ライフサイエンスコーパス: ribulose

1 P-ribose, which was further converted to ADP-ribulose.

2 rs and sugar derivatives tested, including l-ribulose.

3 at there was specific accumulation of form I ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisC

4 rains revealed that either form I or form II ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisC

5 ymes, including the key Calvin Cycle enzyme, Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco

6 Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco

7 Ribulose 1,5 bisphosphate carboxylase/oxygenase (RubisCO

8 postulate, the turnover of 1-(3)H-labeled D-ribulose 1,5-bisphosphate (RuBP) by impaired position-16

9 uncovered the presence of genes that encode ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (

10 Previous studies suggested that ribulose 1,5-bisphosphate (RuBP) is a positive effector

11 abitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg2+ and CO2.

12 atalyzes the addition of CO(2) onto enolized ribulose 1,5-bisphosphate (RuBP), producing 3-phosphogly

13 acterial Rubisco is not readily inhibited by ribulose 1,5-bisphosphate and fallover is not observed,

14 not only carboxylation and oxygenation of d-ribulose 1,5-bisphosphate but also other promiscuous, pr

15 The oxygenation of ribulose 1,5-bisphosphate by Rubisco is the first step i

16 laveria bidentis, a dicotyledonous C4 plant, ribulose 1,5-bisphosphate carboxylase (rubisco) accumula

17 ivity of the CO2-fixing Calvin cycle enzyme, ribulose 1,5-bisphosphate carboxylase (RubisCO), prevent

18 g of the presequence of the small subunit of ribulose 1,5-bisphosphate carboxylase fused to the cytoc

19 These were the rbcL gene for ribulose 1,5-bisphosphate carboxylase, the developmental

20 In Rhodobacter capsulatus, ribulose 1,5-bisphosphate carboxylase-oxygenase (RubisCO

21 In a Rhodobacter sphaeroides ribulose 1,5-bisphosphate carboxylase-oxygenase deletion

22 assembles around many copies of the enzymes ribulose 1,5-bisphosphate carboxylase/ oxygenase and car

23 in the well-characterized CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxidase (Rubisco).

24 ation of Lys-14 in the large subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

25 Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO

26 Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO

27 e multiple copies of the CO(2)-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

28 Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

29 The chloroplast enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

30 n dioxide fixation relies on the function of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

31 increased productivity by overexpression of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

32 Some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO

33 a proteinaceous outer shell and filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO

34 D-Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO

35 thotrophic bacteria, the CO(2)-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

36 sisting of a proteinaceous shell filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO

37 Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

38 biological selection of randomly mutagenized ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

39 Previously, a ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

40 e effects of temperature on gas exchange and ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

41 oxide gas, catalyzed primarily by the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

42 that is required for the light activation of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

43 Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

44 In a ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

45 ate, the substrate for the CO2 fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

46 th the genes (rbcL and rbcS) encoding form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

47 d cbbZ were found downstream from the form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

48 The photosynthetic CO(2) fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

49 The photosynthetic CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco

50 Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

51 cy of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

52 that form a shell to encapsulate the enzymes ribulose 1,5-bisphosphate carboxylase/oxygenase and carb

53 -balancing systems was further manifested in ribulose 1,5-bisphosphate carboxylase/oxygenase and phos

54 solate contains both the denitrification and ribulose 1,5-bisphosphate carboxylase/oxygenase gene clu

55 nces of the P. vulgaris rbcS2 gene, encoding ribulose 1,5-bisphosphate carboxylase/oxygenase small su

56 (oilseed rape), Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) acts wi

57 Rubisco (d-ribulose 1,5-bisphosphate carboxylase/oxygenase) is resp

58 ve sites of the CO(2)-fixing enzyme Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) to rele

59 idative decarboxylase, class II aldolase, or ribulose 1,5-bisphosphate carboxylase/oxygenase, large s

60 oding the large and small subunits of form I ribulose 1,5-bisphosphate carboxylase/oxygenase, or Rubi

61 s a potent, naturally occurring inhibitor of ribulose 1,5-bisphosphate carboxylase/oxygenase.

