Molecular Characterization of a Secreted Enzyme with Phospholipase B Activity from
            <i>Moraxella bovis</i>

Farn, Jacinta L.; Strugnell, Richard A.; Hoyne, Peter A.; Michalski, Wojtek P.; Tennent, Jan M.

doi:10.1128/jb.183.22.6717-6720.2001

Cited by 54 publications

(42 citation statements)

References 29 publications

(18 reference statements)

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“…Repeat 2 is fully equipped with the catalytic triad, but not the other repeats [10]. The secreted PLB enzyme from M. Bovis also has the GDSL motif as well [1]. Thus the catalytic triad can comprise the catalytic nucleophile serine (present in the motif GxSxG or GDSL), aspartate and histidine.…”

Section: Discussionmentioning

confidence: 99%

“…Essentially these enzymes display phospholipase A/lysophospholipase activity, catalysing the total deacylation of phospholipids. Phosphatidylcholine (PC)-hydrolysing PLB activities have been described in bacteria [1], fungi [2], Dictyostelium discoideum [3] and in mammalian cells [4][5][6][7][8][9][10][11], and three distinct gene families have been identified from bacteria, fungi and mammals. In the microorganism Moraxella bovis, the plb gene encodes a protein of 616 amino acids and the enzyme hydrolyses PC/LPC (lysoPC) to produce NEFAs (non-esterified fatty acids, also known as free fatty acids) and glycerophosphorylcholine (GPC) [1].…”

Section: Introductionmentioning

confidence: 99%

“…Phosphatidylcholine (PC)-hydrolysing PLB activities have been described in bacteria [1], fungi [2], Dictyostelium discoideum [3] and in mammalian cells [4][5][6][7][8][9][10][11], and three distinct gene families have been identified from bacteria, fungi and mammals. In the microorganism Moraxella bovis, the plb gene encodes a protein of 616 amino acids and the enzyme hydrolyses PC/LPC (lysoPC) to produce NEFAs (non-esterified fatty acids, also known as free fatty acids) and glycerophosphorylcholine (GPC) [1]. PLB enzymes have been cloned from different fungi, including Candida albicans [12], Saccharomyces cerevisae [13][14][15], Cryptococcus neoformans [16], Penicillium notatum and Torulaspora delbruekii, and are related by sequence [2], but not to M. bovis PLB.…”

Section: Introductionmentioning

confidence: 99%

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Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast

Morgan

Insall

Haynes

et al. 2004

Biochemical Journal

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The social amoeba Dictyostelium discoideum exhibits high activities of phospholipase and lysophospholipase [Ferber, Munder, Fischer and Gerisch (1970) Eur. J. Biochem. 14, 253-257]. We assayed Dictyostelium lysates to demonstrate the presence of a highly active phospholipase B (PLB) enzyme that removed both fatty-acid chains from phosphatidylcholine and produced the water-soluble glycerophosphorylcholine. We purified the PLB activity from Dictyostelium cytosol using standard agarose media (size exclusion and ion exchange), and combined this with an affinity purification step using myristoylated ARF1 (ADP-ribosylation factor 1), a protein which has a single fatty acid at its N-terminus. Two proteins co-purified (48 kDa and 65 kDa), and the 48 kDa protein was digested with trypsin, peptide fragments were separated by reverse-phase chromatography, and the resultant peptides were sequenced by Edman degradation. From the peptide sequences obtained, database searches revealed a gene which encodes a protein of 65 kDa with unknown function. The 48 kDa protein therefore appears to be a fragment of the fulllength 65 kDa product. Expression of the gene in Escherichia coli confirmed that it encodes a PLB. Characterization of its substrate specificity indicated that, in addition to phosphatidylcholine deacylation, the enzyme also hydrolysed phosphatidylinositol and phosphatidylethanolamine. The PLB identified in the present study is not related to existing PLBs found in bacteria, fungi or mammals. There are, however, genes similar to Dictyostelium PLB in mammals, flies, worms and Giardia, but not in yeast. We therefore have identified a novel family of intracellular PLBs.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast

