Purification and characterization of bifunctional dehydroquinase-shikimate: NADP oxidoreductase from pea seedlings

Mousdale, David M.; Campbell, Murray S.; Coggins, John R.

doi:10.1016/s0031-9422(00)83568-2

Cited by 41 publications

(27 citation statements)

References 46 publications

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“…In the final FPLC Mono Q ion exchange step of the purification three activity peaks were seen (in a ratio of about 8: 1: 1) [31]. Only the major peak was taken for peptide sequencing.…”

Section: Dgmilanttsigmqpkvdetmentioning

confidence: 99%

The characterisation of the shikimate pathway enzyme dehydroquinase fromPisum sativum

et al. 1994

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Peptides accounting for 157 residues of the bifunctional shikimate pathway enzyme, dehydroquinase/shikimate dehydrogenase, of Pisum sativum were sequenced. Three of the peptides were homologous to regions in Escherichia coli dehydroquinase and two to E. coli shikimate dehydrogenase. The pea dehydroquinase activity was inhibited by treatment with dehydroquinate plus sodium borohydride, establishing it as a type I dehydroquinase.Synthetic oligonucleotides designed from the amino acid sequence were used as PCR primers to amplify fragments of F! sativum cDNA. DNA sequence analysis showed that these amplified products were derived from dehydroquinase/shikimate dehydrogenase cDNA. The complete amino acid sequence of the dehydroquinase domain has been defined; it is homologous to all other type I dehydroquinases and is N-terminal.

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“…In the final FPLC Mono Q ion exchange step of the purification three activity peaks were seen (in a ratio of about 8: 1: 1) [31]. Only the major peak was taken for peptide sequencing.…”

Section: Dgmilanttsigmqpkvdetmentioning

confidence: 99%

The characterisation of the shikimate pathway enzyme dehydroquinase fromPisum sativum

et al. 1994

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“…Monofunctional 3-dehydroquinases have been identified in bacteria (Berlyn & Giles, 1969); the Escherichia coli enzyme has been purified to homogeneity and the complete sequence is known Duncan et al, 1986). The plant enzyme occurs on a bifunctional polypeptide chain in association with shikimate dehydrogenase (Polley, 1978;Koshiba, 1978;Mousdale et al, 1987), which catalyses the fourth step on the shikimate pathway. In the third class, exemplified by the fungi, 3-dehydroquinase is one of the five activities carried on the arom multifunctional enzyme, the others being the activities of steps, 2, 4, 5 and 6 of the same pathway (Lumsden & Coggins, 1977Gaertner & Cole, 1977;Smith & Coggins, 1983;Lambert et al, 1985;Coggins et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases

Chaudhuri

Duncan

Graham

et al. 1991

Biochemical Journal

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The lysine residues involved in Schiff-base formation at the active sites of both the 3-dehydroquinase component of the pentafunctional arom enzyme of Neurospora crassa and of the monofunctional 3-dehydroquinase of Escherichia coli were labelled by treatment with 3-dehydroquinate in the presence of NaB3H4. Radioactive peptides were isolated by h.p.l.c. following digestion with CNBr (and in one case after further digestion with trypsin). The sequence established for the N. crassa peptide was ALQHGDVVKLVVGAR, and that for the E. coli peptide was QSFDADIPKIA. An amended nucleotide sequence for the E. coli gene (aroD) that encode 3-dehydroquinase is also presented, along with a revised alignment of the deduced amino acid sequences for the biosynthetic enzymes.

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“…In most prokaryotes examined to date, the seven shikimate pathway enzymes are encoded as separate polypeptides. The plant enzymes are also encoded in separate polypeptides, with the exception of AroD and AroE, which are fused and encode a bifunctional polypeptide (31). Plant shikimate pathway enzymes are nucleus encoded, but many possess N-terminal plastid targeting peptides.…”

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confidence: 99%

Evolutionary Origins of the Eukaryotic Shikimate Pathway: Gene Fusions, Horizontal Gene Transfer, and Endosymbiotic Replacements

et al. 2006

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Currently the shikimate pathway is reported as a metabolic feature of prokaryotes, ascomycete fungi, apicomplexans, and plants. The plant shikimate pathway enzymes have similarities to prokaryote homologues and are largely active in chloroplasts, suggesting ancestry from the plastid progenitor genome. Toxoplasma gondii, which also possesses an alga-derived plastid organelle, encodes a shikimate pathway with similarities to ascomycete genes, including a five-enzyme pentafunctional arom. These data suggests that the shikimate pathway and the pentafunctional arom either had an ancient origin in the eukaryotes or was conveyed by eukaryote-to-eukaryote horizontal gene transfer (HGT). We expand sampling and analyses of the shikimate pathway genes to include the oomycetes, ciliates, diatoms, basidiomycetes, zygomycetes, and the green and red algae. Sequencing of cDNA from Tetrahymena thermophila confirmed the presence of a pentafused arom, as in fungi and T. gondii. Phylogenies and taxon distribution suggest that the arom gene fusion event may be an ancient eukaryotic innovation. Conversely, the Plantae lineage (represented here by both Viridaeplantae and the red algae) acquired different prokaryotic genes for all seven steps of the shikimate pathway. Two of the phylogenies suggest a derivation of the Plantae genes from the cyanobacterial plastid progenitor genome, but if the full Plantae pathway was originally of cyanobacterial origin, then the five other shikimate pathway genes were obtained from a minimum of two other eubacterial genomes. Thus, the phylogenies demonstrate both separate HGTs and shared derived HGTs within the Plantae clade either by primary HGT transfer or secondarily via the plastid progenitor genome. The shared derived characters support the holophyly of the Plantae lineage and a single ancestral primary plastid endosymbiosis. Our analyses also pinpoints a minimum of 50 gene/domain loss events, demonstrating that loss and replacement events have been an important process in eukaryote genome evolution.

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Purification and characterization of bifunctional dehydroquinase-shikimate: NADP oxidoreductase from pea seedlings

Cited by 41 publications

References 46 publications

The characterisation of the shikimate pathway enzyme dehydroquinase fromPisum sativum

The characterisation of the shikimate pathway enzyme dehydroquinase fromPisum sativum

Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases

Evolutionary Origins of the Eukaryotic Shikimate Pathway: Gene Fusions, Horizontal Gene Transfer, and Endosymbiotic Replacements

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