ライフサイエンスコーパス: PGM

1 PGM and bPGM are key catalysts of glycolysis that have b

2 PGM binding was within 75-149 amino acids (aa) of Pak1,

3 PGM mRNA was detectable by RNA-blot analysis in all tiss

4 PGM plays a central role in the glycolytic pathway at th

5 PGM-RP is expressed predominantly in muscle with the hig

6 PGM-RP is therefore a good marker of the contractile/dif

7 users versus 19% in low users (P < or =.05; PGM and WM, not significant).

8 ressor of T-cell receptor signaling-1 (Sts-1 PGM) protein.

9 enzymatic activity of phosphoglucomutase 1 (PGM), an important regulatory enzyme in cellular glucose

10 s are altered to their counterparts in Sts-1(PGM) has substantially increased activity.

11 glycerate mutase-like domain of Sts-1 (Sts-1(PGM)) has a potent phosphatase activity that contributes

12 of Sts-2(PGM) is remarkably similar to Sts-1(PGM), including conservation of all catalytic residues.

13 ity of the correspondent Sts-1 domain, Sts-1(PGM), is key for its ability to negatively regulate the

14 In this study, we analyze 10 PGM protein haplotypes with respect to PGM activity, the

15 Overall, our data demonstrate that Sts-2(PGM) adopts the conformation of an active phosphatase wh

16 The function of Sts-2(PGM) as a phosphatase has been less clear, principally b

17 ylated substrates, we demonstrate that Sts-2(PGM) has clear, albeit weak, phosphatase activity.

18 e, we present the crystal structure of Sts-2(PGM) in the phosphorylated active form and bound to VO(3

19 The crystal structure of Sts-2(PGM) is remarkably similar to Sts-1(PGM), including cons

20 arkably similar to the one seen in apo-Sts-2(PGM) suggesting that the spatial arrangement of the cata

21 increases the phosphatase activity of Sts-2(PGM) toward model substrates.

22 s specificity determinants, in that an Sts-2(PGM) triple mutant in which these three amino acids are

23 e activity of the PGM domain of Sts-2, Sts-2(PGM).

24 =.05) in all regions: r = 0.79 (AGM), 0.57 (PGM), and 0.76 (WM).

25 a Glc-1-P uridylyltransferase (cps3U) and a PGM homologue (cps3M) are present in the type 3 capsule

26 The function of this gene product as a PGM was demonstrated through enzymatic and complementati

27 for 24 h, along with reduced synthesis of a PGM identified as a 67-kD phosphoprotein on two-dimensio

28 These observations reveal a PGM/AcP-like enzyme activity involved in the control of

29 clinical lab tests into POC tests that use a PGM.

30 feine reduced CBF (P < or =.05) by 23% (AGM, PGM) and 18% (WM) in all subjects.

31 Two classes of phosphoglucomutases (alpha-PGM and beta-PGM) are distinguished on the basis of thei

32 find a twofold difference in activity among PGM protein haplotypes that is associated with a threefo

33 l technoeconomic model of substitution among PGMs within the automotive sector (the largest user of P

34 passengers was heterozygous for both FVL and PGM.

35 Pak1 and PGM were colocalized in model cell systems and showed fu

36 nzyme assay, we have identified both PMM and PGM activity from one of these genes, Rv3257c (MtmanB).

37 three-dimensional structure of B. anthracis PGM is composed of two structural and functional domains

38 from Escherichia coli but had little if any PGM activity and gave no detectable PGM activity in B. s

39 Beta-PGM conserves the core domain catalytic scaffold of the

40 beta-PGM is a member of the haloacid dehalogenase (HAD) super

41 beta-PGM is unusual among family members in that the common p

42 n X-ray crystal structure of the Mg(2+)-beta-PGM complex is examined in the context of previously rep

43 e, the three-dimensional structure of a beta-PGM and the first view of the true phosphoenzyme interme

44 s of phosphoglucomutases (alpha-PGM and beta-PGM) are distinguished on the basis of their specificity

45 -PGM activation by the Mg(2+) cofactor, beta-PGM activation by Asp8 phosphorylation, and the role of

46 In this paper, we examine beta-PGM activation by the Mg(2+) cofactor, beta-PGM activati

47 tal-binding loop in Mg(2+) anchoring in beta-PGM is consistent with the relatively loose binding indi

