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1 poor ability to recover from incubation with ribulose 1,5-bisphosphate.
2 xidative damage of the CO2 acceptor molecule ribulose 1,5-bisphosphate.
3 nitiated by abstraction of the 3-proton of d-ribulose 1,5-bisphosphate.
4 CO(2), to permit its efficient fixation onto ribulose 1,5-bisphosphate.
5 hibited a reduced affinity for the substrate ribulose 1,5-bisphosphate.
6 e abstraction of a proton from the substrate ribulose-1,5-bisphosphate.
7 s involved in the conversion of glycolate to ribulose-1,5-bisphosphate.
8 nylalanine 342 had an increased affinity for ribulose-1,5-bisphosphate.
9 acterial Rubisco is not readily inhibited by ribulose 1,5-bisphosphate and fallover is not observed,
10 not only carboxylation and oxygenation of d-ribulose 1,5-bisphosphate but also other promiscuous, pr
11 rains revealed that either form I or form II ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisC
12 at there was specific accumulation of form I ribulose 1, 5-bisphosphate carboxylase/oxygenase (RubisC
13 ymes, including the key Calvin Cycle enzyme, Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco
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
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).
25 e effects of temperature on gas exchange and ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
27 oxide gas, catalyzed primarily by the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
28 that is required for the light activation of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
31 ate, the substrate for the CO2 fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
32 th the genes (rbcL and rbcS) encoding form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
33 d cbbZ were found downstream from the form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
34 in WH7803 chromosomal DNA digests, using the ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
35 s denitrificans, encoding form I and form II ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
36 ep in the carboxylation pathway catalyzed by ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
37 cy of C3 plants suffers from the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
38 ation of Lys-14 in the large subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
40 e multiple copies of the CO(2)-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
43 increased productivity by overexpression of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
45 a proteinaceous outer shell and filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO
47 thotrophic bacteria, the CO(2)-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO
48 sisting of a proteinaceous shell filled with ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO
50 biological selection of randomly mutagenized ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco
51 that form a shell to encapsulate the enzymes ribulose 1,5-bisphosphate carboxylase/oxygenase and carb
52 -balancing systems was further manifested in ribulose 1,5-bisphosphate carboxylase/oxygenase and phos
53 solate contains both the denitrification and ribulose 1,5-bisphosphate carboxylase/oxygenase gene clu
54 nces of the P. vulgaris rbcS2 gene, encoding ribulose 1,5-bisphosphate carboxylase/oxygenase small su
56 idative decarboxylase, class II aldolase, or ribulose 1,5-bisphosphate carboxylase/oxygenase, large s
57 oding the large and small subunits of form I ribulose 1,5-bisphosphate carboxylase/oxygenase, or Rubi
60 e abundant cytosolic bicarbonate and provide ribulose 1.5-bisphosphate carboxylase/oxygenase (RubisCO
61 nce of the precursor to the small subunit of ribulose-1, 5-bisphosphate carboxylase (pS) in a precurs
62 tid rbcL gene, encoding the large subunit of ribulose-1, 5-bisphosphate carboxylase, in higher plants
63 in the chloroplast-encoded large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (EC 4.1
64 (L290F) substitution in the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisc
66 bcL gene that codes for the large subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase, the ke
67 The recovery of nearly 100 genes encoding ribulose-1,5 bisphosphate carboxylase-oxygenase subunit
68 ructures of the plant SET domain enzyme, pea ribulose-1,5 bisphosphate carboxylase/oxygenase large su
69 tion of CAB1, CAB2, and the small subunit of ribulose-1,5-bisphosphate carboxylase (RBCS) promoters i
70 m the genes that encode the small subunit of ribulose-1,5-bisphosphate carboxylase (rbcS), the gene f
71 to glycine reassignment and an archaeal-type ribulose-1,5-bisphosphate carboxylase (RubisCO) involved
72 e enzyme responsible for C3 carbon fixation, ribulose-1,5-bisphosphate carboxylase (Rubisco), however
73 n case of evolutionary adaptation is that of ribulose-1,5-bisphosphate carboxylase (RubisCO), the enz
74 levels relevant to the (1)(3)C flux studies, ribulose-1,5-bisphosphate carboxylase activity is predic
76 /b-binding protein (cab) or small subunit of ribulose-1,5-bisphosphate carboxylase oxygenase (rbcS).
