Chemosynthetic, Photosynthetic, and Cyanobacterial Ribulose Bisphosphate Carboxylase

McFadden, Bruce A.; Purohit, K.

doi:10.1007/978-1-4684-8106-8_13

Cited by 22 publications

(18 citation statements)

References 112 publications

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“…Autotrophs effect the reduction and incorporation of CO2 into organic carbon by the exploitation of either light (photoautotrophy) or chemical (chemoautotrophy) energy, from which they obtain ATP and reductant. The pentose phosphate pathway ("Calvin-Benson cycle") of CO2 reduction is common to most autotrophs (McFadden and Purohit, 1978). The key carboxylating enzyme of the Calvin cycle is ribulose bis-phosphate carboxylase (Rubisco) and is distinguished from other carboxylating systems in that the products are two three-carbon (C3) molecules.…”

Section: Culbertson and R S Oremland (Unpublished Data)]mentioning

confidence: 99%

Use of “Specific” Inhibitors in Biogeochemistry and Microbial Ecology

Oremland

Capone

1988

Advances in Microbial Ecology

479

321

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Section: Culbertson and R S Oremland (Unpublished Data)]mentioning

confidence: 99%

Use of “Specific” Inhibitors in Biogeochemistry and Microbial Ecology

Oremland

Capone

1988

Advances in Microbial Ecology

479

321

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“…Inhibition of CO, fixation by 6PGlu occurs with purified, high HCO; (20 mM)-activated 8L8S RuBisCOs from cyanobacteria (Tabita & McFadden, I 9-72 ;Codd & Stewart, 1977 b ;Tabita & Colletti, 1979), Pseudomonas oxalaticus (Lawlis, Gordon & McFadden, 1979), Thiobacillus neapolitanus (Snead & Shively, 1978) and photosynthetic bacteria (McFadden & Purohit, 1978;Gibson & Tabita, I977a, 6). Inhibition of CO, fixation by 6PGlu occurs with purified, high HCO; (20 mM)-activated 8L8S RuBisCOs from cyanobacteria (Tabita & McFadden, I 9-72 ;Codd & Stewart, 1977 b ;Tabita & Colletti, 1979), Pseudomonas oxalaticus (Lawlis, Gordon & McFadden, 1979), Thiobacillus neapolitanus (Snead & Shively, 1978) and photosynthetic bacteria (McFadden & Purohit, 1978;Gibson & Tabita, I977a, 6).…”

Section: (3) Regulatory Aspectsmentioning

confidence: 99%

“…Inhibition of CO, fixation by 6PGlu occurs with purified, high HCO; (20 mM)-activated 8L8S RuBisCOs from cyanobacteria (Tabita & McFadden, I 9-72 ;Codd & Stewart, 1977 b ;Tabita & Colletti, 1979), Pseudomonas oxalaticus (Lawlis, Gordon & McFadden, 1979), Thiobacillus neapolitanus (Snead & Shively, 1978) and photosynthetic bacteria (McFadden & Purohit, 1978;Gibson & Tabita, I977a, 6). T h e only exceptions to these findings to date have been the 2L RuBisCO from Rhodospirillum rubrum (Tabita & McFadden, 1972;McFadden & Purohit, 1978) and the form I1 (6L) enzymes from Rhodopseudomonas sphaeroides (Gibson & Tabita, 1977 a ) and Rhodopseudomonas capsulata (Gibson & Tabita, 19776). When incubated in the inactive form with low HCO; ( I mM), the 8L8S enzymes from the cyanobacteria Agmenellum quadruplicatum, Anabaena CA and Aphanocapsa 6714, and the zL R .…”