Morgan

Insall

Haynes

et al. 2004

Biochemical Journal

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“…are recognized as major virulence determinants in a number of bacterial species, including human, animal and several invertebrate pathogens (Songer, 1997;Farn et al, 2001;Yang et al, 2012). The ymt gene encoding for a phospholipase D in Yersinia pestis, for example, is needed for persistence in the flea midgut (Hinnebusch et al, 2002).…”

Section: Strain Selectionmentioning

confidence: 99%

Insect pathogenicity in plant-beneficial pseudomonads: phylogenetic distribution and comparative genomics

et al. 2016

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Bacteria of the genus Pseudomonas occupy diverse environments. The Pseudomonas fluorescens group is particularly well-known for its plant-beneficial properties including pathogen suppression. Recent observations that some strains of this group also cause lethal infections in insect larvae, however, point to a more versatile ecology of these bacteria. We show that 26 P. fluorescens group strains, isolated from three continents and covering three phylogenetically distinct sub-clades, exhibited different activities toward lepidopteran larvae, ranging from lethal to avirulent. All strains of sub-clade 1, which includes Pseudomonas chlororaphis and Pseudomonas protegens, were highly insecticidal regardless of their origin (animals, plants). Comparative genomics revealed that strains in this sub-clade possess specific traits allowing a switch between plant-and insect-associated lifestyles. We identified 90 genes unique to all highly insecticidal strains (sub-clade 1) and 117 genes common to all strains of sub-clade 1 and present in some moderately insecticidal strains of sub-clade 3. Mutational analysis of selected genes revealed the importance of chitinase C and phospholipase C in insect pathogenicity. The study provides insight into the genetic basis and phylogenetic distribution of traits defining insecticidal activity in plant-beneficial pseudomonads. Strains with potent dual activity against plant pathogens and herbivorous insects have great potential for use in integrated pest management for crops.

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“…BLASTP analysis revealed the highest sequence similarity of extracellular phospholipases to phospholipase B (PLB) or lysophospholipase; approximately 20 amino acid residues as the putative signal peptide cleavage site were detected at their N-termini of the extracellular phospholipase (PLB group). It has been postulated that PLB might be secreted across the plasma membrane (Farn et al, 2001;Shen et al, 2004). Obviously, the cytoplasmic phospholipases shared homology with phospholipase A (PLA) involved in the removal of the sn-1 acyl group from phospholipids to produce 2-acyllysophospholipids (lysophosphatidic acids) (Watanabe et al, 1999;Richmond & Smith, 2011), which act as precursors in phosphatidic acid biosynthesis.…”

Section: Gtk Motifmentioning

confidence: 99%

Genome mining of fungal lipid-degrading enzymes for industrial applications

et al. 2015

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Lipases are interesting enzymes, which contribute important roles in maintaining lipid homeostasis and cellular metabolisms. Using available genome data, seven lipase families of oleaginous and non-oleaginous yeast and fungi were categorized based on the similarity of their amino acid sequences and conserved structural domains. Of them, triacylglycerol lipase (patatin-domaincontaining protein) and steryl ester hydrolase (abhydro_lipase-domain-containing protein) families were ubiquitous enzymes found in all species studied. The two essential lipases rendered signature characteristics of integral membrane proteins that might be targeted to lipid monolayer particles. At least one of the extracellular lipase families existed in each species of yeast and fungi. We found that the diversity of lipase families and the number of genes in individual families of oleaginous strains were greater than those identified in non-oleaginous species, which might play a role in nutrient acquisition from surrounding hydrophobic substrates and attribute to their obese phenotype. The gene/enzyme catalogue and relevant informative data of the lipases provided by this study are not only valuable toolboxes for investigation of the biological role of these lipases, but also convey potential in various industrial applications.

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Molecular Characterization of a Secreted Enzyme with Phospholipase B Activity from Moraxella bovis

Cited by 54 publications

References 29 publications

Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast

Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast

Insect pathogenicity in plant-beneficial pseudomonads: phylogenetic distribution and comparative genomics

Genome mining of fungal lipid-degrading enzymes for industrial applications

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