48 vidence that the autophosphorylation of beta-PGM by the substrate beta-G1P accounts for the origin of

49 rt a substrate induced-fit mechanism of beta-PGM catalysis, which allows phosphomutase activity to do

50 ons of ground-state analog complexes of beta-PGM involving trifluoroberyllate establish that when the

51 The active site of beta-PGM is located between the core and the cap domain and i

52 er, the trifluoroberyllate complexes of beta-PGM provide a picture of how the enzyme is able to organ

53 Kinetic analyses of the specificity of beta-PGM toward phosphoryl group donors and the specificity o

54 he Mg(2+)-alpha-d-galactose-1-phosphate-beta-PGM, Mg(2+)-phospho-beta-PGM, and Mg(2+)-beta-glucose-6-

55 -G1P accounts for the origin of phospho-beta-PGM in the cell.

56 p donors and the specificity of phospho-beta-PGM toward phosphoryl group acceptors were carried out.

57 se-1-phosphate-beta-PGM, Mg(2+)-phospho-beta-PGM, and Mg(2+)-beta-glucose-6-phosphate-1-phosphorane-b

58 ococcus lactis beta-phosphoglucomutase (beta-PGM) catalyzes the interconversion of beta-d-glucose 1-p

59 phosphorylated beta-phosphoglucomutase (beta-PGM) from Lactococcus lactis has been determined to 2.3

60 e complexes of beta-phosphoglucomutase (beta-PGM) have demonstrated the importance of charge balance

61 Tauhe beta-phosphoglucomutase (beta-PGM) of the haloacid dehalogenase enzyme superfamily (HA

62 -beta-glucose-6-phosphate-1-phosphorane-beta-PGM complexes to identify conformational changes that oc

63 nd to the active site of phosphorylated beta-PGM in such a way as to position the C(1)OH near the pho

64 he mechanism by which hydrolysis of the beta-PGM phospho-Asp8 is avoided during the time that the act

65 nd the failure to detect differences between PGM allozymes in functional studies.

66 the range of targets that can be detected by PGMs, we report here the use of antibodies in combinatio

67 can expand the range of target detection by PGMs significantly.

68 ts in the sample and the glucose measured by PGMs.

69 le biosynthesis is derived from the cellular PGM.

70 that outperforms synthesized and commercial PGM catalysts for CO oxidation in simulated exhaust stre

71 Earlier studies of the common PGM allozymes in Drosophila melanogaster reported no in

72 Aside from their high cost, PGM catalysts struggle with CO oxidation at low temperat

73 hat the cDNAs encode the two known cytosolic PGM isozymes, PGM1 and PGM2.

74 educed amino acid sequences of the cytosolic PGMs contain the conserved phosphate-transfer catalytic

75 The cytosolic PGMs of maize are distinct from a plastidic PGM of spina

76 e if any PGM activity and gave no detectable PGM activity in B. subtilis.

77 A number of recently discovered PGM-like proteins in a variety of organisms have been pr

78 24 normal and 20 tumor-bearing rats, Gd-DTPA PGM was administered intravenously in doses of 2, 10, 20

79 ed two maize (Zea mays L.) cDNAs that encode PGM with 98.5% identity in their deduced amino acid sequ

80 e mutase/bisphosphoglycerate mutase enzymes (PGM/bPGM; EC 5.4.2.1/5.4.2.4).

81 EPPase PGM shows limited substrate specificity with an ability

82 The putative EPPase PGM active site contains signature residues shared by 2H

83 ing site of known prokaryotic and eukaryotic PGMs.

84 of the contractile phenotype) also expressed PGM-RP.

85 The high-performance atomic Fe PGM-free catalyst holds great promise as a replacement f

86 xplain the absence of latitudinal clines for PGM allozyme alleles, the lack of association of PGM all

87 here is, surprisingly, no candidate gene for PGM.

88 mes, with residues known to be important for PGM/AcP catalytic activity conserved in nature and posit

89 us data, suggest that any potential role for PGM-like proteins in regulated exocytosis is unlikely to

90 Platinum group metal-free (PGM-free) metal-nitrogen-carbon catalysts have emerged a

91 s of the same species was also obtained from PGM.