62 d-Ribulose 1,5-bisphosphate carboxylase/oxygenases (RuBisC

63 resistance of atmospheric CO(2) to sites of ribulose 1,5-bisphosphate carboxylation inside bundle sh

64 This effector is most likely ribulose 1,5-bisphosphate or a metabolite derived from t

65 ers the allocation of photosynthates between ribulose 1,5-bisphosphate regeneration and starch synthe

66 y abstraction of the proton from C3 of the d-ribulose 1,5-bisphosphate substrate by a carbamate oxyge

67 conversion of ribulose 5-phosphate (Ru5P) to ribulose 1,5-bisphosphate, the substrate for the CO2 fix

68 nitiated by abstraction of the 3-proton of d-ribulose 1,5-bisphosphate.

69 CO(2), to permit its efficient fixation onto ribulose 1,5-bisphosphate.

70 hibited a reduced affinity for the substrate ribulose 1,5-bisphosphate.

71 xidative damage of the CO2 acceptor molecule ribulose 1,5-bisphosphate.

72 le sugar phosphates, including its substrate ribulose 1,5-bisphosphate.

73 y in Bacillus sp. and (2) the 5-methylthio-d-ribulose 1-phosphate (MTRu 1-P) 1,3-isomerase reaction i

74 sfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxyl

75 enna proteins (LHCA1, LHCB1, and LHCB4), the ribulose 1.5-bisphosphate carboxylase subunits (rbcL and

76 e abundant cytosolic bicarbonate and provide ribulose 1.5-bisphosphate carboxylase/oxygenase (RubisCO

77 tid rbcL gene, encoding the large subunit of ribulose-1, 5-bisphosphate carboxylase, in higher plants

78 in the chloroplast-encoded large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (EC 4.1

79 (L290F) substitution in the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisc

80 Various studies indicate that ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisc

81 bcL gene that codes for the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase, the ke

82 3-phosphoglyceric acid content and increased ribulose-1, 5-bisphosphate content, which is indicative

83 The recovery of nearly 100 genes encoding ribulose-1,5 bisphosphate carboxylase-oxygenase subunit

84 ructures of the plant SET domain enzyme, pea ribulose-1,5 bisphosphate carboxylase/oxygenase large su

85 Ribulose-1,5-biphosphate carboxylase/oxygenase (Rubisco)

86 Ribulose-1,5-biphosphate-carboxylase-oxygenase (RuBisCO)

87 and its rate-limiting carbon fixing enzyme, ribulose-1,5-bis-phosphate carboxylase/oxygenase (Rubisc

88 the reduction in photosynthesis is linked to ribulose-1,5-bis-phosphate carboxylase/oxygenase (Rubisc

89 direct consequence of the pdtpi mutation, as ribulose-1,5-bis-phosphate carboxylase/oxygenase express

90 wo well-studied precursors, small subunit of ribulose-1,5-bis-phosphate carboxylase/oxygenase, and fe

91 ed by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phospha

92 bisco isoform that functions to scavenge the ribulose-1,5-bisphosphate (RuBP) by-product of purine/py

93 is) contains the cbbLS genes encoding form I ribulose-1,5-bisphosphate (RuBP) carboxylase oxygenase (

94 Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (

95 pable of using CO2 as sole source of carbon, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (

96 to reach BS to generate enough ATP to allow ribulose-1,5-bisphosphate (RuBP) regeneration in BS.

97 sco by removing inhibitory molecules such as ribulose-1,5-bisphosphate (RuBP).

98 phic growth due to the accumulation of toxic ribulose-1,5-bisphosphate (RuBP).

99 tion of CAB1, CAB2, and the small subunit of ribulose-1,5-bisphosphate carboxylase (RBCS) promoters i

100 m the genes that encode the small subunit of ribulose-1,5-bisphosphate carboxylase (rbcS), the gene f

101 to glycine reassignment and an archaeal-type ribulose-1,5-bisphosphate carboxylase (RubisCO) involved

102 e enzyme responsible for C3 carbon fixation, ribulose-1,5-bisphosphate carboxylase (Rubisco), however

103 n case of evolutionary adaptation is that of ribulose-1,5-bisphosphate carboxylase (RubisCO), the enz

104 levels relevant to the (1)(3)C flux studies, ribulose-1,5-bisphosphate carboxylase activity is predic

105 Ribulose-1,5-bisphosphate carboxylase activity was confi

106 /b-binding protein (cab) or small subunit of ribulose-1,5-bisphosphate carboxylase oxygenase (rbcS).

