ライフサイエンスコーパス: pantothenate

1 nsation of pantoate and beta-alanine to form pantothenate.

2 location, and kinetic constants for ATP and pantothenate.

3 competitively inhibit the phosphorylation of pantothenate.

4 e medium) in the absence of thiamine excrete pantothenate.

5 cofactors including biotin, riboflavin, and pantothenate.

6 ate to D-(-)-pantoate in the biosynthesis of pantothenate.

7 ad a conditional requirement for thiamine or pantothenate.

8 rds from labeled essential nutrients such as pantothenate.

9 of CoA) was replaced with [(13)C(3)(15)N(1)]-pantothenate.

10 between PanK-III and its substrates ATP and pantothenate.

11 evels of leaf Beta-alanine (1.2- to 4-fold), pantothenate (3.2- to 4.1-fold) and total free amino aci

12 ctive with an apparent K(m) of 28 microM for pantothenate-7-amino-4-methylcoumarin (pantothenate-AMC)

13 e hepatocytes (Hepa 1c1c7) in media in which pantothenate (a precursor of CoA) was replaced with [(13

14 uman malaria parasites rely on the uptake of pantothenate across the parasite plasma membrane for sur

15 Modeling these antimetabolites into the pantothenate active site predicts that they bind in the

16 dodiphosphate (AMPPNP).Mg(2+), AMPPNP.Mg(2+).pantothenate, ADP.Mg(2+).phosphopantothenate, and AMP ph

17 ies was optimized to >99% [(13)C(3)(15)N(1)]-pantothenate after three passages of the murine cells in

18 M for pantothenate-7-amino-4-methylcoumarin (pantothenate-AMC), which was converted to pantothenic ac

19 ement of genes required for the synthesis of pantothenate, an essential vitamin deficient in the lous

20 rolling intracellular coenzyme A levels, and pantothenate analogs are growth-inhibiting antimetabolit

21 rasite Plasmodium falciparum have shown that pantothenate analogs interfere with pantothenate phospho

22 The pantothenate analogs N-pentylpantothenamide and N-heptyl

23 l or better than that of currently available pantothenate analogs.

24 utilize the N-alkylpantothenamide family of pantothenate analogues as alternative substrates, thus m

25 a ternary complex structure of PanK-III with pantothenate and ADP.

26 of beta-alanine, followed by the release of pantothenate and AMP.

27 the transplacental transfer of the vitamins pantothenate and biotin and the essential metabolite lip

28 is-Menten constant (Kt) for the transport of pantothenate and biotin in cDNA-transfected cells is 4.9

29 pressed in HeLa cells, induces Na+-dependent pantothenate and biotin transport activities.

30 le, gluconeogenesis, glutathione metabolism, pantothenate and CoA biosynthesis, and butanoate metabol

31 ion of PfPAT and its ability to deliver both pantothenate and fenpropimorph makes it an attractive ta

32 sites of the natural substrate and product, pantothenate and phosphopantothenate, respectively.

33 the adenosine moieties are buried while the pantothenate and pyrophosphate groups of the coenzyme ar

34 Glycosides of pantothenate and riboflavin appear to be minor products

35 ing phagosome is limiting for riboflavin and pantothenate and that Histoplasma virulence requires de

36 Riboflavin, pantothenate, and biotin auxotrophs of Histoplasma were

37 mine HCl, riboflavin, niacinamide, d-calcium pantothenate, and pyridoxine HCl; 50 microg each of d-bi

38 ated forms of pyridoxine, vitamin D, niacin, pantothenate, and riboflavin exist in nature, whereas gl

39 n synthesize thiamine if increased levels of pantothenate are present in the culture medium.

40 A Schu S4 DeltapanG strain is a pantothenate auxotroph and was genetically and chemicall

41 ty and immunogenicity of a double lysine and pantothenate auxotroph of Mycobacterium tuberculosis in

42 SCID mice infected with the pantothenate auxotroph survived significantly longer (25

43 has been known that E. coli yhhK strains are pantothenate auxotrophs, but the role of YhhK in pantoth

44 at Salmonella enterica yhhK strains are also pantothenate auxotrophs.

45 terium glutamicum panD(+) gene corrected the pantothenate auxotrophy of a S. enterica yhhK strain, su

46 which form a "lid" that folds over the open pantothenate binding groove.

47 Pantothenate binding induces a significant conformationa

48 A connection exists between pantothenate biosynthesis and thiamine biosynthesis in S

49 psis encoded homologues of the remaining two pantothenate biosynthesis enzymes from E. coli, l-aspart

50 findings highlight the importance of de novo pantothenate biosynthesis in limiting the intracellular

51 We explored the possibility of manipulating pantothenate biosynthesis in plants.

52 othenate auxotrophs, but the role of YhhK in pantothenate biosynthesis remained an enigma.

