 equivalent of

164 strate specificity and catalysis in acyl-CoA mutases, however, is incomplete.

165 hionine synthase or methylmalonyl-coenzyme A mutase; however, it did inhibit the in vivo activities o

166 overed family members include isobutyryl-CoA mutase (ICM), which interconverts isobutyryl-CoA and n-b

167 methylmalonyl-CoA mutase and isobutyryl-CoA mutase (ICM).

168 The presence of active mutase in double mutants defective in MeaB and in the sy

169 brates, utilize independent phosphoglycerate mutase in glycolytic and gluconeogenic pathways and that

170 sis product Co2+ Cbl when bound to glutamate mutase in the presence of substrate (or a substrate anal

171 eview focuses on the involvement of acyl-CoA mutases in central carbon and secondary bacterial metabo

172 zyme is a structural homologue of chorismate mutases in the AroQalpha class despite low sequence iden

173 sence of nucleotides) with methylmalonyl-CoA mutase (in the presence and absence of cofactor).

174 e-6-phosphate isomerase and phosphoglycerate mutase), in trehalose-6-P metabolism (trehalose-6-P synt

175 ral fusion protein variant of isobutyryl-CoA mutase, in complex with the adenosylcobalamin cofactor a

176 the crystal structures of wild-type and D58A mutases, in the apo state and in complex with Mg(II), ar

177 ed Cbl-dependent isomerase methylmalonyl-CoA mutase indicate that a common mechanism by which the cof

178 MIC activity did not correlate with UDP-Gal mutase inhibition, suggesting an alternative primary cel

179 nds was screened for M. tuberculosis UDP-Gal mutase inhibition.

180 Binding of 2-methyleneglutarate to glutamate mutase initiates homolysis of adenosylcobalamin.

181 hoglucose isomerase (PGI) and phosphoglucose mutase interconverting glucose 6-phosphate, fructose 6-p

182 nic microorganisms by a cofactor-independent mutase (iPGM) structurally distinct from the mammalian c

183 glycerate-independent phosphoglycerate (PGA) mutases [iPGMs].

184 UDP-galactopyranose mutase is a flavoprotein which catalyses the interconver

185 Methylmalonyl-CoA mutase is a key enzyme in intermediary metabolism, and c

186 e findings demonstrate that ethylmalonyl-CoA mutase is a metabolic control point in the EMC pathway,

187 by adenosyltransferase to methylmalonyl-CoA mutase is gated by a small G protein, MeaB.

188 The reaction mechanism of this mutase is intriguing because the anomeric oxygen forms a

189 nalogue of GTP, the binding of AdoCbl to the mutase is not detected.

190 Glutamate mutase is one of a group of adenosylcobalamin-dependent

191 Glutamate mutase is one of a group of adenosylcobalamin-dependent

192 ), a member of the phosphoenolpyruvate (PEP) mutase/isocitrate lyase (PEPM/ICL) superfamily, hydrolyz

193 lly and functionally novel member of the PEP mutase/isocitrate lyase superfamily and therefore target

194 As with other PEP mutase/isocitrate lyase superfamily members, the protein

195 the lyase branch of the phosphoenolpyruvate mutase/isocitrate lyase superfamily to provide insight i

196 e (OAH), a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily, catalyzes the hydro

197 zyme that belongs to the phosphoenolpyruvate mutase/isocitrate lyase superfamily.

198 ed the three Arabidopsis thaliana chorismate mutase isoforms (AtCM1-3) and determined the x-ray cryst

199 alamin-dependent enzyme 2-methyleneglutarate mutase, it reacts with glutamate mutase to cause time-de

200 es aminoimidazole ribonucleotide carboxylase/mutase, LarC binds Ni and could act in Ni delivery or st

201 In humans, deficiencies in the mutase lead to methylmalonic aciduria, a rare disease th

202 The phosphoglycerate mutase-like domain of Sts-1 (Sts-1(PGM)) has a potent ph

203 xicana cofactor-independent phosphoglycerate mutase (Lm iPGAM) crystallised with the substrate 3-phos

204 sylcobalamin cofactor onto methylmalonyl-CoA mutase (MCM) and precludes loading of inactive cofactor

205 Within this family, methylmalonyl-CoA mutase (MCM) is the best studied and is the only member

206 in coenzyme B12-dependent methylmalonyl-CoA mutase (MCM) lead to methylmalonyl aciduria, a rare dise

207 itochondrial B12-dependent methylmalonyl-CoA mutase (MCM), HCM has a highly conserved domain architec

208 Cbl or coenzyme B(12)), to methylmalonyl-CoA mutase (MCM), resulting in holoenzyme formation.

209 enosyl cobalamin-dependent methylmalonyl-CoA mutase (MCM).

