FRUCTOSE-BISPHOSPHATE ALDOLASES AN EVOLUTIONARY HISTORY PDF

Abstract Background Horizontal or lateral transfer of genetic material between distantly related prokaryotes has been shown to play a major role in the evolution of bacterial and archaeal genomes, but exchange of genes between prokaryotes and eukaryotes is not as well understood. In particular, gene flow from eukaryotes to prokaryotes is rarely documented with strong support, which is unusual since prokaryotic genomes appear to readily accept foreign genes. Two non-homologous forms of fructose bisphosphate aldolase FBA are characteristic of eukaryotes and prokaryotes respectively. However, a eukaryotic gene has been inserted immediately upstream of the ancestral prokaryotic gene in several strains ecotypes of Synechococcus and Prochlorococcus.

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This article has been cited by other articles in PMC. Abstract The gene encoding the Escherichia coli Class I fructose-1, 6-bisphosphate aldolase FBP aldolase has been cloned and the protein overproduced in high amounts.

This gene sequence has previously been identified as encoding an E. However, the purified protein overproduced from the dhnA gene shares all its properties with those known for the E.

The protein is an mer with a native molecular mass of approx. The active-site peptide has been isolated and the Schiff-base-forming lysine residue Lys has been identified by a combination of site-directed mutagenesis, kinetics and electrospray-ionization MS.

A second lysine residue Lys has been implicated in substrate binding. The cloning of this gene and the high levels of overexpression obtained will facilitate future structure-function studies. Selected References These references are in PubMed. This may not be the complete list of references from this article. Perham RN. The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.

Biochem Soc Trans. Fed Proc. Molecular architecture of rabbit skeletal muscle aldolase at 2. The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2. FEBS Lett.

Activity and specificity of human aldolases. J Mol Biol. Biochem J. A class I Schiff base fructose diphosphate aldolase of prokaryotic origin. Purification and properties of Micrococcus aerogenes aldolase. J Biol Chem. Structural comparisons between the class I fructose diphosphate aldolases from Micrococcus aerogenes and rabbit. Variations in the quaternary structure of three lactic acid bacteria aldolases.

Evidence for the existence of a class I and class II aldolase in Lactobacillus casei. Fructose diphosphate aldolase from Mycobacterium smegmatis.

Functional similarities with rabbit muscle aldolase. Arch Biochem Biophys. Purification and properties. Eur J Biochem. Cloning, sequencing, and characterization of the gene encoding the class I fructose-1,6-bisphosphate aldolase of Staphylococcus carnosus.

J Bacteriol. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. An unusual class I Schiff base fructose-1,6-bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis. Aldolase of lactic acid bacteria: a case history in the use of an enzyme as an evolutionary marker. Bacteriol Rev. Fructose-bisphosphate aldolases: an evolutionary history.

Trends Biochem Sci. Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.

A reactive, surface cysteine residue of the class-II fructose-1,6-bisphosphate aldolase of Escherichia coli revealed by electrospray ionisation mass spectrometry. Identification of arginine as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. Protein Sci. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat Struct Biol. The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold.

Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. Statistical analysis of enzyme kinetic data. Methods Enzymol. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Isolation of deoxyribonucleic acid and ribosomal ribonucleic acid from bacteria.

Polymerase chain reaction PCR techniques for site-directed mutagenesis. Biotechnol Adv. Comparison of the mechanisms of two distinct aldolases from Escherichia coli grown on gluconeogenic substrates. Biochim Biophys Acta. A cDNA-based comparison of dehydration-induced proteins dehydrins in barley and corn. Plant Mol Biol. A dehydrin cognate protein from pea Pisum sativum L. An osmotic stress protein of cyanobacteria is immunologically related to plant dehydrins.

Plant Physiol. Comput Appl Biosci. Site-directed mutagenesis identifies aspartate 33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A. The predicted secondary structures of class I fructose-bisphosphate aldolases.

Amino acid sequence around the active site of two class I fructose-1,6-bisphosphate aldolases from staphylococci. ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling.

Deoxyribose aldolase from Lactobacillus plantarum. Polycarboxylic acid activation of rat liver deoxyribose phosphate aldolase. A lysine to arginine substitution at position of rabbit aldolase A changes the rate-determining step to Schiff base formation.

Protein Eng. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res.

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Aldolase A

Citations A model for carbohydrate metabolism in the diatom Phaeodactylum tricornutum deduced from comparative whole genome analysis. PLoS One 3:e A moderate decrease of plastid aldolase activity inhibits photosynthesis, alters the levels of sugars and starch, and inhibits growth of potato plants.

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Fructose-bisphosphate aldolases: an evolutionary history

This article has been cited by other articles in PMC. Abstract The gene encoding the Escherichia coli Class I fructose-1, 6-bisphosphate aldolase FBP aldolase has been cloned and the protein overproduced in high amounts. This gene sequence has previously been identified as encoding an E. However, the purified protein overproduced from the dhnA gene shares all its properties with those known for the E. The protein is an mer with a native molecular mass of approx. The active-site peptide has been isolated and the Schiff-base-forming lysine residue Lys has been identified by a combination of site-directed mutagenesis, kinetics and electrospray-ionization MS.

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Horizontal transfer of a eukaryotic plastid-targeted protein gene to cyanobacteria

This article has been cited by other articles in PMC. Abstract Fructose 1,6-bisphosphate aldolase catalyzes the reversible cleavage of fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. The existing apo-enzyme structure was refined using the crystallographic free-R-factor and maximum likelihood methods that have been shown to give improved structural results that are less subject to model bias. Crystals were also soaked with the natural substrate fructose 1,6-bisphosphate , and the crystal structure of this complex has been determined to 2. The apo structure differs from the previous Brookhaven-deposited structure 1ald in the flexible C-terminal region.

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