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Information on EC 3.1.4.4 - phospholipase D and Organism(s) Vigna unguiculata and UniProt Accession O04865

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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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This record set is specific for:
Vigna unguiculata
UNIPROT: O04865
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The taxonomic range for the selected organisms is: Vigna unguiculata
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
-
-
-
-
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
1,2-diacylglycerophosphate + choline
show the reaction diagram
-
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
show the reaction diagram
phosphoric ester hydrolysis
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
choline + ?
show the reaction diagram
-
-
-
?
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
phospholipid + H2O
phosphatidic acid + alcohol
show the reaction diagram
phosphoric ester hydrolysis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
20-100 mM required for maximal activity in plants
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
pH 8.0, 37°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cow pea
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLDA1_VIGUN
809
0
91565
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
88000
-
x * 88000, SDS-PAGE
88110
-
x * 90000, SDS-PAGE, x * 88110, mass spectrometry
90000
-
x * 90000, SDS-PAGE, x * 88110, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification by single calcium-dependent octyl-sepharose chromatography step
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
high-yield expression in Pichia pastoris
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
heterologous high-yield expression of enzyme in Pichia pastoris and purification by single calcium-dependent octyl-sepharose chromatography step gives 8 mg of pure recombinant protein from 1 l of yeast culture without proteolytic degradation of the N-terminal calcium-dependent C2 lipid binding domain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pappan, K.; Wang, X.
Molecular and biochemical properties and physiological roles of plant phospholipase D
Biochim. Biophys. Acta
1439
151-166
1999
Arabidopsis sp., Brassica oleracea, Saccharomyces cerevisiae, Ricinus communis, Catharanthus roseus, Homo sapiens, Mus musculus, Oryza sativa, Spuriopimpinella brachycarpa, Rattus norvegicus, Zea mays, Vigna unguiculata (O04865), Nicotiana tabacum (P93400)
Manually annotated by BRENDA team
Abergel, C.; Abousalham, A.; Chenivesse, S.; Riviere, M.; Moustacas-Gardies, A.M.; Verger, R.
Crystallization and preliminary crystallographic study of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp)
Acta Crystallogr. Sect. D
57
320-322
2001
Vigna unguiculata
Manually annotated by BRENDA team
El Maarouf, H.; Carriere, F.; Riviere, M.; Abousalham, A.
Functional expression in insect cells, one-step purification and characterization of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp)
Protein Eng.
13
811-817
2000
Vigna unguiculata
Manually annotated by BRENDA team
Ben Ali, Y.; Carriere, F.; Abousalham, A.
High-level constitutive expression in Pichia pastoris and one-step purification of phospholipase D from cowpea (Vigna unguiculata L. Walp)
Protein Expr. Purif.
51
162-169
2007
Vigna unguiculata
Manually annotated by BRENDA team