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Literature summary for 3.1.4.46 extracted from
- The emerging physiological roles of the glycerophosphodiesterase family (2014), FEBS J., 281, 998-1016.
Application
| Application | Comment | Organism |
|---|---|---|
| diagnostics | the enzyme is used for the serological diagnosis of patients with tick-borne relapsing fever because the presence of antibodies against this spirochete has been detected upon infection, and for the setting-up of molecular and serologic techniques for the diagnosis of relapsing fever borreliosis | Borrelia hermsii |
| drug development | the enzyme might be a promising target for anti-malaria drug development | Plasmodium falciparum |
| environmental protection | the enzyme might be useful in the bioremediation of soil, through the detoxification of organophosphate pesticides and products of the degradation of nerve agents | Klebsiella aerogenes |
| medicine | the enzyme has immunogenic potential as a vaccine. Improvement of the GlpQ-based vaccine formulation, a DNA-based vaccine constructed by fusing Treponema pallidum GlpQ with interleukin-2, using chitosan nanoparticles as the vector, effectively attenuated the development of syphilitic lesions | Treponema pallidum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 13 potential homologues are identified and subdivided into two groups: the first comprising proteins with only one GP-PDE domain or canonical type A enzymes, AtGDPD1-6, and the second including proteins with two putative GP-PDE domains, type B enzymes AtGDPDL1-7 | Arabidopsis thaliana |
| constitutive enzyme, transgenic enzyme expression can complement the enzyme UgpQ in a gene ugpQ-deleted strain of Escherichia coli | Staphylococcus aureus |
| GDE2, maps to 11q13.4-13.5, and contains 17 exons and 16 introns, overexpression of a the tagged GDE2 in COS-7, HEK-293cells, and in HeLa cell endoplasmic reticulum, as well as at the plasma membrane, depending on cell confluence, with a predominant plasma-membrane localization in confluent | Homo sapiens |
| gene glpQ, phylogenetic analysis | Escherichia coli |
| gene gpdQ, DNA and amino acid seuence determination and analysis | Klebsiella aerogenes |
| gene ugpQ, phylogenetic analysis | Escherichia coli |
| gene YPL110c | Saccharomyces cerevisiae |
| gene YPL206c | Saccharomyces cerevisiae |
| the genome encodes seven genes, glpQ1-3 and ugpQ1-4 | Streptomyces coelicolor |
| YqiK is regulated by the same operon yqiHIK as other hydrolytic enzymes | Bacillus subtilis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis | Klebsiella aerogenes |
| crystal structure analysis | Agrobacterium tumefaciens |
| crystal structure analysis | Caldanaerobacter subterraneus subsp. tengcongensis |
| crystal structure analysis of the TM1621 protein | Thermotoga maritima |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | through directed evolution, the activity of GpdQ towards larger and nonphysiological substrates can be enhanced | Klebsiella aerogenes |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | plastid-localized isozyme AtGDPD1 | Arabidopsis thaliana | 9507 | - |
| cytoplasm | - |
Saccharomyces cerevisiae | 5737 | - |
| cytoplasm | - |
Bacillus subtilis | 5737 | - |
| cytoplasm | isozymes UgpQ1-4 | Streptomyces coelicolor | 5737 | - |
| cytosol | - |
Escherichia coli | 5829 | - |
| extracellular | isozymes GlpQ1-3 are secreted | Streptomyces coelicolor | - |
- |
| membrane | isozyme GDE2 contains a 43-amino acid intracellular N-terminal region, six transmembrane domains, an intracellular C-terminal domain of 82-amino acid residues and two 13-amino acid intracellular connecting loops between the transmembrane domains | Homo sapiens | 16020 | - |
| membrane | membrane fraction, mainly plasma membrane | Rattus norvegicus | 16020 | - |
| membrane | the enzyme is a hydrophilic lipoprotein that is also assumed to be anchored by N-terminal lipids to the periplasmic leaflet(s) of the peptidoglycan cytoplasmic membrane, and not to be exposed on the outer membrane of the pathogen | Treponema pallidum | 16020 | - |
