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Information on EC 3.1.4.4 - phospholipase D and Organism(s) Saccharomyces cerevisiae and UniProt Accession P36126

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     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:
Saccharomyces cerevisiae
UNIPROT: P36126
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
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-
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AtPLDalpha2
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-
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AtPLDbeta1
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-
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AtPLDbeta2
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AtPLDdelta
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AtPLDepsilon
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AtPLDgamma1
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AtPLDgamma2
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AtPLDgamma3
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AtPLDp1
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-
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AtPLDp2
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AtPLDzeta
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choline phosphatase
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hPLD1
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hPLD2
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lecithinase D
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-
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lipophosphodiesterase II
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-
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Meiosis-specific sporulation protein SPO14
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-
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mPLD1
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mPLD2
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Phosphatidylcholine-hydrolyzing phospholipase D1
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-
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Phosphatidylcholine-hydrolyzing phospholipase D2
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-
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Phospholipase D1 PHOX and PX containing domain
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Phospholipase D2 PHOX and PX containing domain
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-
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PLD delta
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PLD epsilon
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PLD zeta
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PLD1C
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-
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PLDalpha
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PLDalpha3
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PLDbeta
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PLDdelta1
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PLDzeta1
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-
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PLDzeta2
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-
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rPLD1
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-
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rPLD2
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a phosphatidylcholine + H2O = choline + a phosphatidate
show the reaction diagram
the catalysis proceeds via two-step reaction with the formation of phosphatidyl-enzyme intermediate. Both of the two catalytic His residues are critical in the reaction course, where one acts as a nucleophile, while the other functions as a general acid/base, reaction cycle overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine phosphatidohydrolase
Also acts on other phosphatidyl esters.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-87-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
?
show the reaction diagram
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
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-
?
2-decanoyl-1-(O-[(11-(4,4-difluoro-5,7-dimethyl)-4-bora-3a,4a-diaza-s-indacene-3-propionyl)amino]-undecyl)-phosphatidylcholine + H2O
2-decanoyl-1-(O-[(11-(4,4-difluoro-5,7-dimethyl)-4-bora-3a,4a-diaza-s-indacene-3-propionyl)amino]-undecyl)-phosphatidic acid + choline
show the reaction diagram
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BODIPY-fluorophor-phosphatidylcholine as substrate
-
-
?
phosphatidylcholine + butanol
phosphatidylbutanol + choline
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + ethanol
phosphatidylethanol + choline
show the reaction diagram
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-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerophosphate + choline
show the reaction diagram
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-
-
-
?
phosphatidylcholine + H2O
choline + phosphatidate
show the reaction diagram
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-
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?
phosphatidylcholine + H2O
choline + phosphatidic acid
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + heptanol
phosphatidylheptanol + choline
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + hexanol
phosphatidylhexanol + choline
show the reaction diagram
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-
-
-
?
phosphatidylcholine + methanol
phosphatidylmethanol + choline
show the reaction diagram
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-
-
-
?
phosphatidylcholine + pentanol
phosphatidylpentanol + choline
show the reaction diagram
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-
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-
?
phosphatidylcholine + propanol
phosphatidylpropanol + choline
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
ethanolamine + phosphatidate
show the reaction diagram
-
-
-
?
phosphatidylserine + H2O
L-serine + phosphatidate
show the reaction diagram
-
-
-
?
phospholipid + alcohol
phospholipid + alcohol
show the reaction diagram
-
transphosphaditylation
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-
?
phospholipid + H2O
phosphatidic acid + alcohol
show the reaction diagram
-
phosphoric ester hydrolysis
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-
?
additional information
?
-
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 + phosphatidic acid
show the reaction diagram
-
-
-
-
?
phospholipid + alcohol
phospholipid + alcohol
show the reaction diagram
-
transphosphaditylation
-
-
?
phospholipid + H2O
phosphatidic acid + alcohol
show the reaction diagram
-
phosphoric ester hydrolysis
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-
?
additional information
?
-
-
the Arf-GTPase-activating protein Gsc1p is essential for sporulation and positively regulates the phospholipase D Spo14p
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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Ca2+ dependent and independent enzymes
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-synuclein
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Ba2+
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1 mM, 15-25% inhibition
Co2+
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1 mM, 50-60% inhibition
H2O2
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exposure of cells to H2O2 leads to transient increase in activity followed by 90% decrease
Inositol
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at 0.075 mM in culture medium,reduction of enzyme activity by 30-40%
Mn2+
-
1 mM, 45-55% inhibition
Zn2+
-
1 mM, 45% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
butanol
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transphosphatidylation increases activity
Ca2+
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required, 1 mM
ethanol
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transphosphatidylation increases activity
H2O2
-
exposure of cells to H2O2 leads to transient increase in activity followed by 90% decrease
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the PLD superfamily, PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
sec14 mutant, enzyme activity is elevated by 40% at restrictive temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complete to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, expression analysis and regulation
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functional overexpression of SPO14 in yeast cells deficient in an essential phosphatidylinositol and phosphatidylcholine transfer protein, i.e. sec14-1/cki1DELTA cells, is not sufficient to rescue the alpha-synuclein-induced growth defect
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
phospholipase D is a useful enzyme for its transphosphatidylation activity, which enables the enzymatic synthesis of various phospholipids, natural and unnatural phospholipids, and phospholipids with a functional head group, detailed overview
analysis
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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
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
Ella, K.M.; Dolan, J.W.; Meier, K.E.
Characterization of a regulated form of phospholipase D in the yeast Saccharomyces cerevisiae
Biochem. J.
307
799-805
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Tang, X.; Waksman, M.; Ely, Y.; Liscovitch, M.
Characterization and regulation of yeast Ca2+-dependent phosphatidylethanolamine-phospholipase D activity
Eur. J. Biochem.
269
3821-3830
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Connolly, J.E.; Engebrecht, J.
The Arf-GTPase-activating protein Gsc1p is essential for sporulation and regulates the phospholipase D Spo14p
Eukaryot. Cell
5
112-124
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
Rappley, I.; Gitler, A.D.; Selvy, P.E.; LaVoie, M.J.; Levy, B.D.; Brown, H.A.; Lindquist, S.; Selkoe, D.J.
Evidence that alpha-synuclein does not inhibit phospholipase D
Biochemistry
48
1077-1083
2009
Saccharomyces cerevisiae, Homo sapiens
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
Damnjanovic, J.; Iwasaki, Y.
Phospholipase D as a catalyst: application in phospholipid synthesis, molecular structure and protein engineering
J. Biosci. Bioeng.
116
271-280
2013
Actinomadura sp., Streptomyces chromofuscus, Streptomyces cinnamoneus, Brassica oleracea (O82549), Saccharomyces cerevisiae (P36126), Homo sapiens (Q13393), Streptomyces antibioticus (Q53728), Saccharomyces cerevisiae ATCC 204508 (P36126), Actinomadura sp. 362
Manually annotated by BRENDA team