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Information on EC 3.1.4.4 - phospholipase D and Organism(s) Dictyostelium discoideum and UniProt Accession Q54UK0

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.4 phospholipase D
IUBMB Comments
Also acts on other phosphatidyl esters.
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Select one or more organisms in this record: ?
This record set is specific for:
Dictyostelium discoideum
UNIPROT: Q54UK0
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Word Map
The taxonomic range for the selected organisms is: Dictyostelium discoideum
The enzyme appears in selected viruses and cellular organisms
Synonyms
pld, phospholipase d, nape-pld, phospholipase d1, dermonecrotic toxin, phospholipase d2, pc-pld, pldalpha, rpld1, spo14, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AtPLDalpha1
-
-
-
-
AtPLDalpha2
-
-
-
-
AtPLDbeta1
-
-
-
-
AtPLDbeta2
-
-
-
-
AtPLDdelta
-
-
-
-
AtPLDepsilon
-
-
-
-
AtPLDgamma1
-
-
-
-
AtPLDgamma2
-
-
-
-
AtPLDgamma3
-
-
-
-
AtPLDp1
-
-
-
-
AtPLDp2
-
-
-
-
AtPLDzeta
-
-
-
-
choline phosphatase
-
-
-
-
hPLD1
-
-
-
-
hPLD2
-
-
-
-
lecithinase D
-
-
-
-
lipophosphodiesterase II
-
-
-
-
Meiosis-specific sporulation protein SPO14
-
-
-
-
mPLD1
-
-
-
-
mPLD2
-
-
-
-
Phosphatidylcholine-hydrolyzing phospholipase D1
-
-
-
-
Phosphatidylcholine-hydrolyzing phospholipase D2
-
-
-
-
Phospholipase D1 PHOX and PX containing domain
-
-
-
-
Phospholipase D2 PHOX and PX containing domain
-
-
-
-
PLD delta
-
-
-
-
PLD epsilon
-
-
-
-
PLD zeta
-
-
-
-
PLD1C
-
-
-
-
PLDalpha
-
-
-
-
PLDalpha3
-
-
-
-
PLDbeta
-
-
-
-
PLDdelta1
-
-
-
-
PLDzeta1
-
-
-
-
PLDzeta2
-
-
-
-
rPLD1
-
-
-
-
rPLD2
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine phosphatidohydrolase
Also acts on other phosphatidyl esters.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-87-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + H2O
choline + phosphatidate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
phosphatidic acid + choline
show the reaction diagram
-
a phospholipid transphosphatidylation reaction
-
-
?
additional information
?
-
-
phospholipase D activity is essential for actin localization and actin-based motility
-
-
?
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
phosphatidylcholine + H2O
choline + phosphatidate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
show the reaction diagram
-
-
-
?
additional information
?
-
-
phospholipase D activity is essential for actin localization and actin-based motility
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme PLDA; three isozymes PLDA, PLDB, and PDLC, encoded by genes plda, pldb, and pldc
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
cells lacking PldB preferentially sort to the stalk in chimeric fruiting bodies with wild-type cells
metabolism
-
PldB mediates quorum sensing in the CMF pathway and regulates the dissociation of G protein Galpha2betagamma
physiological function
-
PldB regulates cAMP chemotaxis, overview. Phospholipase D controls Dictyostelium development by regulating G protein signaling, its activity is required for CMF to alter the kinetics of cAMP-induced G protein signaling, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLDA_DICDI
1269
0
142142
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of a pldB disruption mutant by nucleotide replacement
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, expression analysis and regulation
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, expression analysis and regulation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zouwail, S.; Pettitt, T.R.; Dove, S.K.; Chibalina, M.V.; Powner, D.J.; Haynes, L.; Wakelam, M.J.; Insall, R.H.
Phospholipase D activity is essential for actin localization and actin-based motility in Dictyostelium
Biochem. J.
389
207-214
2005
Dictyostelium discoideum
Manually annotated by BRENDA team
Raghu, P.; Manifava, M.; Coadwell, J.; Ktistakis, N.T.
Emerging findings from studies of phospholipase D in model organisms (and a short update on phosphatidic acid effectors)
Biochim. Biophys. Acta
1791
889-897
2009
Saccharomyces cerevisiae, Caenorhabditis elegans, Danio rerio (A2BG86), Danio rerio, Homo sapiens (O14939), Homo sapiens (Q13393), Dictyostelium discoideum (Q54UK0), Dictyostelium discoideum (Q54WR4), Dictyostelium discoideum (Q54Z25), Drosophila melanogaster (Q7KML4)
Manually annotated by BRENDA team
Ray, S.; Chen, Y.; Ayoung, J.; Hanna, R.; Brazill, D.
Phospholipase D controls Dictyostelium development by regulating G protein signaling
Cell. Signal.
23
335-343
2011
Dictyostelium discoideum, Dictyostelium discoideum AX3
Manually annotated by BRENDA team