| membrane | the enzyme is most probably bound to the periplasmic side of the inner or outer membrane | Borrelia hermsii | 16020 | - |
| additional information | lipoprotein D ís not surface-exposed | Pasteurella multocida | - |
- |
| additional information | the enzyme contains a 20-amino acid signal peptide typical of lipoproteins | Haemophilus influenzae | - |
- |
| additional information | the enzyme sequence has no signal sequences or hydrophobic motifs common to membrane proteins, but enzyme activity is detected almost exclusively in the membrane fraction | Mycoplasma hyorhinis | - |
- |
| outer membrane | a surface-exposed membrane lipoprotein | Haemophilus influenzae | 19867 | - |
| outer membrane | the enzyme resides on the outer leaflet of the outer membrane | Treponema pallidum | 19867 | - |
| periplasm | - |
Escherichia coli | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required for activity | Escherichia coli |  |
| Ca2+ | a calcium atom is chelated by three conserved residues and a glycerol molecule bound in the catalytic groove | Caldanaerobacter subterraneus subsp. tengcongensis | |
| Mg2+ | dependent on | Plasmodium falciparum | |
| Mg2+ | isozyme At-GDPD1 is Mg2+-dependent | Arabidopsis thaliana | |
| additional information | the enzyme requires divalent cations for activity | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27000 | - |
x * 27000 | Escherichia coli |
| 37000 | - |
x * 37000 | Saccharomyces cerevisiae |
| 138000 | - |
- |
Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | isozyme GDE2-mediated hydrolysis of the RECK GPI anchor is not a phospholipase D-like hydrolysis, which suggests a different attack of the phosphodiester bond compared to that reported for the other GDE2 substrate sn-glycero-3-phosphocholine | ? | - |
? | |
| additional information | Saccharomyces cerevisiae | the enzyme catalyzes cleavage of phosphatidylglycerol to diacylglycerol and glycerophosphate | ? | - |
? | |
| sn-glycero-3-phosphocholine + H2O | Rattus norvegicus | - |
choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | Saccharomyces cerevisiae | - |
choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | Homo sapiens | - |
choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | Borrelia hermsii | - |
choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | Arabidopsis thaliana | isozyme At-GDPD1 | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoethanolamine + H2O | Rattus norvegicus | - |
ethanolamine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoethanolamine + H2O | Arabidopsis thaliana | isozyme At-GDPD1 | ethanolamine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoglycerol + H2O | Arabidopsis thaliana | isozyme At-GDPD1 | glycerol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoinositol + H2O | Homo sapiens | - |
inositol + sn-glycerol 3-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Agrobacterium tumefaciens | - |
- |
- |
| Arabidopsis thaliana | - |
enzymes AtGDPD1-6 and AtGDPDL1-7 | - |
| Bacillus pumilus | - |
- |
- |
| Bacillus pumilus DSM 27 | - |
- |
- |
| Bacillus subtilis | P54527 | - |
- |
| Borrelia hermsii | Q45201 | - |
- |
| Caldanaerobacter subterraneus subsp. tengcongensis | - |
- |
- |
| Escherichia coli | P09394 | gene glpQ | - |
| Escherichia coli | P10908 | gene ugpQ | - |
| Haemophilus influenzae | Q06282 | - |
- |
| Haemophilus influenzae DSM 11121 | Q06282 | - |
- |
| Homo sapiens | Q8WTR4 | GDE2 (also named GDPD5) | - |
| Homo sapiens | Q9NPB8 | - |
- |
| Klebsiella aerogenes | - |
gene gpdQ | - |
| Lupinus albus | - |
two isozymes | - |
| Mus musculus | - |
- |
- |
| Musca domestica | - |
- |
- |
| Mycoplasma hyorhinis | E0TL71 | - |
- |
| Mycoplasma pneumoniae | P75367 | MPN420 or GlpQ; gene glpQ, the genome encodes two potential enzymes (MPN420 or GlpQ, and MPN566), although only GlpQ is functional | - |
| Pasteurella multocida | Q79LP3 | - |
- |
| Plasmodium falciparum | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Saccharomyces cerevisiae | - |
gene YPL206c | - |
| Saccharomyces cerevisiae | Q02979 | Gde1p; gene YPL110c | - |
| Staphylococcus aureus | Q99387 | constitutive enzyme | - |
| Streptomyces coelicolor | - |