107 lleviates the problem of reduced affinity of ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO

108 Carboxysomes are BMCs containing ribulose-1,5-bisphosphate carboxylase oxygenase and carb

109 ding those involved in photosynthesis (e.g., ribulose-1,5-bisphosphate carboxylase oxygenase genes rb

110 tid rbcL gene (encoding the large subunit of ribulose-1,5-bisphosphate carboxylase) is regulated post

111 tation with archaeal-like hybrid type II/III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO

112 illales from the lower mesopelagic contained ribulose-1,5-bisphosphate carboxylase-oxygenase and sulf

113 ts to metabolize toxic glycolate formed when ribulose-1,5-bisphosphate carboxylase-oxygenase oxygenat

114 the key Calvin-Benson-Bassham cycle enzyme, ribulose-1,5-bisphosphate carboxylase.

115 Ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1

116 glyceraldehyde-3-phosphate dehydrogenase or ribulose-1,5-bisphosphate carboxylase/oxygenase (compari

117 it (S) increases the catalytic efficiency of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.

118 e (CA), pyruvate, phosphate dikinase (PPDK), ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO

119 s), which sequester the CO(2)-fixing enzymes ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

120 ich algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

121 in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

122 sensitive green fluorescent protein (GFP) to ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO

123 ADP sensitivity for both ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

124 Archaeoglobus fulgidus RbcL2, a form III ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

125 ription activator gene, cbbR, and the form I ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO

126 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

127 in of activase is involved in recognition of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

128 nd 6 in the alpha/beta-barrel active site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

129 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

130 Victorin-induced proteolysis of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

131 biological selection of randomly mutagenized ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

132 ensional structure and active-site residues, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

133 The light activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

134 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

135 ing a product with substantial similarity to ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO

136 In the active form of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

137 in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

138 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

139 The activation state of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

140 Form I ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO

141 The photorespiratory cycle begins with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

142 f nonstructural carbohydrates and changes in ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

143 loroplast gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

144 s been shown previously to express a form II ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO

145 3A, encoding a small subunit protein (S) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

146 es not markedly facilitate the activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

147 ynthesis and growth to maturity of antisense ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

148 mining the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

149 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

150 ytic inefficiencies of the CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

151 y focused on enhancing the CO2 fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

152 ts and concentrates the carbon-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO

153 capsulated the two key carboxysomal enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO

154 Carboxysomes compartmentalize the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO

155 raising the CO2 concentration at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

156 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

157 hat enhance carbon fixation by concentrating ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO

158 important enzymes, and immunolocalization of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

159 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

160 In photosynthetic organisms, D-ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

161 The enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

162 Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO

163 ivated transition-state analog-bound form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

164 ining the CO(2) concentration at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

165 ria and some chemoautotrophs by sequestering ribulose-1,5-bisphosphate carboxylase/oxygenase and carb

166 al domains of the TP of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and its

167 for interaction with CcmM and, by extension, ribulose-1,5-bisphosphate carboxylase/oxygenase and the

168 ost efficient answer to the dual activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and the

169 s into the conservation of Mg(2+) within the ribulose-1,5-bisphosphate carboxylase/oxygenase family o

170 The dual affinity of ribulose-1,5-bisphosphate carboxylase/oxygenase for O(2)

171 The lowest ribulose-1,5-bisphosphate carboxylase/oxygenase per leaf

172 containing the rbcL gene for cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase produced

173 Finally, XCT is important for ribulose-1,5-bisphosphate carboxylase/oxygenase producti

174 io calculations of an active-site mimic of D-ribulose-1,5-bisphosphate carboxylase/oxygenase suggest

175 precursors of Toc75 and the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase to intac

176 Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalys

177 ction center protein D1), and "Form I" rbcL (ribulose-1,5-bisphosphate carboxylase/oxygenase) genes f

178 in which the shell and the internal RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) lattice

179 ubunits of the carbon-fixing enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), a majo

180 entuates the feedback and down-regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase, resulti

181 rbcS-1A, which encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase, was not

182 -light conditions, major contribution of the ribulose-1,5-bisphosphate carboxylase/oxygenase-bypass t

183 tion of CO(2) and O(2) at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase.