92 Studies of future PGM flows have focused on trends within material flows o

93 e total Pt content per kW of power (<0.125 g(PGM)/kW) at cell potential 0.65 V: a value of 0.15 g(Pt)

94 ctor V Leiden (FVL) and prothrombin G20210A (PGM), which predispose to venous thromboembolism.

95 tion GM (AGM), and posterior circulation GM (PGM).

96 enzymes and all other PGM-like proteins have PGM activity.

97 Pgm amino acid polymorphisms show that high PGM activity, and apparently higher flux to glycogen syn

98 We have sequenced 1.8 kb of the human PGM-RP promoter and shown that it lacks a conventional T

99 and eukaryotic mutases are not conserved in PGM-RP, a finding consistent with the lack of enzymatic

100 xocytosis, but showed a dramatic decrease in PGM activity.

101 A 2-fold increase in PGM activity enhances glycolytic flux, allows indefinite

102 A reduction in PGM mRNA accumulation was detected in roots deprived of

103 ing number of cytoplasmic proteins including PGM-RP remains to be explored.

104 ely on threonine 466 significantly increased PGM enzymatic activity and could be blocked by transfect

105 s of Bacillus anthracis cofactor-independent PGM (iPGM).

106 tructure of a diphosphoglycerate-independent PGM to be determined.

107 Stable transfection of PGM into PGM-deficient K562 leukemia cells further demonstrated t

108 edlings, distinct from the pathway involving PGM.

109 niquely, T. brucei has been able to lose its PGM gene.

110 ysis suggests that several of these may lack PGM enzymatic activity.

111 Insertion mutants that lacked PGM activity were avirulent in both immunologically norm

112 of the Ion Torrent Personal Genome Machine (PGM) in food traceability analyzing candies as a model o

113 on the Ion Torrent Personal Genome Machine (PGM).

114 ing the Ion Torrent Personal Genome Machine (PGM).

115 Platinum group metal (PGM) catalysts are the current standard for control of p

116 Whether the alternative Pt group metal (PGM) catalysts can exhibit such high performance is an i

117 d challenge to replace platinum group metal (PGM) catalysts with earth-abundant materials for the oxy

118 technical target for total Pt group metals (PGM) loading.

119 Platinum-group metals (PGMs) are technological and economic enablers of many in

120 activities similar to platinum group metals (PGMs), yet TMCs are orders of magnitude more abundant an

121 nstrated the use of personal glucose meters (PGMs) and functional DNAs for the detection of many nong

122 rt a discovery that personal glucose meters (PGMs) can give a dose-dependent response to nicotinamide

123 port application of personal glucose meters (PGMs), which are widely available, low cost, and simple

124 of particles is termed the phonon gas model (PGM), and it has been used almost ubiquitously to try an

125 g expressions based on the phonon gas model (PGM).

126 ology measurements on porcine gastric mucin (PGM) show that pH elevation by H. pylori induces a drama

127 particles (VLPs) against pig gastric mucin (PGM) using 4 VLPs that represent different GII.4 norovir

128 the known atomic structure of rabbit muscle PGM, suggests that both ciliate enzymes and all other PG

129 thin its C-terminal phosphoglycerate mutase (PGM) homology domain and key for the regulation of TCR s

130 hosphatase (EPPase) phosphoglycerate mutase (PGM) homology domain, the first structure of a steroid p

131 stearothermophilus phosphoglycerate mutase (PGM), which interconverts 2- and 3-phosphoglyceric acid

132 e glycolytic enzyme phosphoglycerate mutase (PGM).

133 Phosphoglycerate mutases (PGMs) catalyze the isomerization of 2- and 3-phosphoglyc

134 Lastly, we evaluated several new PGM technologies in the context of antibody sequencing.

135 So far, no PGM catalyst shows activity for CO oxidation at cryogeni

136 A facile synthesis of non-PGM ORR electrocatalysts through thermolysis of one-pot

137 des." Nevertheless, the specific activity of PGM was not significantly affected in roots deprived of

138 stent with the lack of enzymatic activity of PGM-RP in vitro, and the absence of a phosphorylated int

139 allozyme alleles, the lack of association of PGM allozymes with the cosmopolitan In(3L)P inversion, a

140 milar activity and, conversely, depletion of PGM or glucosephosphate isomerase with short interfering

141 Strong direct interaction of PGM with Pak1 but not Pak2, Pak3, or Pak4 was observed.

142 When a strain lacking the major isoform of PGM (pgm2Delta) was grown on media containing galactose

143 epot and (ii) increasing forespore levels of PGM approximately 10-fold in B. subtilis resulted in a l

144 Levels of PGM-RP increased in quiescent PAC1 and A10 cells, and we

145 lacks metavinculin, expressed low levels of PGM-RP.