the genome encodes seven genes that are putative GP-PDEs, GlpQ1-3 and UgpQ1-4 | - |
| Thermotoga maritima | - |
- |
- |
| Treponema pallidum | O30405 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| lipoprotein | a surface-exposed membrane lipoprotein, the enzyme contains a 20-amino acid signal peptide typical of lipoproteins | Haemophilus influenzae |
| lipoprotein | lipoprotein D has enzyme activity similar to other bacterial enzyme, which is modulated by, but not dependent on, its N-terminal lipidation | Pasteurella multocida |
| lipoprotein | the enzyme is a hydrophilic lipoprotein that is also assumed to be anchored by N-terminal lipids to the periplasmic leaflet(s) of the peptidoglycan cytoplasmic membrane | Treponema pallidum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| brain | high expression level | Homo sapiens | - |
| brain | the brain enzyme is regionally and developmentally regulated | Rattus norvegicus | - |
| kidney | - |
Rattus norvegicus | - |
| larva | - |
Musca domestica | - |
| liver | - |
Rattus norvegicus | - |
| additional information | GDE2 is widely expressed, with relative low levels in the kidney and prostate | Homo sapiens | - |
| neuron | mature motor neurons and not in undifferentiated progenitors | Homo sapiens | - |
| skeletal muscle | - |
Homo sapiens | - |
| uterus | in uterine secretion | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| bis(glycerophospho)glycerol + H2O | low activity | Escherichia coli | ? | - |
? | |
| cardiolipin + H2O | low activity | Escherichia coli | ? | - |
? | |
| additional information | high substrate specificity | Mus musculus | ? | - |
? | |
| additional information | high substrate specificity | Rattus norvegicus | ? | - |
? | |
| additional information | high substrate specificity | Homo sapiens | ? | - |
? | |
| additional information | isozyme GDE2-mediated hydrolysis of the RECK GPI anchor is not a phospholipase D-like hydrolysis, which suggests a different attack of the phosphodiester bond compared to that reported for the other GDE2 substrate sn-glycero-3-phosphocholine | Homo sapiens | ? | - |
? | |
| additional information | the enzyme catalyzes cleavage of phosphatidylglycerol to diacylglycerol and glycerophosphate | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | recombinant isozyme AtGPDPL1 shows limited enzymatic activity toward glycerophosphodiesters | Arabidopsis thaliana | ? | - |
? | |
| additional information | the enzyme has a broad substrate specificity. It hydrolyzes glycerophosphodiester bonds through its recognition of the glycerophospho moiety, but it does not hydrolyze other types of bonds, such as that of bis(p-nitrophenyl)phosphate. No activity towards phosphatidyl-DL-glycerol or lysophosphatidyl-DL-glycerol | Escherichia coli | ? | - |
? | |
| additional information | the enzyme has a very broad substrate specificity, it catalyzes the hydrolysis not only of glycerophosphoethanolamine, but also of phosphomonoesters, diesters and triesters, in addition to phosphothiolates. The enzyme can hydrolyze several organophosphates | Klebsiella aerogenes | ? | - |
? | |
| additional information | the enzyme is active towards more complex substrates, even if their final product is always glycerol 3-phosphate. It hydrolyzes phosphodiester bonds between adjacent glycerol units. Substrates are polyglycerophosphates, such as purified cell-wall teichoic acid, as well as deacylated, unsubstituted lipoteichoic acid, di(glycerophospho)glycerol (deacylated cardiolipin) and mono(glycerophospho)glycerol | Bacillus pumilus | ? | - |
? | |
| additional information | the enzyme is active towards more complex substrates, even if their final product is always glycerol 3-phosphate. It hydrolyzes phosphodiester bonds between adjacent glycerol units. Substrates are polyglycerophosphates, such as purified cell-wall teichoic acid, as well as deacylated, unsubstituted lipoteichoic acid, di(glycerophospho)glycerol (deacylated cardiolipin) and mono(glycerophospho)glycerol | Bacillus pumilus DSM 27 | ? | - |
? | |
| sn-glycero-3-phospho-L-serine | - |
Escherichia coli | L-serine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | - |
