Chloroplast class I and class II aldolases are bifunctional for fructose‐1,6‐biphosphate and sedoheptulose‐1,7‐biphosphate cleavage in the Calvin cycle

Flechner, Anke; Groß, Wolfgang; Martin, William; Schnarrenberger, Claus

doi:10.1016/s0014-5793(99)00285-9

Cited by 70 publications

(47 citation statements)

References 17 publications

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“…The CI-FBA from Synechocystis sp. Flechner et al (1999). PCC 6803 showed about eight times lower affinity for SBP than spinach chloroplast CI-FBA.…”

Section: Discussionmentioning

confidence: 89%

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Nakahara

Yamamoto

Miyake

et al. 2003

Plant and Cell Physiology

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;The whole genome sequence database for Synechocystis sp. PCC 6803 has revealed the presence of genes encoding class-I (CI) and class-II (CII) fructose-1,6-bisphosphate aldolases (FBAs) in this organism. Two types of FBA from Synechocystis sp. PCC 6803 were separated by chromatography on phenyl-Sepharose. The activity of the enzyme in the major peak was inhibited by the presence of 25 mM EDTA; however, the activity in the minor peak was not. Therefore, the FBA in the former fractions was designated as CII-FBA, and in the latter designated as CI-FBA. CI-FBA was functionally redundant in Synechocystis sp. PCC 6803, while no disruptant for the gene encoding CII-FBA was obtained under photoautotrophic conditions. The kinetic parameters of CI-and CII-FBAs purified from Synechocystis sp. PCC 6803 in the cleavage reaction of FBP were generally similar, except in their reactivity for SBP. The SBP/FBP activity ratio of the CII-FBA was two times higher than that of the CI-FBA.

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“…The CI-FBA from Synechocystis sp. Flechner et al (1999). PCC 6803 showed about eight times lower affinity for SBP than spinach chloroplast CI-FBA.…”

Section: Discussionmentioning

confidence: 89%

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Nakahara

Yamamoto

Miyake

et al. 2003

Plant and Cell Physiology

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“…Because there is no evidence for the presence of a functional Calvin cycle in any of the Trypanosomatidae, this SBPase can find its function only in a modified hexosemonophosphate pathway, where it hydrolyzes SBPase, synthesized from erythrose 4-phosphate and dihydroxyacetone phosphate through the action of a bifunctional aldolase. Such bifunctional aldolases, capable of forming both FBPase and SBPase by using either glyceraldehyde 3-phosphate or erythrose 4-phosphate as substrate in the condensation reaction with dihydroxyacetone phosphate, have been described only for chloroplasts (19). We then analyzed whether the trypanosomatid aldolases could have been acquired by horizontal gene transfer from a chloroplast as well (Fig.…”

Section: Resultsmentioning

confidence: 99%

Plant-like traits associated with metabolism of Trypanosoma parasites

Hannaert

Saavedra

Duffieux

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

197

137

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Trypanosomatid parasites cause serious diseases among humans, livestock, and plants. They belong to the order of the Kinetoplastida and form, together with the Euglenida, the phylum Euglenozoa. Euglenoid algae possess plastids capable of photosynthesis, but plastids are unknown in trypanosomatids. Here we present molecular evidence that trypanosomatids possessed a plastid at some point in their evolutionary history. Extant trypanosomatid parasites, such as Trypanosoma and Leishmania, contain several ''plant-like'' genes encoding homologs of proteins found in either chloroplasts or the cytosol of plants and algae. The data suggest that kinetoplastids and euglenoids acquired plastids by endosymbiosis before their divergence and that the former lineage subsequently lost the organelle but retained numerous genes. Several of the proteins encoded by these genes are now, in the parasites, found inside highly specialized peroxisomes, called glycosomes, absent from all other eukaryotes, including euglenoids.

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“…However, only a few class II aldolases have so far been shown to be active as SBP aldolases, e.g. in the alga C. paradoxa (Flechner et al, 1999), the cyanobacterium Synechocystis sp. PCC6803 (Nakahara et al, 2003) and in the methylotrophic bacterium M. capsulatus Bath (Rozova et al, 2010).…”

Section: Bioinformatic Analysis and Phylogeny Of The Fbas From B Metmentioning

confidence: 99%

The methylotrophic Bacillus methanolicus MGA3 possesses two distinct fructose 1,6-bisphosphate aldolases

2013

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The thermotolerant Gram-positive methylotroph Bacillus methanolicus is able to grow with methanol, glucose or mannitol as a sole carbon and energy source. Fructose 1,6-bisphosphate aldolase (FBA), a key enzyme of glycolysis and gluconeogenesis, is encoded in the genome of B. methanolicus by two putative fba genes, the chromosomally located fba C and fba P on the naturally occurring plasmid pBM19. Their amino acid sequences share 75 % identity and suggest a classification as class II aldolases. Both enzymes were purified from recombinant Escherichia coli and were found to be active as homotetramers. Both enzymes were activated by either manganese or cobalt ions, and inhibited by ADP, ATP and EDTA. The kinetic parameters allowed us to distinguish the chromosomally encoded FBA C from the plasmid encoded FBA P , since FBA C showed higher affinity towards fructose 1,6-bisphosphate (K m of 0.16±0.01 mM as compared to 2±0.08 mM) as well as higher glycolytic catalytic efficiency (31.3 as compared to 0.8 s "1 mM "1 ) than FBA P

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Chloroplast class I and class II aldolases are bifunctional for fructose‐1,6‐biphosphate and sedoheptulose‐1,7‐biphosphate cleavage in the Calvin cycle

Cited by 70 publications

References 17 publications

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Purification and Characterization of Class-I and Class-II Fructose-1,6-bisphosphate Aldolases from the Cyanobacterium Synechocystis sp. PCC 6803

Plant-like traits associated with metabolism of Trypanosoma parasites

The methylotrophic Bacillus methanolicus MGA3 possesses two distinct fructose 1,6-bisphosphate aldolases

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