146 n Glc-1-P and Glc-6-P due to a limitation of PGM enzymatic activity in the pgm2Delta strain.

147 The loss of PGM activity in the insertion mutants also caused growth

148 s approach is able to increase the number of PGM-free active sites.

149 This is the first example in any organism of PGM activity being completely replaced in this way and i

150 Pak1-mediated phosphorylation of PGM selectively on threonine 466 significantly increased

151 hrough its phosphorylation and regulation of PGM activity.

152 ide first insight into the possible roles of PGM/bPGM in plant physiology and in plant-pathogen inter

153 Stable transfection of PGM into PGM-deficient K562 leukemia cells further demon

154 n the automotive sector (the largest user of PGMs) reflecting the rational response of firms to chang

155 an facilitate immortalization via effects on PGM levels and glycolysis.

156 ests that both ciliate enzymes and all other PGM-like proteins have PGM activity.

157 he phosphoglycerate mutase/acid phosphatase (PGM/AcP) family of enzymes, with residues known to be im

158 ents (namely, repeating phosphodisaccharide (PGM), phosphoglycan, phosphosaccharide core-lyso-alkyl-p

159 Phosphoglucomutase (PGM) catalyzes the interconversion of glucose (Glc)-1- a

160 Phosphoglucomutase (PGM) is a key enzyme in glucose metabolism, where it cat

161 Phosphoglucomutase (PGM) is a ubiquitous highly conserved enzyme involved in

162 Glc and is mediated by a phosphoglucomutase (PGM) and a Glc-1-P uridylyltransferase, respectively.

163 mplementation of PMM and phosphoglucomutase (PGM) deficient strains of Pseudomonas aeruginosa, and an

164 samine mutase (PAGM) and phosphoglucomutase (PGM) reversibly catalyse the transfer of phosphate betwe

165 Although the enzyme phosphoglucomutase (PGM) possesses several allozyme polymorphisms, it is uni

166 of the major isoform of phosphoglucomutase (PGM) causes an accumulation of glucose 1-phosphate when

167 The phosphoglucomutase (PGM) and Glc-1-P uridylyltransferase activities necessar

168 is a novel member of the phosphoglucomutase (PGM) family of proteins.

169 PGMs of maize are distinct from a plastidic PGM of spinach (Spinacia oleracea).

170 mination of three ligand-bound states of PMM/PGM harboring a mutation that suppresses activity.

171 Previous structural studies of PMM/PGM have established a key role for conformational chang

172 tional flexibility of different forms of PMM/PGM in solution, including its active, phosphorylated st

173 amic reorientation in the active site of PMM/PGM.

174 e phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa catalyzes an intramolec

175 e phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa catalyzes the reversibl

176 e phosphomannomutase/phosphoglucomutase (PMM/PGM) from the bacterium Pseudomonas aeruginosa is involv

177 Phosphomannomutase/phosphoglucomutase (PMM/PGM) is a ubiquitous four-domain enzyme that catalyzes p

178 Collective responses of Pseudomonas PMM/PGM to phosphosugar substrates and inhibitor were assess

179 Structural characterization of two PMM/PGM-intermediate complexes with glucose 1,6-bisphosphate

180 specific phosphoglucomutase-related protein (PGM-RP) which is expressed predominantly in adult viscer

181 The PGM-related protein (PGM-RP), which contains 506 amino acids (55.6 kDa), is s

182 The reduced PGM activity of JY1060 resulted in enhanced binding of c

183 In contrast, a mutant (JY1060) with reduced PGM activity was avirulent in the former but had only mo

184 Because wild-type p53 down-regulates PGM, mutation of p53 can facilitate immortalization via

185 demonstrated the role of Pak1 in regulating PGM activity.