184 Levels of 3-phosphoglyceric acid and ribulose-1,5-bisphosphate decreased and increased, respe

185 Carboxylation of the common substrate ribulose-1,5-bisphosphate leads to photosynthetic carbon

186 o 3 times more xylulose-1,5-bisphosphate per ribulose-1,5-bisphosphate utilized than wild-type or F92

187 An were used to model maximal rates of RuBP (ribulose-1,5-bisphosphate) carboxylation (Vcmax ) and el

188 external Ci and their modulation of internal ribulose-1,5-bisphosphate, phosphoglycerate, and Ci pool

189 s involved in the conversion of glycolate to ribulose-1,5-bisphosphate.

190 nylalanine 342 had an increased affinity for ribulose-1,5-bisphosphate.

191 xygenase oxygenates rather than carboxylates ribulose-1,5-bisphosphate.

192 e abstraction of a proton from the substrate ribulose-1,5-bisphosphate.

193 bisco (Vc,max 117 mumol CO2 m(-2) s(-1)) and ribulose-1:5-bisphosphate limited carboxylation rate (Jm

194 the precursor form of the small subunit for ribulose-2,5-bisphosphate carboxylase/oxygenase (prSSU)

195 lly undergoes C1-C2 bond cleavage to yield d-ribulose 3 and formate.

196 versible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate

197 I), which catalyzes the interconversion of d-ribulose 5-phosphate (Ru5P) and d-arabinose 5-phosphate

198 eps in the riboflavin pathway and converts d-ribulose 5-phosphate (Ru5P) to l-3,4-dihydroxy-2-butanon

199 e (PRK) is responsible for the conversion of ribulose 5-phosphate (Ru5P) to ribulose 1,5-bisphosphate

200 orted functional and structural studies of d-ribulose 5-phosphate 3-epimerase (RPE) from Streptococcu

201 The superfamily includes d-ribulose 5-phosphate 3-epimerase (RPE), orotidine 5'-mon

202 thm, genes (ribose 5-phosphate isomerase and ribulose 5-phosphate 3-epimerase) in the pentose phospha

203 nate 6-phosphate decarboxylase (SgbH), and L-ribulose 5-phosphate 4-epimerase (SgbE).

204 lulose 5-phosphate 3-epimerase (UlaE), and L-ribulose 5-phosphate 4-epimerase (UlaF).

205 ryotes, that mediates the interconversion of ribulose 5-phosphate and arabinose 5-phosphate.

206 The CD spectra of L-ribulose 5-phosphate and D-xylulose 5-phosphate differ s

207 quilibration of the pentulose 5-phosphates d-ribulose 5-phosphate and d-xylulose 5-phosphate in the p

208 crystal structure suggests the location of a ribulose 5-phosphate binding site and suggests a role fo

209 at connects the active site of YaaE with the ribulose 5-phosphate binding site was identified.

210 observations implicate new components of the ribulose 5-phosphate binding site.

211 miting tautomerization of the 1,2-enediol of ribulose 5-phosphate consistent with the proposed role o

212 ssibility of a catalytic role of Asp186 of D-ribulose 5-phosphate epimerase by site-directed mutagene

213 ldol condensation between formaldehyde and d-ribulose 5-phosphate in formaldehyde-fixing methylotroph

214 structures were used to model the substrate ribulose 5-phosphate in the active site with the phospha

215 Y. pestis yrbH, catalyses the conversion of ribulose 5-phosphate into arabinose 5-phosphate (A5P), t

216 The pH profile of V/K for L-ribulose 5-phosphate is bell-shaped with pK values of 5.

217 A ribulose 5-phosphate is bound to YaaD via an imine with

218 lative to the wild-type enzyme, the Km for D-ribulose 5-phosphate is essentially unaltered with D186N

219 r each, the promiscuity is altered so that d-ribulose 5-phosphate is the preferred substrate.