Rattus norvegicus | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | - |
Saccharomyces cerevisiae | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | - |
Arabidopsis thaliana | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | - |
Escherichia coli | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | - |
Homo sapiens | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | - |
Borrelia hermsii | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | preferred substrate | Musca domestica | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | isozyme At-GDPD1 | Arabidopsis thaliana | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphocholine + H2O | the brain enzyme is specific for | Rattus norvegicus | choline + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoethanolamine + H2O | - |
Rattus norvegicus | ethanolamine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoethanolamine + H2O | - |
Musca domestica | ethanolamine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoethanolamine + H2O | - |
Escherichia coli | ethanolamine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoethanolamine + H2O | isozyme At-GDPD1 | Arabidopsis thaliana | ethanolamine + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoglycerol + H2O | - |
Musca domestica | glycerol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoglycerol + H2O | - |
Escherichia coli | glycerol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoglycerol + H2O | isozyme At-GDPD1 | Arabidopsis thaliana | glycerol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoinositol + H2O | - |
Musca domestica | inositol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoinositol + H2O | - |
Escherichia coli | inositol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoinositol + H2O | - |
Homo sapiens | inositol + sn-glycerol 3-phosphate | - |
? | |
| sn-glycero-3-phosphoserine | - |
Musca domestica | serine + sn-glycerol 3-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 37000 | Saccharomyces cerevisiae |
| ? | x * 27000 | Escherichia coli |
| hexamer | the T2047enzyme forms a hexamer as a trimer of dimers, with a channel passing through the center of the assembly | Agrobacterium tumefaciens |
| More | the GP-PDE domain localized at the C terminus | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GDE | - |
Rattus norvegicus |
| Gde1p | - |
Saccharomyces cerevisiae |
| GDE2 | - |
Homo sapiens |
| GDE5 | - |
Homo sapiens |
| GDPD5 | - |
Homo sapiens |
| GDPD6 | - |
Homo sapiens |
| GlpQ | - |
Escherichia coli |
| GlpQ | - |
Haemophilus influenzae |
| GlpQ | - |
Treponema pallidum |
| GlpQ | - |
Pasteurella multocida |
| GlpQ | - |
Mycoplasma pneumoniae |
| GlpQ1 | - |
Streptomyces coelicolor |
| GlpQ2 | - |
Streptomyces coelicolor |
| GlpQ3 | - |
Streptomyces coelicolor |
| glycerophosphodiester phosphodiesterase | - |
Mus musculus |
| glycerophosphodiester phosphodiesterase | - |
Rattus norvegicus |
| glycerophosphodiester phosphodiesterase | - |
Saccharomyces cerevisiae |
| glycerophosphodiester phosphodiesterase | - |
Arabidopsis thaliana |
| glycerophosphodiester phosphodiesterase | - |
Klebsiella aerogenes |
| glycerophosphodiester phosphodiesterase | - |
Lupinus albus |
| glycerophosphodiester phosphodiesterase | - |
Streptomyces coelicolor |
| glycerophosphodiester phosphodiesterase | - |
Bacillus pumilus |
| glycerophosphodiester phosphodiesterase | - |
Plasmodium falciparum |
| glycerophosphodiester phosphodiesterase | - |
Agrobacterium tumefaciens |
| glycerophosphodiester phosphodiesterase | - |
Thermotoga maritima |
| glycerophosphodiester phosphodiesterase | - |
Musca domestica |
| glycerophosphodiester phosphodiesterase | - |
Caldanaerobacter subterraneus subsp. tengcongensis |
| glycerophosphodiester phosphodiesterase | - |
Escherichia coli |
| glycerophosphodiester phosphodiesterase | - |
Homo sapiens |
| glycerophosphodiester phosphodiesterase | - |
Staphylococcus aureus |
| glycerophosphodiester phosphodiesterase | - |
Haemophilus influenzae |
| glycerophosphodiester phosphodiesterase | - |
Borrelia hermsii |
| glycerophosphodiester phosphodiesterase | - |
Treponema pallidum |