53 In addition, depletion of Pan6 (pantothenate biosynthesis) but not Bio2 function (biotin

54 nuating auxotrophic mutations in leucine and pantothenate biosynthesis.

55 , including photorespiration, methionine and pantothenate biosynthesis.

56 vity had previously been associated with the pantothenate biosynthetic gene panE.

57 The pantothenate biosynthetic pathway is well-established in

58 e reductase (EC 1.1.1.169), an enzyme in the pantothenate biosynthetic pathway, catalyzes the NADPH-d

59 is obligatorily dependent on Na+ and accepts pantothenate, biotin, and lipoate as substrates.

60 , induces inward currents in the presence of pantothenate, biotin, and lipoate in a Na+-, concentrati

61 which transports the water-soluble vitamins pantothenate, biotin, and lipoate, from a placental chor

62 The transporter is specific for pantothenate, biotin, and lipoate.

63 acterial pathogen that is able to synthesize pantothenate but is lacking the known ketopantoate reduc

64 a-ketopantoate to form D-(-)-pantoate in the pantothenate/coenzyme A biosynthetic pathway.

65 Pantothenate, commonly referred to as vitamin B(5), is a

66 fPAT mediated survival of yeast cells in low pantothenate concentrations and restored sensitivity of

67 ed FBS, due to lower contaminating unlabeled pantothenate content.

68 ts receiving 13.5 mmol choline plus 1.4 mmol pantothenate/d had a significant decline in urinary carn

69 nt assay using a novel fluorescently labeled pantothenate derivative.

70 ignificantly higher levels of phosphorylated pantothenate-derived metabolites and CoA in vivo and exc

71 intermediates, TCA cycle intermediates, and pantothenate expand dramatically in both mitochondrial d

72 olutely dependent on the acquisition of host pantothenate for its development within human erythrocyt

73 ives of purF mutants that no longer required pantothenate for thiamine-independent growth were isolat

74 The rate of pantothenate formation from the adenylate and beta-alani

75 tase (EC 6.3.2.1) catalyzes the formation of pantothenate from ATP, D-pantoate, and beta-alanine in b

76 rium tuberculosis catalyzes the formation of pantothenate from ATP, D-pantoate, and beta-alanine.

77 ation of D-pantoate and beta-alanine to form pantothenate in bacteria, yeast and plants.

78 sotope exchange of [(14)C]-beta-alanine into pantothenate in the presence of AMP was observed, indica

79 ine metabolism was distinct from the role of pantothenate in thiamine synthesis.

80 Commercially, pantothenate is chemically synthesised and used in vitam

81 ement of panE mutants for either thiamine or pantothenate is manifest only when flux through the puri

82 We show here that the effect of pantothenate is prevented by blocks in the oxidative pen

83 Pantothenate is the precursor of the essential cofactor

84 Pantothenate is the product of the ATP-dependent condens

85 K-III in complex with one of its substrates (pantothenate), its product (phosphopantothenate) as well

86 Pantothenate kinase (CoaA) catalyzes the first and regul

87 Pantothenate kinase (CoaA) is a key regulator of coenzym

88 CoA biosynthesis in bacteria and mammals is pantothenate kinase (CoaA), which governs the intracellu

89 In Bacillus anthracis, the novel type III pantothenate kinase (PanK(Ba); encoded by coaX) catalyze

90 al and animal coenzyme A (CoA) biosynthesis, pantothenate kinase (PANK) activity is critical in regul

91 In contrast, a novel type III pantothenate kinase (PanK) catalyzes the first committed

92 Pantothenate kinase (PanK) catalyzes the first step in t

93 Pantothenate kinase (PanK) catalyzes the first step of t

94 Pantothenate kinase (PanK) is a key regulatory enzyme in

95 Pantothenate kinase (PanK) is a rate-determining enzyme

96 Pantothenate kinase (PanK) is a regulatory enzyme that c

97 Pantothenate kinase (PanK) is the key regulatory enzyme

98 Pantothenate kinase (PanK) is the key regulatory enzyme

99 y enzymatic phosphorylation with E. faecalis pantothenate kinase (PanK).

100 The mouse murine pantothenate kinase (Pank1) gene consists of seven intro

101 The human isoform 2 of pantothenate kinase (PanK2) is localized to the mitochon

102 miR107 is located in intron 5 of the pantothenate kinase 1 (PANK1) gene.

103 Mutations in the pantothenate kinase 2 (PANK2) gene have been identified

104 Pantothenate kinase 2 (PANK2) is an essential regulatory

105 disease have mutations in the gene encoding pantothenate kinase 2 (PANK2); these patients are said t

106 Mutations in the pantothenate kinase 2 gene cause a severe form of neurod

107 Predicted levels of pantothenate kinase 2 protein correlate with the severit

108 The PANK2 gene encodes the human pantothenate kinase 2 protein isoforms, and PANK2 mutati

109 In bacteria, regulation of pantothenate kinase activity is a major factor in contro

110 ramatically in a yeast mutant with defective pantothenate kinase activity.