220 decarboxylation of 6PG to the 1,2-enediol of ribulose 5-phosphate proceeds via a stepwise mechanism w

221 4-epimerase catalyzes the epimerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate by an ald

222 entanediol, were used to model the substrate ribulose 5-phosphate, and to propose catalytic roles for

223 subunits: YaaD catalyzes the condensation of ribulose 5-phosphate, glyceraldehyde-3-phosphate, and am

224 5.3.1.6) interconvert ribose 5-phosphate and ribulose 5-phosphate.

225 generated by promiscuous phosphatases from d-ribulose 5-phosphate.

226 me demonstrated Michaelis constant values of ribulose-5-phosphate (226 microM) and ATP (208 microM),

227 ut also inhibition of LKB1-AMPK signaling by ribulose-5-phosphate (Ru-5-P), the product of the third

228 d that GPT1 preferentially exchanges G6P for ribulose-5-phosphate (Ru5P).

229 Assays determined that ribulose-5-phosphate 3-epimerase (Rpe) was specifically

230 terologous expression of the gene encoding D-ribulose-5-phosphate 3-epimerase from any source, thereb

231 is of (13)C and deuterium isotope effects, L-ribulose-5-phosphate 4-epimerase catalyzes the epimeriza

232 H97N, H95N, and Y229F mutants of L-ribulose-5-phosphate 4-epimerase had 10, 1, and 0.1%, re

233 ses (APIs) catalyze the interconversion of d-ribulose-5-phosphate and D-arabinose-5-phosphate, the fi

234 e in part to reduced levels of 6PGD products ribulose-5-phosphate and NADPH, which led to reduced RNA

235 In the nonoxidative part of the OPPP, ribulose-5-phosphate is converted to ribose-5-phosphate

236 rophosphate or ethanol and destabilized by D-ribulose-5-phosphate or 2-mercaptoethanol.

237 Either a failure to convert ribulose-5-phosphate to R5P or a block in purine nucleot

238 enzyme that converts 6-phosphogluconate into ribulose-5-phosphate with NADP(+) as cofactor in the pen

239 rement for the production via these steps of ribulose-5-phosphate.

240 under this condition, FGGY silencing led to ribulose accumulation.

241 omers for arabinose, lyxose, ribose, xylose, ribulose, and xylulose, is reported.

242 revisiae deletion mutant of YDR109C revealed ribulose as one of the metabolites with the most signifi

243 onsumes ATP to produce the Rubisco substrate ribulose bisphosphate (RuBP).

244 metabolic substrates, bicarbonate, CO(2) and ribulose bisphosphate and the product 3-phosphoglycerate

245 s in other phototrophic organisms, including ribulose bisphosphate carboxylase (Calvin cycle), citrat

246 nding protein (CAB) and the small subunit of ribulose bisphosphate carboxylase (RBCS) was also impair

247 ssing are genes for the Calvin cycle enzymes ribulose bisphosphate carboxylase (RuBisCO) and phosphor

248 In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolde

249 Ribulose bisphosphate carboxylase (Rubisco) is localized

250 which induced the aggregation of homodimeric ribulose bisphosphate carboxylase (Rubisco), did not aff

251 isoform that delivers CO2 intracellularly to ribulose bisphosphate carboxylase (RuBPCase).

252 The control proteins ribulose bisphosphate carboxylase and cytochrome f were

253 tif (another LRE) and the native Arabidopsis ribulose bisphosphate carboxylase small subunit gene RBC

254 rease in chlorophyll a/b-binding protein and ribulose bisphosphate carboxylase small subunit gene tra

255 The ratios of PEPC and PPDK to ribulose bisphosphate carboxylase were substantially low

256 amily of genes encoding the small subunit of ribulose bisphosphate carboxylase) that are sufficient f

257 gene encoding the large subunit of Rubisco (ribulose bisphosphate carboxylase).

