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Literature summary extracted from

  • Tong, S.; Lin, Y.; Lu, S.; Wang, M.; Bogdanov, M.; Zheng, L.
    Structural insight into substrate selection and catalysis of lipid phosphate phosphatase PgpB in the cell membrane (2016), J. Biol. Chem., 291, 18342-18352 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.27 pgpB gene is cloned into the pET22b vector (Novagen) to generate the C-terminal His6-tagged protein. Mutants were generated using standard site-directed mutagenesis. The PgpB wild type and mutant proteins are expressed in Escherichia coli strain C41(DE3) Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.27 vapor diffusion method, the structure is determined at 3.2 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.27 D211A mutant enzyme retains 50% activity Escherichia coli
3.1.3.27 H163A mutation increases hydrolysis of 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] by 50% Escherichia coli
3.1.3.27 K93A the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gains 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme Escherichia coli
3.1.3.27 K93A/K97A the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gained 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme Escherichia coli
3.1.3.27 K93T mutant enzyme with significantly improved activity for lysophosphatidic acid, (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, and phosphatidic acid by 2.5- or 3.4-fold but not for 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] Escherichia coli
3.1.3.27 K93T/K97A the mutant enzyme loses all activity for lysophosphatidic acid or (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, but retains 50% activity for phosphatidic acid or 1,2-dipalmitoryl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] Escherichia coli
3.1.3.27 K97A the mutant enzyme shows complete activity loss for lysophosphatidic acid and (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate, whereas it retains full activity for phosphatidic acid and gained 40% more activity toward phosphatidylglycerol phosphate compared with wild type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.27 orthovanadate
-
 Escherichia coli
3.1.3.27 phosphatidylethanolamine 3 mM, 70% inhibition. competitive Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.27 0.108
-
 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate pH 7.5, 23°C Escherichia coli
3.1.3.27 5.052
-
 1-hexanoyl-sn-glycero-3-phosphate pH 7.5, 23°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.27 membrane integral membrane protein Escherichia coli 16020
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.27 Escherichia coli P0A924
-
-
3.1.3.27 Escherichia coli K12 P0A924
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.27
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.27 (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate + H2O
-
 Escherichia coli ?
-
 ?
3.1.3.27 (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol-1-phosphate + H2O
-
 Escherichia coli K12 ?
-
 ?
3.1.3.27 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O
-
 Escherichia coli 1,2-dihexadecanoyl-sn-glycerol + phosphate
-
 ?
3.1.3.27 1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O
-
 Escherichia coli K12 1,2-dihexadecanoyl-sn-glycerol + phosphate
-
 ?
3.1.3.27 1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] + H2O
-
 Escherichia coli ? + phosphate
-
 ?
3.1.3.27 1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1'-(3'-phospho)glycerol)] + H2O
-
 Escherichia coli K12 ? + phosphate
-
 ?
3.1.3.27 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O
-
 Escherichia coli 1-(9Z-octadecenoyl)-sn-glycerol + phosphate
-
 ?
3.1.3.27 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O
-
 Escherichia coli K12 1-(9Z-octadecenoyl)-sn-glycerol + phosphate
-
 ?
3.1.3.27 1-hexanoyl-sn-glycero-3-phosphate + H2O
-
 Escherichia coli 1-hexanoyl-sn-glycerol + phosphate
-
 ?
3.1.3.27 1-hexanoyl-sn-glycero-3-phosphate + H2O
-
 Escherichia coli K12 1-hexanoyl-sn-glycerol + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.27 PgpB
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.27 2.7
-
 phosphatidylethanolamine pH 7.5, 23°C Escherichia coli