Two Distinct Aldolases of Class II Type in the Cyanoplasts and in the Cytosol of the Alga Cyanophora paradoxa

Groß, Wolfgang; Bayer, Manfred G.; Schnarrenberger, Claus; Gebhart, Ulrike B.; Maier, Thomas; Schenk, Hainfried E. A.

doi:10.1104/pp.105.4.1393

Cited by 23 publications

(16 citation statements)

References 19 publications

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“…First, the class I1 aldolase of E. gracilis showed a requirement for monovalent ions, in this case for K+, Na+, Rb-, and NH,+, but not for Li+ or Cs+, as is also the case with the class I1 aldolases of Saccharomyces cerevisiae, Candida utilis, Clostridium perfringens, and of some algae, although with a different specificity for monovalent ions (Bard and Gunsalus, 1950;Richards and Rutter, 1961b;Kowal et al, 1966;Ikawa et al, 1972;Gross et al, 1994). The class I1 aldolasN+containing algae include also the cytosol and plastid enzyme of Cyanophora paradoxa (Glaucocystophyta).…”

Section: Discussionmentioning

confidence: 99%

“…Third, the inhibition of a class I1 enzyme by Cys was not known before for the enzyme of E. gracilis. None of the eukaryotic class I1 aldolases are activated by Cys, including the enzymes of red a n d brown algae a n d the cytosol and plastid enzyme of C. paradoxa (Ikawa et al, 1972;Gross et al, 1994), whereas the enzymes of fungi (Richards and Rutter, 1961b;Kowal et al, 1966) are inhibited. In contrast, Cys is reported as a necessary factor for the activation of the bacterial and cyanobacterial enzymes (Willard and Gibbs, 1968b;Ikawa et al, 1972; Dhar a n d Altekar, 1986Altekar, , 1989.…”

Section: Discussionmentioning

confidence: 99%

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Plastid Class I and Cytosol Class II Aldolase of Euglena gracilis (Purification and Characterization)

1994

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l h e plastidic class I and cytosolic class II aldolases of Euglena gracilis have been purified to apparent homogeneity. In autotrophically grown cells, up to 81% of the total activity is due to class I activity, whereas in heterotrophically grown cells, it is only 7%. l h e class I aldolase has been purified to a specific activity of 20 units/mg protein by anion-exchange chromatography, affinity chromatography, and gel filtration. l h e native enzyme (molecular mass 160 kD) consisted of four identical subunits of 40 kD. The FBP aldolase is one of the essential enzymes in glycolysis, gluconeogenesis, and the Calvin cycle. Two distinct classes of aldolases have been detected in biological systems (Richards and Rutter, 1961a;Rutter, 1964). Class I aldolases are tetrameric proteins with a molecular mass of about 160 kD. They form a Schiff's base with the substrate and are inactivated by borohydride (NaBH4) but not by metal-chelating agents (Rutter, 1964). Class I1 aldolases are dimers with a molecular mass of about 80 kD and form an endiole as reaction intermediate. The catalytic activity of the latter enzyme depends on divalent metal ions and is, therefore, inhibited by EDTA (Richards and Rutter, 1961b;Rutter, 1964). Class I aldolases are present in animals, higher plants, fems, mosses, and some eukaryotic algae. Class I1 aldolases are confined to more primitive organisms such as bacteria, cyanobacteria, and fungi. Only a few bacteria possess, in addition or exclusively, a class I aldolase. Algae and protists show a diverse distribution of class I and class I1 aldolases (Rutter, 1964;Antia, 1967;Lebherz and Rutter, 1969; Buko-* Correspondinz author; fax 49-30-838-4313. wiecki and Anderson, 1974; Altekar, 1986, 1989; for reviews see March and Lebherz, 1992;Schnarrenberger et al., 1992).Class I aldolases have been sequenced from several animals, protists, plants, and algae. The homology among the eukaryotic aldolases is at least 50% . Recently, the sequence of the class I aldolase of the prokaryote Staphylococcus carnosus was also determined. The latter enzyme differs from the eukaryotic aldolases because it is a monomer of somewhat smaller size (33 kD) than the eukaryotic class I aldolases. Its homology with the eukaryotic aldolases is only 30% (Witke and Gotz, 1993). Therefore, the S. carnosus aldolase has to be considered as ancestral in respect to both oligomeric state and sequence conservation.Class I1 aldolase sequences exist for the enzymes of yeast, Escherichia coli, and Co ynebacterium glutamicum (Alefounder et al., 1989;Schwellberger et al., 1989;von der Osten et al., 1989). They do not show any homology with class I aldolases. It was concluded that class I1 aldolases developed independently of class I aldolases in evolution (March and Lebherz, 1992). Further, the sequence homology among the class I1 aldolases is only on the order of 37 to 45%. This may indicate a greater variability among class I1 aldolases than among class I aldolases.Euglena gracilis is one of the few eukaryotic organisms that contains...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Plastid Class I and Cytosol Class II Aldolase of Euglena gracilis (Purification and Characterization)

1994

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“…The coexistence of class I and class II FBAs could be found in lower eukaryotes (Witke & Götz, 1993), such as Euglena gracilis (Plaumann et al, 1997), and bacteria like E. coli and M. tuberculosis (Bai et al, 1982). Two different class II FBAses, as found in B. methanolicus, are present in Cyanophora paradoxa in the cyanelles and cytosol (Gross et al, 1994). A bifunctional role of FBP aldolases as SBP aldolases in the Calvin cycle is well known for class I aldolases of higher plants.…”

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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“…Rather, they are related by a complex and continuous series of gene duplications that accompanied the endosymbiotic origins of organelles. Since many of these duplications occurred early in eukaryotic evolution, it is not surprising that in early branching photosynthetic protists both Calvin cycle enzymes [20,32] and their cytosolic homologues [37] in some cases have an evolutionary origin which is distinct from that found in higher plants.…”

Section: Origin Of Higher-plant Chloroplast and Cytosolic Fbp Isoenzymesmentioning

confidence: 99%

Higher-plant chloroplast and cytosolic fructose-1,6-bisphophosphatase isoenzymes: origins via duplication rather than prokaryote-eukaryote divergence

et al. 1996

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Full-size cDNAs encoding the precursors of chloroplast fructose-1,6-bisphosphatase (FBP), sedoheptulose-1,7-bisphosphatase (SBP), and the small subunit of Rubisco (RbcS) from spinach were cloned. These cDNAs complete the set of homologous probes for all nuclear-encoded enzymes of the Calvin cycle from spinach (Spinacia oleracea L.). FBP enzymes not only of higher plants but also of non-photosynthetic eukaryotes are found to be unexpectedly similar to eubacterial homologues, suggesting a eubacterial origin of these eukaryotic nuclear genes. Chloroplast and cytosolic FBP isoenzymes of higher plants arose through a gene duplication event which occurred early in eukaryotic evolution. Both FBP and SBP of higher plant chloroplasts have acquired substrate specificity, i.e. have undergone functional specialization since their divergence from bifunctional FBP/SBP enzymes of free-living eubacteria.

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Two Distinct Aldolases of Class II Type in the Cyanoplasts and in the Cytosol of the Alga Cyanophora paradoxa

Cited by 23 publications

References 19 publications

Plastid Class I and Cytosol Class II Aldolase of Euglena gracilis (Purification and Characterization)

Plastid Class I and Cytosol Class II Aldolase of Euglena gracilis (Purification and Characterization)

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

Higher-plant chloroplast and cytosolic fructose-1,6-bisphophosphatase isoenzymes: origins via duplication rather than prokaryote-eukaryote divergence

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