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Information on EC 3.1.4.4 - phospholipase D and Organism(s) Streptomyces sp. and UniProt Accession P84147
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3.1.4.4 phospholipase DIUBMB Comments
Also acts on other phosphatidyl esters.
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Word Map
- 3.1.4.4
-
phosphatidic
- diacylglycerol
- pkc
-
liposomal
- doxorubicin
- agonist
-
pegylated
-
phorbol
- phospholipases
-
transphosphatidylation
- 12-myristate
-
adp-ribosylation
- 13-acetate
- pertussis
-
phosphohydrolase
-
arachidonic
- propranolol
- phosphoinositide
-
gtp-binding
- fmlp
-
prelabeled
- anandamide
- rhoa
- 1-butanol
-
endocannabinoids
- staurosporine
-
lysophosphatidic
- pc-plc
-
phosphatidylcholine-specific
-
latissimus
- diglyceride
- pkcalpha
-
phosphatidylinositol-specific
- pseudotuberculosis
- 1,2-diacylglycerol
- arf6
- cannabinoids
-
fmet-leu-phe
-
listening
-
fmlp-stimulated
-
platinum-resistant
- analysis
-
phosphoinositide-specific
- gtpgammas
- synthesis
-
3hcholine
-
hand-foot
-
platinum-sensitive
-
fmlp-induced
- lymphadenitis
- medicine
-
ptdins4,5p2
- molecular biology
- 5-kinase
- agriculture
- biotechnology
The taxonomic range for the selected organisms is: Streptomyces sp.
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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 D
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
-
-
-
-
additional information
the enzyme belongs to the PLD superfamily containing two HKD motifs
PLD
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphatidylcholine + H2O = choline + a phosphatidate
catalytic mechanism, PLD uses a ping-pong type of reaction through the formation of a covalent phosphatidyl-enzyme intermediate, structure-function relationship, and substrate recognition and specificity, overview
a phosphatidylcholine + H2O = choline + a phosphatidate
mechanism, structural requirements of substrate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine phosphatidohydrolase
Also acts on other phosphatidyl esters.
CAS REGISTRY NUMBER
COMMENTARY
9001-87-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dioleoyl-sn-glycerophosphocholine + 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)-1,3-propanediol
choline + 1,2-dioleoyl-sn-glycerophospho-2-[bis(2-hydroxyethyl)imino]-2-(hydroxymethyl)-1,3-propanediol
-
with BisTris as acceptor alcohol two regioisomeric forms of phosphatidyl-BisTris are obtained, product yield: 19.6% (regioisomer I), 3,1% (regioisomer II), purity of product: 98% (regioisomer I), 97% (regioisomer I)
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + diethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-diethanolamine
-
product yield: 47.2%, purity of product: 81.5%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + H2O
choline + 1,2-dioleoyl-sn-glycero-3-phosphatidic acid
-
-
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + serinol
choline + 1,2-dioleoyl-sn-glycerophospho-serinol
-
product yield: 45.8%, purity of product: 68%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + triethanolamine
choline + 1,2-dioleoyl-sn-glycerophospho-triethanolamine
-
product yield: 33.7%, purity of product: 65.4%
-
-
?
1,2-dioleoyl-sn-glycerophosphocholine + tris(hydroxymethyl)-aminomethane
choline + 1,2-dioleoyl-sn-glycerophospho-tris(hydroxymethyl)-aminomethane
-
product yield: 31.6%, purity of product: 95%
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidic acid + choline
-
-
phosphatidic acid is negatively charged
?
2 1,2-dioleoyl-sn-glycerophosphocholine + diethanolamine
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-diethanolamine
-
-
-
-
?
2 1,2-dioleoyl-sn-glycerophosphocholine + serinol
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-serinol
-
-
-
-
?
2 1,2-dioleoyl-sn-glycerophosphocholine + triethanolamine
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-triethanolamine
-
-
-
-
?
2 1,2-dioleoyl-sn-glycerophosphocholine + tris(hydroxymethyl)-aminomethane
2 choline + bis(1,2-dioleoyl-sn-glycerophospho)-tris(hydroxymethyl)-aminomethane
-
-
-
-
?
phosphatidylcholine + L-serine
phosphatidyl-L-serine + choline
-
-
-
?
phosphatidylcholine + glycerol
phosphatidylglycerol + choline
-
catalyzes the transphosphatidylation of glycerol, but not that of L-serine, myo-inositol or ethanolamine
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
-
hydrolytic and transphosphatylation activity
-
?
additional information
?
-
PLD performs two different reactions: a hydrolytic reaction and a transphosphatidylation reaction, the latter with a primary alcohol, both pathway share a common intermediate, mechanism, overview
-
-
?
additional information
?
-
-
structural requirements of substrates, general molecular aspects
-
?
additional information
?