210 alpha-Methyleneglutarate mutase (MGM) catalyzes the rearrangement of 2-methyleneg

211 Methylmalonyl-CoA mutase (MMCM) is an enzyme that utilizes the adenosylcob

212 des a monofunctional and secreted chorismate mutase (*MtCM) with a 33-amino-acid cleavable signal seq

213 d by defective activity of methylmalonyl-CoA mutase (MUT) that exhibits multiorgan system pathology.

214 f the mitochondrial enzyme methylmalonyl-CoA mutase (MUT), is often complicated by end stage renal di

215 ), caused by deficiency of methylmalonyl-CoA mutase (MUT), usually presents in the newborn period wit

216 itochondrial B12-dependent methylmalonyl-CoA mutase (MUT).

217 the vitamin B12-dependent methylmalonyl-CoA-mutase MutAB.

218 N5-Carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase or PurE) from Escherichia coli ca

219 on the branch leading to Trp and chorismate mutase on the branch leading to Phe and Tyr.

220 minoimidazole ribonucleotide mutase (N5-CAIR mutase or PurE) from Escherichia coli catalyzes the reve

221 nnomutase (PMM), phospho-N-acetylglucosamine mutase (PAGM) and phosphoglucomutase (PGM) reversibly ca

222 d in vivo by the AtoAD and methylmalonyl-CoA mutase pathways, respectively, to produce 15-methyl-6-dE

223 potential of the isovaleryl-CoA/pivalyl-CoA mutase (PCM) reaction, we initially attempted to enginee

224 osphonopyruvate, catalyzed by the enzyme PEP mutase (PepM), is shared by the vast majority of known p

225 the interaction of Pak with phosphoglycerate mutase (PGAM)-B, an enzyme of the glycolytic pathway.

226 on of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells.

227 cated within its C-terminal phosphoglycerate mutase (PGM) homology domain and key for the regulation

228 sphate phosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first structure of a s

229 ified the glycolytic enzyme phosphoglycerate mutase (PGM).

230 Phosphoglycerate mutases (PGMs) catalyze the isomerization of 2- and 3-ph

231 have cloned and characterized two CHORISMATE MUTASE (PhCM1 and PhCM2) cDNAs from petunia.

232 Phosphoglucosamine mutase (PNGM) is an evolutionarily conserved bacterial e

233 ivity of the biosynthetic enzymes chorismate mutase, prephenate dehydratase, and prephenate dehydroge

234 se domain of the Escherichia coli chorismate mutase-prephenate dehydratase.

235 , ADCS, IS, and SS do not possess chorismate mutase promiscuous activity, contrary to several previou

236 rboxyaminoimidazole ribonucleotide (N5-CAIR) mutase (PurE) catalyzes the reversible interconversion o

237 rfamily, yet it has evolved to function as a mutase rather than as a phosphatase.

238 s associated with this process for glutamate mutase reacting with deuterated glutamate.

239 an entropic penalty for the enzyme-catalyzed mutase reaction (DeltaS(++) = -12.1 +/- 0.6 cal/(mol K))

240 ions tested, and (iii) the methylmalonyl-CoA mutase reaction is reversible, but its reversibility dec

241 hionine (SAM) protein PylB mediates a lysine mutase reaction that produces 3-methylornithine, which i

242 dazole mutase) catalyzes a chemically unique mutase reaction.

243 es methionine synthase and methylmalonyl-CoA mutase, respectively.

244 show that PhCM1 is the principal CHORISMATE MUTASE responsible for the coupling of metabolites from

245 PEP mutase sequence conservation is strongly correlated with

246 where its partner protein methylmalonyl-CoA mutase should bind.

247 However, it is thus far the only acyl-CoA mutase showing substrate specificity for hydroxylated ca

248 the catalytic domains of ThiC and glutamate mutase shows that these two enzymes share similar active

249 group in AdoCbl-dependent methylmalonyl-CoA mutase shows the enzymic and enzyme-free data sets are i

250 analyzed by 2H NMR, which revealed that the mutase shuttles the pro-3S hydrogen to C2 of the beta-is

251 eficiencies can result from mutations in the mutase structural gene or from mutations that impair the

252 sophilic enzyme Bacillus subtilis chorismate mutase substrate complex (BsCM x S): (i) electrostatic i

253 mulations of Thermus thermophilus chorismate mutase substrate complex (TtCM x S) have been carried ou

254 s identify critical determinants of acyl-CoA mutase substrate specificity and predict new acyl-CoA mu

255 e same as that of other isocitrate lyase/PEP mutase superfamily members, including a swapped eighth h

256 of the isocitrate lyase/phosphoenolpyruvate mutase superfamily, a substrate screen that employed a (

257 s (GTs) TaGT43-4 and TaGT47-13; two putative mutases (TaGT75-3 and TaGT75-4) and two non-GTs; a germi

258 fector control in the Arabidopsis chorismate mutases than previously reported.