Section: (3) Regulatory Aspectsmentioning

confidence: 99%

The Carboxysomes (Polyhedral Bodies) of Autotrophic Prokarygtes

Codd¹,

Marsden²

1984

Biological Reviews

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Summary 1. Polyhedral bodies are present in several groups of autotrophic bacteria that assimilate inorganic carbon via the Calvin cycle, including members of the colourless sulphur‐ oxidizing bacteria, ammonia‐ and nitrite‐oxidizing bacteria and all cyanobacteria (blue‐green algae) examined. Other groups of Calvin‐cycle bacteria lack the inclusions, which have not been found in the purple photosynthetic bacteria, or in the hydrogen bacteria, with one exception in each case. Polyhedral bodies also occur in the chlorophyll b‐containing photosynthetic symbiotic prokaryote, Prochloron, and in several cyanelles. The inclusion bodies have not been found in prokaryotes that cannot fix carbon dioxide via the Calvin cycle, or in eukaryotes. 2. Polyhedral bodies have been isolated from a colourless sulphur bacterium (Thiobacillus neapolitanus), two nitrifying bacteria (Nitrobacter agilis and Nitrosomonas sp.) and two cyanobacteria (Anabaena cylindrica and Chlorogloeopsis fritschii). Ribulose 1,5‐bisphosphate carboxylase/oxygenase (RuBisCO), the carbon dioxide‐fixing enzyme of the Calvin cycle, has been found in the polyhedral bodies in each case, confirming that these inclusions in autotrophic bacteria be re‐termed carboxysomes. 3. Knowledge of carboxysome composition has been constrained by difficulties in carboxysome isolation, although effective methods, including cell disruption in low‐ionic‐strength buffers followed by density‐gradient centrifugation through silicon polymers, or sucrose, followed be preparative agarose electrophoresis, are now available. 4. Analysis of isolated T. neapolitanus, N. agilis and C. fritschii carboxysomes by dissociating sodium dodecyl sulphate‐polyacrylamide gel electrophoresis has revealed the presence of 7–15 polypeptides, the most abundant being the large and small subunits of RuBisCO. Two polypeptides of the T. neapolitanus carboxysomes have been ascribed to the carboxysome membrane (shell), although the identity of other polypeptides is unknown. 5. DNA of unknown function has been reported in carboxysomes isolated from two Nitrobacter species and may be present in the organelles from T. neapolitanus. 6. RuBisCO occurs in both the carboxysomes and in soluble form in the cytoplasm of carboxysome‐containing bacteria. Structural, kinetic, regulatory and immunological comparisons have demonstrated full or near identity between the cytoplasmic and carboxysomal forms of the enzyme. As with RuBisCO from chloroplasts and from almost all non‐carboxysome‐containing bacteria, the cytoplasmic and carboxysomal RuBisCOs each consist of eight large plus eight small subunits. All RuBisCOs are bifunctional enzymes, oxygen acting as a competitive inhibitor of carboxylation, and carbon dioxide acting competitively to inhibit the apparently wasteful oxygenase reaction. Carbon dioxide and oxygen fixation occur at the same site on the large subunit. Despite extensive study, the function of the small subunits is unknown. All RuBisCOs can exist in an inactive and active form, activation proceeding by an ord...

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“…The crucial elements in the control of this key metabolic branch point in Escherichia coli are the Km values of ICL and ICDH for isocitrate and its intracellular concentration, as well as the inactivation of ICDH through phosphorylation of an active-site serine residue, S 113. Furthermore, two tight binding inhibitors of ICL are already known, itaconate (McFadden & Purohit, 1977;Vanni, Giachetti, Pinzauti & McFadden, 1990) and 3-nitropropionate (Schloss & Cleland, 1982). ICL and enzymes from the glyoxylate bypass offer an attractive target for the development of new pharmaceuticals © 1997 International Union of Crystallography Printed in Great Britain -all rights reserved because the bypass is inactive in human hosts but operative in Pseudomonas aeroginosa, a major contributor to pathogenesis in cystic fibrosis (Shimamoto & Berk, 1980), Mycobacterium leprae, the organism responsible for leprosy and species of Leishmania, an insidious human parasite (Simon, Martin & Mukkada, 1978).…”

Section: Introductionmentioning

confidence: 99%

Isocitrate lyase fromAspergillus nidulans: crystallization and X-ray analysis of a glyoxylate cycle enzyme

Langridge¹,

Baker²,

Lucas³

et al. 1997

Acta Cryst D

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Isocitrate lyase (ICL) from the filamentous fungus Aspergillus nidulans catalyzes the first committed step of the carbon-conserving glyoxylate bypass. This enzyme has been crystallized by the hanging-drop method of vapour diffusion using polyethylene glycol 2000 as the precipitant. Diffraction patterns show that the crystals diffract to beyond 2.5 A and are probably in space group P4(2)2(1)2 with unit-cell dimensions of a = b = 91.9 and c = 152.7 A, with one molecule in the asymmetric unit. The elucidation of the structure of this enzyme to high resolution will advance the understanding of how the metabolic branch point between the tricarboxylic acid cycle and the glyoxylate bypass is controlled by the affinity of ICL for its substrate isocitrate and contribute to a programme of rational drug design.

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Chemosynthetic, Photosynthetic, and Cyanobacterial Ribulose Bisphosphate Carboxylase

Cited by 22 publications

References 112 publications

Use of “Specific” Inhibitors in Biogeochemistry and Microbial Ecology

Use of “Specific” Inhibitors in Biogeochemistry and Microbial Ecology

The Carboxysomes (Polyhedral Bodies) of Autotrophic Prokarygtes

Isocitrate lyase fromAspergillus nidulans: crystallization and X-ray analysis of a glyoxylate cycle enzyme

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