111 gulator, and antimetabolite binding sites on pantothenate kinase and provide a framework for studies

112 e structural information on Escherichia coli pantothenate kinase by determining the structure of the

113 We used yeast and its pantothenate kinase Cab1 as models to characterize mode

114 Pantothenate kinase catalyzes a key regulatory step in c

115 Pantothenate kinase catalyzes the first step in the bios

116 atment for neurodegeneration associated with pantothenate kinase deficiency.

117 The two enzymes have homologous pantothenate kinase domains, but AtPANK2 also carries a

118 of two new classes of compounds that inhibit pantothenate kinase from M. tuberculosis are described,

119 s, including the finding of mutations in the pantothenate kinase gene and ferritin light chain gene,

120 ow that HSS is caused by a defect in a novel pantothenate kinase gene and propose a mechanism for oxi

121 Although two eukaryotic-type putative pantothenate kinase genes (PanK1 and PanK2) have been id

122 , especially given the existence of multiple pantothenate kinase genes in humans and multiple PanK2 t

123 perature-sensitive mutation of the bacterial pantothenate kinase in E. coli strain ts9.

124 Given the role of pantothenate kinase in production of Coenzyme A and in p

125 trate the key role of feedback regulation of pantothenate kinase in the control of intracellular CoA

126 ns indicate that this type of "bifunctional" pantothenate kinase is conserved in other higher eukaryo

127 Pantothenate kinase is the master regulator of CoA biosy

128 Pantothenate kinase isoform PanK3 is highly related to t

129 report here the characterization of a second pantothenate kinase of Arabidopsis, AtPANK2, as well as

130 The absence of feedback regulation at the pantothenate kinase step allows the accumulation of high

131 s to the highest resolution reported for any pantothenate kinase structure.

132 Pantothenate kinase, a key enzyme in the universal biosy

133 The activity of the second pantothenate kinase, AtPANK2, was confirmed by its abili

134 ate specificities associated with endogenous pantothenate kinase, the first enzyme in the CoA biosynt

135 PANK2 mutations cause pantothenate kinase-associated neurodegeneration (PKAN),

136 Pantothenate kinase-associated neurodegeneration (PKAN,

137 den-Spatz syndrome, the disorder was renamed pantothenate kinase-associated neurodegeneration after d

138 Pantothenate kinase-associated neurodegeneration is a fo

139 PanK2(G521R), the most frequent mutation in pantothenate kinase-associated neurodegeneration, was de

140 In all patients with pantothenate kinase-associated neurodegeneration, whethe

141 isoforms, and PANK2 mutations are linked to pantothenate kinase-associated neurodegeneration.

142 e 2 (PANK2); these patients are said to have pantothenate kinase-associated neurodegeneration.

143 ndings in six cases of molecularly confirmed pantothenate kinase-associated neurodegeneration.

144 e identify prominent ubiquinated deposits in pantothenate kinase-associated neurodegeneration.

145 s the starting metabolite, phosphorylated by pantothenate kinase.

146 ions of the phosphoryl transfer mechanism of pantothenate kinase.

147 N-alkylpantothenamides are substrates for pantothenate kinase.

148 ural substrate PA for phosphorylation by the pantothenate kinase.

149 ackup" regulator of pathway flux relative to pantothenate kinase.

150 ry properties exhibited by the family of the pantothenate kinases allowed the rate of CoA biosynthesi

151 , both active sites of the dimeric mammalian pantothenate kinases coordinately switch between the on

152 contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse.

153 berculosis enzyme but similar to that in the pantothenate kinases of other organisms.

154 quence that is more similar to the mammalian pantothenate kinases than the prototypical bacterial Coa

155 in human brain, distinguishing it from other pantothenate kinases that do not possess mitochondrial-t

156 In contrast to all known pantothenate kinases, SaCoaA activity is not feedback-re

157 ontrast plants expressing KPHMT had elevated pantothenate levels in leaves, flowers siliques and seed

158 No significant change of pantothenate levels in PS transgenic lines was observed.

159 lants are capable of de novo biosynthesis of pantothenate, making this pathway a potential target for

160 both purine and thiamine; however, exogenous pantothenate may be substituted for the thiamine require

161 the effects of supplementary choline and/or pantothenate on the carnitine and lipid status of free-l

162 nstream compounds in the coenzyme A pathway, pantothenate or beta-alanine.