77 lleviates the problem of reduced affinity of ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO
78 ding those involved in photosynthesis (e.g., ribulose-1,5-bisphosphate carboxylase oxygenase genes rb
79 tid rbcL gene (encoding the large subunit of ribulose-1,5-bisphosphate carboxylase) is regulated post
80 tation with archaeal-like hybrid type II/III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO
81 illales from the lower mesopelagic contained ribulose-1,5-bisphosphate carboxylase-oxygenase and sulf
84 glyceraldehyde-3-phosphate dehydrogenase or ribulose-1,5-bisphosphate carboxylase/oxygenase (compari
85 it (S) increases the catalytic efficiency of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.
88 ing a product with substantial similarity to ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
90 in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
93 capsulated the two key carboxysomal enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
96 f nonstructural carbohydrates and changes in ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
97 loroplast gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
98 s been shown previously to express a form II ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
99 3A, encoding a small subunit protein (S) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
100 Carboxysomes compartmentalize the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
101 es not markedly facilitate the activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
102 ynthesis and growth to maturity of antisense ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
103 mining the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
104 on of the Arabidopsis thaliana gene encoding ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
106 raising the CO2 concentration at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
107 bacco Rubisco activase in ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
109 hat enhance carbon fixation by concentrating ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
114 ivated transition-state analog-bound form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
115 ytic inefficiencies of the CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
116 ich algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
117 y focused on enhancing the CO2 fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
118 in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
119 sensitive green fluorescent protein (GFP) to ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
120 ts and concentrates the carbon-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO
121 ADP sensitivity for both ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
122 Archaeoglobus fulgidus RbcL2, a form III ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
123 ription activator gene, cbbR, and the form I ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO
125 in of activase is involved in recognition of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
126 nd 6 in the alpha/beta-barrel active site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
129 biological selection of randomly mutagenized ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
130 ensional structure and active-site residues, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco
131 ria and some chemoautotrophs by sequestering ribulose-1,5-bisphosphate carboxylase/oxygenase and carb
132 al domains of the TP of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and its
133 ost efficient answer to the dual activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and the
134 for interaction with CcmM and, by extension, ribulose-1,5-bisphosphate carboxylase/oxygenase and the
135 s into the conservation of Mg(2+) within the ribulose-1,5-bisphosphate carboxylase/oxygenase family o
138 containing the rbcL gene for cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase produced
140 io calculations of an active-site mimic of D-ribulose-1,5-bisphosphate carboxylase/oxygenase suggest
141 precursors of Toc75 and the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase to intac
143 ction center protein D1), and "Form I" rbcL (ribulose-1,5-bisphosphate carboxylase/oxygenase) genes f
144 in which the shell and the internal RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) lattice
145 entuates the feedback and down-regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase, resulti
146 rbcS-1A, which encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase, was not
147 -light conditions, major contribution of the ribulose-1,5-bisphosphate carboxylase/oxygenase-bypass t
149 resistance of atmospheric CO(2) to sites of ribulose 1,5-bisphosphate carboxylation inside bundle sh
150 An were used to model maximal rates of RuBP (ribulose-1,5-bisphosphate) carboxylation (Vcmax ) and el
151 3-phosphoglyceric acid content and increased ribulose-1, 5-bisphosphate content, which is indicative
154 bisco (Vc,max 117 mumol CO2 m(-2) s(-1)) and ribulose-1:5-bisphosphate limited carboxylation rate (Jm
156 external Ci and their modulation of internal ribulose-1,5-bisphosphate, phosphoglycerate, and Ci pool
157 ers the allocation of photosynthates between ribulose 1,5-bisphosphate regeneration and starch synthe
158 postulate, the turnover of 1-(3)H-labeled D-ribulose 1,5-bisphosphate (RuBP) by impaired position-16
159 uncovered the presence of genes that encode ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (
162 ed by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phospha
163 bisco isoform that functions to scavenge the ribulose-1,5-bisphosphate (RuBP) by-product of purine/py
164 is) contains the cbbLS genes encoding form I ribulose-1,5-bisphosphate (RuBP) carboxylase oxygenase (
165 pable of using CO2 as sole source of carbon, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (
167 to reach BS to generate enough ATP to allow ribulose-1,5-bisphosphate (RuBP) regeneration in BS.
169 y abstraction of the proton from C3 of the d-ribulose 1,5-bisphosphate substrate by a carbamate oxyge
170 conversion of ribulose 5-phosphate (Ru5P) to ribulose 1,5-bisphosphate, the substrate for the CO2 fix
171 o 3 times more xylulose-1,5-bisphosphate per ribulose-1,5-bisphosphate utilized than wild-type or F92
172 d the lack of fallover and the inhibition by ribulose 1,5-bisphosphate were similar to those of form
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