| glycerophosphodiester phosphodiesterase | - |
Pasteurella multocida |
| glycerophosphodiester phosphodiesterase | - |
Mycoplasma pneumoniae |
| glycerophosphodiester phosphodiesterase | - |
Mycoplasma hyorhinis |
| glycerophosphodiester phosphodiesterase | - |
Bacillus subtilis |
| GP-PDE | - |
Mus musculus |
| GP-PDE | - |
Rattus norvegicus |
| GP-PDE | - |
Saccharomyces cerevisiae |
| GP-PDE | - |
Arabidopsis thaliana |
| GP-PDE | - |
Klebsiella aerogenes |
| GP-PDE | - |
Lupinus albus |
| GP-PDE | - |
Streptomyces coelicolor |
| GP-PDE | - |
Bacillus pumilus |
| GP-PDE | - |
Plasmodium falciparum |
| GP-PDE | - |
Agrobacterium tumefaciens |
| GP-PDE | - |
Thermotoga maritima |
| GP-PDE | - |
Musca domestica |
| GP-PDE | - |
Caldanaerobacter subterraneus subsp. tengcongensis |
| GP-PDE | - |
Escherichia coli |
| GP-PDE | - |
Homo sapiens |
| GP-PDE | - |
Staphylococcus aureus |
| GP-PDE | - |
Haemophilus influenzae |
| GP-PDE | - |
Borrelia hermsii |
| GP-PDE | - |
Treponema pallidum |
| GP-PDE | - |
Pasteurella multocida |
| GP-PDE | - |
Mycoplasma pneumoniae |
| GP-PDE | - |
Mycoplasma hyorhinis |
| GP-PDE | - |
Bacillus subtilis |
| GPCPD1 | - |
Homo sapiens |
| GPD | - |
Borrelia hermsii |
| GPD protein | - |
Mycoplasma hyorhinis |
| GpdQ | - |
Klebsiella aerogenes |
| HPD | - |
Haemophilus influenzae |
| lipoprotein D | - |
Pasteurella multocida |
| MPN420 | - |
Mycoplasma pneumoniae |
| PfGDPD | - |
Plasmodium falciparum |
| Pgc1p | - |
Saccharomyces cerevisiae |
| Protein D | - |
Haemophilus influenzae |
| T2047 | - |
Agrobacterium tumefaciens |
| TM1621 | - |
Thermotoga maritima |
| ttGDD | - |
Caldanaerobacter subterraneus subsp. tengcongensis |
| UGP1 | - |
Streptomyces coelicolor |
| Ugp2 | - |
Streptomyces coelicolor |
| UGP3 | - |
Streptomyces coelicolor |
| Ugp4 | - |
Streptomyces coelicolor |
| UgpQ | - |
Escherichia coli |
| YqiK | - |
Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
- |
Musca domestica |
| 7.5 | - |
- |
Escherichia coli |
| 9 | - |
- |
Escherichia coli |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Homo sapiens | osmotic stress conditions resulting from high salt concentrations cause a decrease in the sioyzme GDE2 mRNA half-life, with the consequent lowering of GDE2 protein levels and a decrease in glycero-3-phosphocholine hydrolysis in transgenic murine mIMCD3 cells | down |
| Escherichia coli | expression of the UgpQ protein is significantly induced in phosphate-starved wild-type Escherichia coli | up |
| Homo sapiens | GDE2 up-regulation upon retinoic-acid treatment | up |
| Bacillus subtilis | high-salinity growth conditions induce the up-regulation of the transcription of the operon yqiHIK encoding the enzyme | up |
| Saccharomyces cerevisiae | increased enzyme expression in microarray studies under low-phosphate conditions | up |
| Arabidopsis thaliana | salt and osmotic stress induce up-regulation of AtGDPDL genes, while AtGDPDs genes are up-regulated by inorganic phosphate deprivation | up |
| Lupinus albus | the isozymes are induced by phosphate deprivation | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | phylogenetic analysis, overview | Mus musculus |
| evolution | phylogenetic analysis, overview | Rattus norvegicus |
| evolution | phylogenetic analysis, overview | Arabidopsis thaliana |
| evolution | phylogenetic analysis, overview | Lupinus albus |
| evolution | phylogenetic analysis, overview | Streptomyces coelicolor |
| evolution | phylogenetic analysis, overview | Bacillus pumilus |
| evolution | phylogenetic analysis, overview | Musca domestica |
| evolution | phylogenetic analysis, overview | Caldanaerobacter subterraneus subsp. tengcongensis |
| evolution | phylogenetic analysis, overview | Homo sapiens |
| evolution | phylogenetic analysis, overview | Staphylococcus aureus |
| evolution | phylogenetic analysis, overview | Saccharomyces cerevisiae |
| evolution | phylogenetic analysis, overview | Haemophilus influenzae |
| evolution | phylogenetic analysis, overview | Borrelia hermsii |
| evolution | phylogenetic analysis, overview | Treponema pallidum |
| evolution | phylogenetic analysis, overview | Pasteurella multocida |