163 hip between the cDNA-specific uptake rate of pantothenate or biotin and Na+ concentration is sigmoida

164 r proteins responsible for the conversion of pantothenate (Pan) to CoASH in Escherichia coli are cons

165 In summary, we characterized the pantothenate pathway in Francisella novicida and F. tula

166 own that pantothenate analogs interfere with pantothenate phosphorylation and block asexual blood sta

167 n normal cells providing clear evidence that pantothenate phosphorylation was a rate-controlling step

168 teracting with the hydrophobic dome over the pantothenate pocket, which is also accessed by the beta-

169 beta expression eliminated the intracellular pantothenate pool and triggered a 13-fold increase in in

170 ns, was necessary and sufficient to increase pantothenate production and allow PurF-independent thiam

171 s took 0.20 mmol and 0.02 mmol/kg choline or pantothenate, respectively.

172 rences in the binding modes for both ATP and pantothenate substrates, and suggests that these differe

173 Choline, but not pantothenate, supplementation significantly decreased ur

174 dent multivitamin transporter for biotin and pantothenate), SVCT (for vitamin C), and CaT1 (for Ca up

175 The lack of a de novo pantothenate synthesis pathway allowed for efficient and

176 Pantothenate synthetase (EC 6.3.2.1) catalyzes the forma

177 Pantothenate synthetase (EC 6.3.2.1), encoded by the pan

178 T), L: -aspartate-alpha-decarboxylase (ADC), pantothenate synthetase (PS) and ketopantoate reductase

179 Pantothenate synthetase (PS) from Mycobacterium tubercul

180 Pantothenate synthetase (PS) is one of the potential new

181 antoate hydroxymethyltransferase (KPHMT) and pantothenate synthetase (PtS) catalyse the first and las

182 Protein kinase B and pantothenate synthetase are examined in detail.

183 e reactions have therefore demonstrated that pantothenate synthetase catalyzes the formation of a pan

184 9, Q72, and K160 residues in M. tuberculosis pantothenate synthetase caused a greater than 1000-fold

185 hree-dimensional structural determination of pantothenate synthetase from Mycobacterium tuberculosis

186 Pantothenate synthetase from Mycobacterium tuberculosis

187 Pantothenate synthetase from Mycobacterium tuberculosis

188 [betagamma-(18)O(6)]-ATP was incubated with pantothenate synthetase in the presence of d-pantoate, a

189 ion of pantoyl adenylate intermediate in the pantothenate synthetase reaction.

190 a kinetically competent intermediate in the pantothenate synthetase reaction.

191 tion studies showed the kinetic mechanism of pantothenate synthetase to be Bi Uni Uni Bi Ping Pong, w

192 ase of pyrophosphate from the active site of pantothenate synthetase.

193 strain MG1655DeltapanC lacking a functional pantothenate synthetase.

194 alidation against Mycobacterium tuberculosis pantothenate synthetase.

195 determining the structure of the enzyme.ADP.pantothenate ternary complex.

196 ) coupled with hydrogen bonding of the C1 of pantothenate to Asp-127 suggests different interpretatio

197 ha-decarboxylase (PanD) enzyme that converts pantothenate to beta-alanine.

198 ribose 5-P may play a role in the ability of pantothenate to substitute for thiamine.

199 vidence for an essential role of a candidate pantothenate transport in malaria transmission to Anophe

200 Recently, a P. falciparum candidate pantothenate transporter (PAT) was characterized by func

201 e molecular identity of the parasite-encoded pantothenate transporter remains unknown.

202 onal characterization of the first protozoan pantothenate transporter, PfPAT, from P. falciparum.

203 nts the growth defect of the yeast fen2Delta pantothenate transporter-deficient mutant and mediates t

204 restored sensitivity of yeast cells lacking pantothenate uptake to fenpropimorph.

205 nce for the importance of the early steps of pantothenate utilization in the regulation of CoA biosyn

206 reduction of ketopantoate to pantoate on the pantothenate (vitamin B(5)) biosynthetic pathway.

207 Pantothenate (vitamin B(5)) is the precursor of the 4'-p

208 s in cell culture to include [(13)C(3)(15)N]-pantothenate (vitamin B(5)), a CoA precursor, instead of

209 1.169), is essential for the biosynthesis of pantothenate (vitamin B(5)).

210 llaboration in branched-chain amino acid and pantothenate (vitamin B5) biosynthesis.

211 Pantothenate (vitamin B5) is the precursor for the biosy

212 In nearly all non-photosynthetic cells, pantothenate (vitamin B5) transport and utilization are

213 Pantothenate was the most abundant pathway component (42

214 tions for the formation of pyrophosphate and pantothenate were determined using rapid quench techniqu

215 thenate was prepared by hydrolysis of methyl pantothenate with Na(18)OH, followed by enzymatic phosph

216 ts that they bind in the same orientation as pantothenate with their alkyl chains interacting with th