258 carbon, carbon dioxide may be fixed via the ribulose bisphosphate carboxylase, Wood-Ljungdahl pathwa

259 lycine produced in the oxygenase reaction of ribulose bisphosphate carboxylase-oxygenase is incorpora

260 ration-dependent data on the yield of native ribulose bisphosphate carboxylase/oxygenase (Rubisco) as

261 Plants rely on ribulose bisphosphate carboxylase/oxygenase (Rubisco) fo

262 llowing salinity stress with transcripts for ribulose bisphosphate carboxylase/oxygenase (RuBisCO) su

263 lus neapolitanus fixes CO2 by using a form I ribulose bisphosphate carboxylase/oxygenase (RuBisCO), t

264 o CO(2), raising the CO(2) concentration for Ribulose bisphosphate carboxylase/oxygenase (Rubisco).

265 in the chloroplast and the specificities of ribulose bisphosphate carboxylase/oxygenase (Rubisco).

266 oncentration around the carboxylating enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO).

267 the transit peptide of the small subunit of ribulose bisphosphate carboxylase/oxygenase did not affe

268 tration (Cb) using a simple kinetic model of ribulose bisphosphate carboxylase/oxygenase function.

269 Ribulose bisphosphate carboxylase/oxygenase is commonly

270 erized by three unique enzymatic activities: ribulose bisphosphate carboxylase/oxygenase, phosphoribu

271 hotosynthetic carbon dioxide fixation enzyme ribulose bisphosphate carboxylase/oxygenase.

272 s were compared in the model, and increasing ribulose bisphosphate regeneration rate will allow for f

273 in Udotea extracts was equivalent to that of ribulose-bisphosphate carboxylase [Rubisco; 3-phospho-D-

274 used to the transit peptide of ferredoxin or ribulose-bisphosphate carboxylase activase for stromal t

275 nated by the cbbL genes (67%-82%) coding the ribulose-bisphosphate carboxylase large chain in the Cal

276 the large subunit of the CO(2)-fixing enzyme ribulose-bisphosphate carboxylase.

277 Ribulose-bisphosphate carboxylase/oxygenase (Rubisco) ac

278 se of tight-binding inhibitors from dead-end ribulose-bisphosphate carboxylase/oxygenase (Rubisco) co

279 chaperonin-dependent, folding model protein ribulose-bisphosphate carboxylase/oxygenase (RuBisCO), a

280 The key enzyme of the CBB cycle, ribulose-bisphosphate carboxylase/oxygenase (RubisCO), i

281 osynthetic carbon metabolism is initiated by ribulose-bisphosphate carboxylase/oxygenase (Rubisco), w

282 3)(-) to CO(2) for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase (RuBisCO).

283 egulated synthesis of both photopigments and ribulose-bisphosphate carboxylase/oxygenase (Rubisco).

284 assist GroEL-mediated refolding of bacterial ribulose-bisphosphate carboxylase/oxygenase but gained t

285 In human HEK293 cells, ribulose could only be detected when ribitol was added t

286 ers for a locus from the chloroplast genome, ribulose diphosphate carboxylase.

287 etone phosphate, glyceraldehyde 3-phosphate, ribulose, erythrose, and sucrose as potential precursors

288 enzymes, serving to re-phosphorylate free d-ribulose generated by promiscuous phosphatases from d-ri

289 at the sulfate site and the placement of the ribulose group guided by the glycerol site.

290 esponsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro.

291 alyzes the isomerization of L-arabinose to L-ribulose in vivo.

292 dolase enzymes, the de novo preparation of L-ribulose, L-lyxose, D-ribose, D-tagatose, 1-amino-1-deox

293 Although the ribulose monophosphate (RuMP) cycle used by methylotroph

294 thway and the assimilatory and dissimilatory ribulose monophosphate cycles, and by a formate dehydrog

295 ter, a multidrug-efflux pump, and either the ribulose monophosphate operon or ascorbate metabolism op

296 mbining the nonoxidative glycolysis with the ribulose monophosphate pathway to convert methanol to hi

297 hat assimilate formaldehyde by the serine or ribulose monophosphate pathway.

298 r substrate preference of both kinases for d-ribulose over a range of other sugars and sugar derivati

299 with the hypothesis that the members of the "ribulose phosphate binding" (beta/alpha)(8)-barrel "supe

300 The "ribulose phosphate binding" superfamily defined by the S