| evolution | phylogenetic analysis, overview | Mycoplasma pneumoniae |
| evolution | phylogenetic analysis, overview | Mycoplasma hyorhinis |
| evolution | phylogenetic analysis, overview | Bacillus subtilis |
| evolution | phylogenetic analysis, overview. A common feature of this enzyme family is the presence of the classical triosephosphate isomerase barrel fold | Thermotoga maritima |
| evolution | phylogenetic analysis, overview. Escherichia coli GlpQ and UgpQ possess a significant similarity, suggesting a common evolutionary origin | Escherichia coli |
| evolution | phylogenetic analysis, overview. PfGDPD shows clear homology with bacterial GP-PDEs | Plasmodium falciparum |
| evolution | phylogenetic analysis, overview. The enzyme Pgc1p belongs to the superfamily of phospholipase-C-like enzymes | Saccharomyces cerevisiae |
| evolution | phylogenetic analysis, overview. The enzyme shows a structure unusual for the enzyme family, the T2047enzyme of Agrobacterium tumefaciens forms a hexamer and, in particular, a trimer of dimers, with a channel passing through the center of the assembly | Agrobacterium tumefaciens |
| evolution | phylogenetic analysis, overview. The phosphodiesterase GpdQ is unrelated to the Escherichia coli enzyme UgpQ. The crystal structure of GpdQ emphasizes its difference compared to all other bacterial GP-PDEs with respect to the absence of the conserved triosephosphate isomerase barrel fold in the catalytic site. GpdQ is clustered separately in the phylogenetic tree and appears as a structurally distinct GP-PDE, its secondary structure prediction suggests that it more properly belongs to the alpha/beta-sandwich metallo-dependent phosphoesterase family | Klebsiella aerogenes |
| malfunction | ablating GDE2 expression in the spinal cord using small-interfering RNAs results in the loss of post-mitotic motor neurons and an increase in cell death | Homo sapiens |
| malfunction | deletion of the YPL110c gene leads to the massive accumulation of glycero-3-phosphocholine | Saccharomyces cerevisiae |
| malfunction | deletion of the yqiHIK operon impairs the growth of Bacillus subtilis at high salinity | Bacillus subtilis |
| malfunction | inactivation of gene glpQ results in reduced bacteria growth, loss of hydrogen peroxide production and a complete loss of Mycoplasma pneumoniae cytotoxicity towards HeLa cells | Mycoplasma pneumoniae |
| malfunction | isozyme GDE5 expression down-regulation in several types of skeletal muscle atrophies is induced by aging and denervation | Homo sapiens |
| malfunction | loss-of-function of the plastid-localized isozyme AtGDPD1 induces a decrease of enzyme activity, glycerol 3-phosphate and inorganic phosphate content, and seedling growth rate compared to the wild-type plant | Arabidopsis thaliana |
| additional information | absence of the conserved triosephosphate isomerase barrel fold in the catalytic site, the secondary structure shows an alpha/beta-sandwich | Klebsiella aerogenes |
| additional information | lipoprotein D has enzyme activity similar to other bacterial enzyme, which is modulated by, but not dependent on, its N-terminal lipidation | Pasteurella multocida |
| additional information | proposal of a mechanism of catalysis through two reaction steps, with the glycerol and the phosphate moieties forming a cyclic phosphate intermediate that is stabilized by the calcium ion | Caldanaerobacter subterraneus subsp. tengcongensis |
| additional information | the brain enzyme is regionally and developmentally regulated | Rattus norvegicus |
| additional information | the enzyme TM1621 structure suggests that the biologically relevant form is a monomer composed of 11 beta-strands, 10 alpha-helices and four 310-helices | Thermotoga maritima |
| additional information | the GP-PDE domain localized at the C terminus | Saccharomyces cerevisiae |
| additional information | the organism encodes two potential enzymes (MPN420 or GlpQ, and MPN566), although only GlpQ is functional. MPN566 has no enzymatic activity, and inactivation of its gene does not result in any detectable phenotype | Mycoplasma pneumoniae |