186 method opens an attractive avenue to replace PGMs in high energy density applications such as fuel ce

187 ed in a distant gene (pgm) encoding a second PGM homologue.

188 The best studied PGM-like protein is parafusin, a major phosphoprotein in

189 platforms (Illumina HiSeq, Life Technologies PGM and Proton, Pacific Biosciences RS and Roche 454).

190 the model support previous conclusions that PGM use is likely to grow, in some cases strongly, by 20

191 The model also indicates that PGM-demand growth will be significantly influenced by th

192 is study, we make the novel observation that PGM is also involved in the regulation of cellular Ca(2+

193 study of nucleotide variation observed that PGM allozymes are a heterogeneous mixture of amino acid

194 We propose that PGM is a stable protein and that existing levels are suf

195 The results suggest that PGM plays a critical role in pneumococcal virulence by a

196 The PGM-related protein (PGM-RP), which contains 506 amino a

197 The PGM-RP promoter may have acquired negative regulatory el

198 Furthermore, mAb against the PGM reversed (approximately 70%) the effect of LPG.

199 ective, the problem with trying to apply the PGM to amorphous materials is the fact that one cannot r

200 PGM for amorphous materials by assuming the PGM is applicable, and then, using a combination of latt

201 s still has many open questions, because the PGM itself becomes questionable when one cannot rigorous

202 ypothesis of disomic inheritance at both the PGM and slow-PGI loci.

203 tally different way than is described by the PGM.

204 When labeled with Gd-DTPA, the PGM-based graft copolymer significantly increases signal

205 information and species per product from the PGM platform than PCR-CS.

206 he results of this approach show that if the PGM was valid, a large number of the mid and high freque

207 These results demonstrate that most of the PGM activity required for type 3 capsule biosynthesis is

208 investigate the phosphatase activity of the PGM domain of Sts-2, Sts-2(PGM).

209 Here, we tested the validity of the PGM for amorphous materials by assuming the PGM is appli

210 The organisation of the PGM-RP gene is essentially identical to that of PGM1.

211 This then strongly suggests that the PGM is inapplicable to amorphous solids.

212 ncies between methodologies suggest that the PGM platform is still pre-mature for its use in food tra

213 We propose that the PGM-RP gene, which we have mapped to human chromosome 9q

214 Sequence comparisons suggest that the PGM-RP promoter evolved from the main phosphoglucomutase

215 es binding to endothelial cells, whereas the PGM domain mediates the cell inhibitory effect.

216 Therefore, PGM is not one of the so-called "anaerobic polypeptides.

217 n of a possible catalytic mechanism for this PGM.

218 no acids (aa) of Pak1, while Pak1 binding to PGM was in the N-terminal 96 aa.

219 ze 10 PGM protein haplotypes with respect to PGM activity, thermostability, and adult glycogen conten

220 (2002), but not the Sydney (2012) strain, to PGM.

221 limited geographic availability, has led to PGMs being labeled as "critical materials".

222 or (Roche), MiSeq (Illumina) and Ion Torrent PGM (Life Technologies) are laser-printer sized and offe

223 Unlike the MiSeq, the Ion Torrent PGM and 454 GS Junior both produced homopolymer-associat

224 Run in 100-bp mode, the Ion Torrent PGM had the highest throughput (80-100 Mb/h).

225 s been designed for the benchtop Ion Torrent PGM platform and can be operated with minimal bioinforma

226 mplicon sequencing method on the Ion Torrent PGM platform for targeted resequencing of a panel of six

227 -Seq data were acquired using an Ion Torrent PGM platform.

228 ibody variable domains using the Ion Torrent PGM platform.

229 cing (Illumina HiSeq 2500/MiSeq, Ion Torrent PGM, Pacific Biosciences RS) are allowing for previously

230 emblies projects sequenced using Ion Torrent PGM.

231 making it possible to detect 40 pM DNA using PGM that can detect glucose only at the mM level.

232 interference (RNAi) suggests that, in vivo, PGM activity is catalysed by both enzymes.

233 ers (P < or =.05) by 31% (AGM) and 32% (WM) (PGM, not significant).