Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.4.46 - glycerophosphodiester phosphodiesterase and Organism(s) Haemophilus influenzae and UniProt Accession Q06282

for references in articles please use BRENDA:EC3.1.4.46
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.46 glycerophosphodiester phosphodiesterase
IUBMB Comments
Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Haemophilus influenzae
UNIPROT: Q06282
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Haemophilus influenzae
The enzyme appears in selected viruses and cellular organisms
Synonyms
glycerophosphodiester phosphodiesterase, lipoprotein d, glpq2, igd-binding protein, glpq1, gpd protein, outer membrane protein d, pfgdpd, gpcpd1, ttgdpd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycerophosphodiester phosphodiesterase
-
gene hpd protein
-
-
-
-
glycerophosphodiester phosphodiesterase
glycerophosphoryl diester phosphodiesterase
-
-
-
-
GPX-PDE
-
-
-
-
IGD-binding protein
-
-
-
-
IgD-binding protein D
-
-
-
-
immunoglobulin D-binding protein
-
-
-
-
outer membrane protein D
-
-
phosphodiesterase, glycerophosphodiester
-
-
-
-
phosphohydrolase GpdQ
-
-
-
-
protein D/glycerophosphodiester phosphodiesterase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic diester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
glycerophosphodiester glycerophosphohydrolase
Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY hide
86280-59-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerophosphocholine + H2O
sn-glycerol 3-phosphate + choline
show the reaction diagram
-
utilization of glycerophosphocholine and incorporation of choline from host cell membranes
-
-
?
L-alpha-glycerophosphocholine + H2O
choline + sn-glycerol-3-phosphate
show the reaction diagram
-
-
-
-
?
L-alpha-glycerophosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme responsible for interaction with immunoglobulin D, important virulence factor
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycerophosphocholine + H2O
sn-glycerol 3-phosphate + choline
show the reaction diagram
-
utilization of glycerophosphocholine and incorporation of choline from host cell membranes
-
-
?
L-alpha-glycerophosphocholine + H2O
choline + sn-glycerol-3-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme responsible for interaction with immunoglobulin D, important virulence factor
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
a surface-exposed membrane lipoprotein
Manually annotated by BRENDA team
additional information
the enzyme contains a 20-amino acid signal peptide typical of lipoproteins
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic analysis, overview
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
malfunction
-
abrogation of nontypeable Haemophilus influenzae protein D function reduces phosphorylcholine decoration, adherence to airway epithelial A549 cells, and fitness in a chinchilla, Chinchilla lanigera, model of otitis media. Exposure of NTHI to antibodies directed against the vaccine formulation recapitulates the phosphorylcholine decoration and NTHI adherence phenotypes exhibite by PD/GlpQ-deficient NTHI, mechanism(s) of anti-PD/GlpQ antibody-mediated protection from NTHI-induced otitis media, overview
physiological function
-
PD/GlpQ enzymatic activity is predicted to facilitate choline and sn-glycerol-3-phosphate acquisition via the cleavage of L-alpha-glycerophosphocholine, an abundant catabolite of host phospholipids
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
a surface-exposed membrane lipoprotein, the enzyme contains a 20-amino acid signal peptide typical of lipoproteins
lipoprotein
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
generation of a nonpolar hpd/glpQ mutant strain, that retains detectable mRNA expression of the upstream gene glpT, which is cotranscribed with hpd/glpQ
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
generation of an 86-028NP-derived NTHI strain that expresses an hpd/glpQ promoter-driven luciferase reporter from the vector pKMLN-01, hpd/glpQ is expressed in an operon with glpT
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
to study if membrane protein D (PD)-induced protection against NTHI as a vaccine is due to antibodies that inhibit or neutralize its enzymatic activity, a GlpQ enzyme inhibition assay is developed, and serum samples collected from Finnish infants before and after Pnc-PD vaccination are analyzed for enzyme inhibition and anti-PD IgG antibody concentration. Before vaccination at age 2 months, the majority (84%) of infants has no detectable anti-PD IgG antibodies, and all are enzyme inhibition assay negative. At age 13 to 16 months, all infants receiving three or four doses of Pnc-PD have detectable anti-PD IgG antibodies and 36% of the infants receiving three doses and 26% of the infants receiving four doses of Pnc-PD are inhibition assay positive
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Munson, R.S.; Sasaki, K.
Protein D, a putative immunoglobulin D-binding protein produced by Haemophilus influenzae, is glycerophosphodiester phosphodiesterase
J. Bacteriol.
175
4569-4571
1993
Haemophilus influenzae
Manually annotated by BRENDA team
Yanaka, N.
Mammalian glycerophosphodiester phosphodiesterases
Biosci. Biotechnol. Biochem.
71
1811-1818
2007
Haemophilus influenzae, Escherichia coli (P09394), Escherichia coli (P10908)
Manually annotated by BRENDA team
Toropainen, M.; Raitolehto, A.; Henckaerts, I.; Wauters, D.; Poolman, J.; Lestrate, P.; Kaeyhty, H.
Pneumococcal Haemophilus influenzae protein D conjugate vaccine induces antibodies that inhibit glycerophosphodiester phosphodiesterase activity of protein D
Infect. Immun.
76
4546-4553
2008
Haemophilus influenzae
Manually annotated by BRENDA team
Johnson, R.W.; McGillivary, G.; Denoel, P.; Poolman, J.; Bakaletz, L.O.
Abrogation of nontypeable Haemophilus influenzae protein D function reduces phosphorylcholine decoration, adherence to airway epithelial cells, and fitness in a chinchilla model of otitis media
Vaccine
29
1211-1221
2011
Haemophilus influenzae, Haemophilus influenzae 86-028NP
Manually annotated by BRENDA team
Corda, D.; Mosca, M.; Ohshima, N.; Grauso, L.; Yanaka, N.; Mariggio, S.
The emerging physiological roles of the glycerophosphodiesterase family
FEBS J.
281
998-1016
2014
Agrobacterium tumefaciens, Arabidopsis thaliana, Bacillus pumilus, Bacillus pumilus DSM 27, Bacillus subtilis (P54527), Borrelia hermsii (Q45201), Caldanaerobacter subterraneus subsp. tengcongensis, Escherichia coli (P09394), Escherichia coli (P10908), Haemophilus influenzae (Q06282), Haemophilus influenzae DSM 11121 (Q06282), Homo sapiens (Q8WTR4), Homo sapiens (Q9NPB8), Klebsiella aerogenes, Lupinus albus, Mus musculus, Musca domestica, Mycoplasma hyorhinis (E0TL71), Mycoplasma pneumoniae (P75367), Pasteurella multocida (Q79LP3), Plasmodium falciparum, Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q02979), Staphylococcus aureus (Q99387), Streptomyces coelicolor, Thermotoga maritima, Treponema pallidum (O30405)
Manually annotated by BRENDA team