259 t the protein was a moderately effective PGA mutase that also exhibited low levels of phosphohydrolas

260 d by a patient mutation in methylmalonyl-CoA mutase that does not impair the activity of this enzyme

261 of RGP2, a gene that encodes a UDP-arabinose mutase that interconverts UDP-arabinopyranose and UDP-ar

262 o be interconverted into UDP-Araf by UDP-Ara mutases that are located outside on the cytosolic surfac

263 psis RGP protein family members as UDP-L-Ara mutases that catalyze the formation of UDP-Araf from UDP

264 he closely related isomerase, isobutyryl-CoA mutase the homologous residues are F80 and Q198, respect

265 ence databases as carboxyphosphoenolpyruvate mutase, the enzyme is actually a C-C bond cleaving lyase

266 nit transporter (Wzx), and a galactofuranose mutase, the enzyme that promotes synthesis of UDP-Galf,

267 ormans strain that lacks UDP-galactopyranose mutase; this enzyme forms UDP-Galf, the nucleotide sugar

268 neglutarate mutase, it reacts with glutamate mutase to cause time-dependent inhibition of the enzyme.

269 study of the Thermus thermophilus chorismate mutase (TtCM) is described by using quantum mechanics (s

270 nzyme uridine 5'-diphosphate galactopyranose mutase (UGM or Glf) catalyzes the interconversion of UDP

271 generated by the enzyme UDP-galactopyranose mutase (UGM or Glf).

272 K. kingae genes encoding UDP-galactopyranose mutase (ugm) and two putative galactofuranosyl transfera

273 UDP-galactopyranose mutase (UGM) catalyzes the conversion of UDP-galactofura

274 nose biosynthetic enzyme UDP-galactopyranose mutase (UGM) from T. cruzi, which are the first structur

275 UDP-Galactopyranose mutase (UGM) is a flavin-containing enzyme that catalyze

276 UDP-galactopyranose mutase (UGM) is a flavin-containing enzyme that catalyze

277 UDP-galactopyranose mutase (UGM) is a flavoenzyme that catalyzes the convers

278 UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose

279 UDP-galactopyranose mutase (UGM) requires reduced FAD (FAD(red)) to catalyze

280 lactose synthase (YerE), UDP-galactopyranose mutase (UGM), and type II isopentenyl diphosphate:dimeth

281 A key enzyme, UDP-galactopyranose mutase (UGM), that participates in Galf incorporation me

282 LPG biosynthetic enzyme, UDP-galactopyranose mutase (UGM).

283 Galp) by the flavoenzyme UDP-galactopyranose mutase (UGM).

284 d-galactose produced by UDP-galactopyranose mutases (UGMs), is present in surface glycans of some pr

285 ely 1.5-fold higher rate than with wild-type mutase under single-turnover conditions.

286 recently demonstrated that an isobutyryl-CoA mutase variant, IcmF, a member of this enzyme family tha

287 ormation of 5'-deoxyadenosine when glutamate mutase was reacted with [5'-(3)H]adenosylcobalamin and L

288 For one of these enzymes, glutamate mutase, we have investigated whether hydrogen tunneling

289 llosteric regulation in the plant chorismate mutases, we analyzed the three Arabidopsis thaliana chor

290 alcium-binding protein, and phosphoglycerate mutase were also identified.

291 phosphorylation of NME1 and phosphoglycerate mutase were used with immunoblotting and sequencing IgG

292 yryl-CoA and n-butyryl-CoA; ethylmalonyl-CoA mutase, which interconverts (2R)-ethylmalonyl-CoA and (2

293 hylsuccinyl-CoA; and 2-hydroxyisobutyryl-CoA mutase, which interconverts 2-hydroxyisobutyryl-CoA and

294 the gene encoding phosphoenolpyruvate (PEP) mutase, which is required for the biosynthesis of most p

295 the ground state is compared with chorismate mutase whose catalytic prowess, when compared with water

296 The structures of Klebsiella pneumoniae mutase with FAD and with FADH- bound have been determine

297 structure of the Mycobacterium tuberculosis mutase with FAD has been determined to 2.25 A.

298 The crystal structure of the mutase with Mg(II) and sulfopyruvate (a phosphonopyruvat

299 have investigated the reaction of glutamate mutase with the glutamate analogue, 2-thiolglutarate.

300 ted allosteric mechanism of yeast chorismate mutase (YCM) was studied by normal mode analysis and tar