-
-
in presence of glycerol, the rate of hydrolysis of phosphatiylcholine and the rate of phosphytidylglycerol formation are almost identical
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
required, leads to aggregation, fusion and precipitation of phospholipid vesicles due to complexes with negatively charged reaction product
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
124
-
transphosphatidylation reaction, substrate: tris(hydroxymethyl)-aminomethane, specific activity of hydrolysis reaction: value below 5 micromol/min/mg
166.9
-
bio-imprinted immobilized enzyme, pH 6.0, temperature not specified in the publication
223.5
-
transphosphatidylation reaction, substrate: ethanolamine, specific activity of hydrolysis reaction: value below 5 micromol/min/mg
38.5
-
transphosphatidylation reaction, substrate: 2-[bis(2-hydroxyethyl)imino]-2-(hydroxymethyl)-1,3-propanediol, specific activity of hydrolysis reaction: 22 micromol/min/mg
380.3
-
transphosphatidylation reaction, substrate: diethanolamine, specific activity of hydrolysis reaction: value below 5 micromol/min/mg
410.1
-
transphosphatidylation reaction, substrate: triethanolamine, specific activity of hydrolysis reaction: value below 5 micromol/min/mg
489.7
-
transphosphatidylation reaction, substrate: serinol, specific activity of hydrolysis reaction: value below 5 micromol/min/mg
additional information
wild-type protein shows nearly the same enzymatic activity as the recombinant protein produced in Escherichia coli
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
45
additional information
-
up to 60°C, increase of activity with increase of temperature
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
45
-
enzyme ist stable at or below 45°C when assayed after 40 h and 2 h, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable at high temperature and neutral pH-values, but significantly unstable in the alkaline range
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using ammonium sulfate fractionation, gel filtration with sepharose CL-6B, anion-exchange chromatography with DEAE-sepharose CL-6B and a second gel filtration with sepharose CL-6B
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PLD DNA and amino acid sequence determination, comparison, and analysis
expression in Escherichia coli. Cytotoxicity of protein for host is strictly coorelated to enzyme activity
-
recombinantly expressed in Escherchia coli as a His-tagged fusion protein
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
creation of a high performance PLD with superior transphosphatidylation activity and low hydrolysis activity can be very useful for the synthesis of phospholipids used in pharmaceuticals, foods, cosmetics, and other industries
analysis
-
synthesis of fluorogenic analogue of phosphatidylcholine 1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine, and use as direct substrate for real-time measurement of enzyme activity. 1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine is substrate for both phospholipases C and D
biotechnology
-
the feature of the enzyme, to be highly active in moderate pH and temperature, makes PLD684 easy to handle and thus substantiate its potential biocatalytic application in the industrial scale
synthesis
synthesis
-
production of enzyme in Escherichia coli is strongly influenced by the catalytic activity as cytotoxicity of protein for host is strictly coorelated to enzyme activity. Synthesis of inactive mutants gives recovery yields 5-10 times higher than for wild-type
synthesis
-
hyperactivation of PLD by bio-imprinting and immobilization by adsorption and precipitation, followed by cross-linking results in increased catalytic activity. The maximum activity of immobilized PLD reaches 166953 U/g protein, compared to 11922 U/mg protein for the free form. The selectivity of PLD is significantly enhanced after immobilization. The yield of phosphatidylglycerol and phosphatidic acid reaches 94.0% and 5.96%, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leiros, I.; Hough, E.; D'Arrigo, P.; Carrea, G.; Pedrocchi-Fantoni, G.; Secundo, F.; Servi, S.
Crystallization and preliminary X-ray diffraction studies of phospholipase D from Streptomyces sp
Acta Crystallogr. Sect. D
56
466-468
2000
Streptomyces sp.
-
Lim, S.K.; Choi, J.W.; Chung, M.H.; Lee, E.T.; Khang, Y.H.; Kim, S.D.; Nam, D.H.
Production and characterization of extracellular phospholipase D from Streptomyces sp. YU100
J. Microbiol. Biotechnol.
12
189-195
2002
Streptomyces sp.
-
Bossi, L.; D'Arrigo, P.; Pedrocchi-Fantoni, G.; Mele, A.; Servi, S.; Leiros, I.
The substrate requirements of phospholipase D
J. Mol. Catal. B
11
433-438
2001
Streptomyces sp.
-
Ichikawa, S.; Walde, P.
Phospholipase D-mediated aggregation, fusion, and precipitation of phospholipid vesicles
Langmuir
20
941-949
2004
Streptomyces sp., Streptomyces sp. AA586
Simkhada, J.R.; Cho, S.S.; Lee, H.J.; Yoo, J.C.
Purification and biochemical properties of phospholipase D (PLD57) produced by Streptomyces sp. CS-57
Arch. Pharm. Res.
30
1302-1308
2007
Streptomyces sp., Streptomyces sp. CS-57
Fedeli, C.; Carrea, G.; Monti, D.
On the effects of site-specific mutations on activity and expression of the Streptomyces PMF phospholipase D
J. Mol. Catal. B
41
1-7
2006
Streptomyces sp.
-
Rose, T.M.; Prestwich, G.D.
Synthesis and evaluation of fluorogenic substrates for phospholipase D and phospholipase C
Org. Lett.
8
2575-2578
2006
Arachis hypogaea, Brassica oleracea, Saccharomyces cerevisiae, Streptomyces sp.
Simkhada, J.R.; Lee, H.J.; Jang, S.Y.; Kim, J.H.; Lee, H.C.; Sohng, J.K.; Yoo, J.C.
A novel low molecular weight phospholipase D from Streptomyces sp. CS684
Biores. Technol.
100
1388-1393
2009
Streptomyces sp.
Dippe, M.; Mrestani-Klaus, C.; Schierhorn, A.; Ulbrich-Hofmann, R.
Phospholipase D-catalyzed synthesis of new phospholipids with polar head groups
Chem. Phys. Lipids
152
71-77
2008
Brassica oleracea, Streptomyces sp.
Lee, J.S.; Bat-Ochir, M.; Demirev, A.V.; Nam, D.H.
Molecular cloning of the phospholipase D gene from Streptomyces sp. YU100 and its expression in Escherichia coli
J. Microbiol.
47
116-122
2009
Streptomyces sp. (B0FZD9)
Uesugi, Y.; Hatanaka, T.
Phospholipase D mechanism using Streptomyces PLD
Biochim. Biophys. Acta
1791
962-969
2009
Streptomyces antibioticus, Streptomyces cinnamoneus, Streptomyces halstedii, Streptomyces septatus, Streptomyces sp. (P84147)
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