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

4 at there was specific accumulation of form I 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 acterial Rubisco is not readily inhibited by ribulose 1,5-bisphosphate and fallover is not observed,

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

39 in WH7803 chromosomal DNA digests, using the ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

40 s denitrificans, encoding form I and form II ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO

41 ep in the carboxylation pathway catalyzed by ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

62 d the lack of fallover and the inhibition by ribulose 1,5-bisphosphate were similar to those of form

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

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

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

66 poor ability to recover from incubation with ribulose 1,5-bisphosphate.

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

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

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

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

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

72 nce of the precursor to the small subunit of ribulose-1, 5-bisphosphate carboxylase (pS) in a precurs

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

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

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

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

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

78 3-phosphoglyceric acid content and increased ribulose-1, 5-bisphosphate content, which is indicative

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

136 3A, encoding a small subunit protein (S) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

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

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

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

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

141 on of the Arabidopsis thaliana gene encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

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

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

144 bacco Rubisco activase in ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

173 EP75 and the precursor to a small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase.

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

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

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

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

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

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

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

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

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

183 he Euglena precursor to the small subunit of ribulose-15-bisphosphate carboxylase/oxygenase (pSSU) is

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

211 4-epimerase catalyzes the epimerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate by an ald

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

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

214 5.3.1.6) interconvert ribose 5-phosphate and ribulose 5-phosphate.

215 ic kinetics relative to the concentration of ribulose 5-phosphate.

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

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

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

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

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

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

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

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

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

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

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

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

228 nonallergenic food proteins, such as spinach ribulose bis-phosphate carboxylase/oxygenase, were diges

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

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

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

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

233 Ribulose bisphosphate carboxylase (Rubisco) is localized

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

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

236 The control proteins ribulose bisphosphate carboxylase and cytochrome f were

237 ly trapped folding-incompetent conformers of ribulose bisphosphate carboxylase are converted to the n

238 nins GroEL and GroES catalyze the folding of ribulose bisphosphate carboxylase at a rate proportional

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

254 Ribulose bisphosphate carboxylase/oxygenase is commonly

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

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

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

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

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

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

261 Ribulose-bisphosphate carboxylase/oxygenase (Rubisco) ac

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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