| physiological function | enzyme Pgc1p controls the phosphatidylglycerol content of the cell membranes by cleavage of phosphatidylglycerol to diacylglycerol and glycerophosphate | Saccharomyces cerevisiae |
| physiological function | isozyme GDE2 is directly linked to cell differentiation, which triggers motor neuron differentiation, and it acts as an osmoregulated enzyme. GDE2 promotion of neurogenesis follows a different molecular mechanism compared to that postulated for GDE2 osmoregulation of kidney cells, overview. GDE2 up-regulation upon retinoic-acid treatment is sufficient to induce neurite formation that is blocked upon GDE2 downregulation by siRNAs. Isozmye GDE2 is involved in the regulation of neuronal transcriptional programs | Homo sapiens |
| physiological function | isozyme GDE5 inhibits skeletal muscle development independent of its enzymatic activity. Isozyme GDE5 expression in brain can contribute to variations in cortical surface area. Decreased isozyme GDE5 expression might represent an adaptation response to counteract the pathology, overview | Homo sapiens |
| physiological function | lipoprotein D is not surface-exposed and is not a virulence factor useful for vaccine design | Pasteurella multocida |
| physiological function | plastid-localized isozyme AtGDPD1 is devoted to the glycerophosphodiester degradation pathway as a source of inorganic phosphate | Arabidopsis thaliana |
| physiological function | the enzyme activity contributes to bacterial pathogenicity, overview. The enzyme has all of the properties necessary for its application as an antigenically active carrier protein for conjugate vaccines, mainly because it is a surface-exposed membrane lipoprotein that is highly conserved among different Haemophilus influenzae strains | Haemophilus influenzae |
| physiological function | the enzyme is considered to be essential during the phase of metamorphosis, when the larvae enter the pupal stage and the organism extensively hydrolyzes its cellular constituents and reassembles the components into the tissues of the adult organism | Musca domestica |
| physiological function | the enzyme is required for glycerol 3-phosphate production starting from deacylated phospholipids. This metabolic pathway appears to contribute to cell proliferation during host infection, which leads to an increased cell density of Borrelia hermsii in the host blood | Borrelia hermsii |
| physiological function | the enzyme is responsible for glycero-3-phosphocholine hydrolysis, which is used as a phosphate source. It might also act by binding potential partners involved in phosphate metabolism | Saccharomyces cerevisiae |
| physiological function | the enzyme might contribute to the damage to the human host cell membranes by Mycoplasma hyorhinis, that is involved in human gastric cancer | Mycoplasma hyorhinis |
| physiological function | the enzyme might have a role in osmoprotection | Bacillus subtilis |
| physiological function | the functional glycerophosphodiester phosphodiesterase also controls the expression of a set of genes that encode lipoproteins, the glycerol facilitator and a metal ion ABC transporter | Mycoplasma pneumoniae |
| physiological function | the primary physiological function of UgpQ is the use of glycerophosphodiesters as a source of phosphate, an activity that is performed more efficiently by UgpQ than by homologue GlpQ. The enzyme might have a role in bacterial pathogenicity | Escherichia coli |
| physiological function | the primary physiological function of UgpQ is the use of glycerophosphodiesters as a source of phosphate, an activity that is performed more efficiently by UgpQ than by homologue GlpQ. The ugp-encoded transport system represents another Escherichia coli transport system for sn-glycerol 3-phosphate | Escherichia coli |
| physiological function | the two isozymes are phosphate-deprivation induced and regulate root hair development and density, suggesting their role in plant acclimation to phosphate deprivation | Lupinus albus |
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Release 2023.1 (January 2023)
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