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Information on EC 4.1.1.65 - phosphatidylserine decarboxylase
for references in articles please use BRENDA:EC4.1.1.65
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EC Tree 4 Lyases
4.1 Carbon-carbon lyases
4.1.1 Carboxy-lyases
4.1.1.65 phosphatidylserine decarboxylase
IUBMB Comments
The enzyme contains a tightly-bound pyruvoyl cofactor.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 4.1.1.65
- phospholipid
- phosphatidylcholine
-
kennedy
- cdp-ethanolamine
- decarboxylases
-
3hserine
-
ptdetn
- cdp-diacylglycerol
- phosphatidylglycerophosphate
-
dowhan
-
spinothalamic
-
base-exchange
-
aminophospholipids
-
interorganelle
- cdp-diglyceride
- medicine
- analysis
showSynonyms
phosphatidylserine decarboxylase, psdc, ps decarboxylase, psd1p, psd2p, phosphatidylserine decarboxylase 1, phosphatidylserine decarboxylase 2, phosphatidylserine decarboxylase2, ct699, psd1 enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CT699
Decarboxylase, phosphatidylserine
-
-
-
-
FG10007
Phosphatidylserine decarboxylase
phosphatidylserine decarboxylase 1
phosphatidylserine decarboxylase2
PKH_072580
PS decarboxylase
PSD
PSD1
Psd1p
PSD2
Psd2p
PSDB
Tb927.9.10080
Phosphatidylserine decarboxylase
-
-
-
-
PS decarboxylase
-
-
-
-
PSD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
decarboxylation via Schiff base formation between a covalently bound pyruvoyl prosthetic group and the amine of serine
-
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
a Schiff base is formed by addition of the amino group of phosphatidylserine to the pyruvate residue of the enzyme as an essential step in the action of the decarboxylase
-
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
reaction is completely stereospecific with overall retention of configuration
-
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosphatidylserine and phosphatidylethanolamine biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
phosphatidyl-L-serine carboxy-lyase (phosphatidylethanolamine-forming)
The enzyme contains a tightly-bound pyruvoyl cofactor.
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CAS REGISTRY NUMBER
COMMENTARY
9054-78-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidyl-L-serine
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Substrates: the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine
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phosphatidyl-L-serine
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Substrates: important enzyme in the synthesis of phosphatidylethanolamine
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phosphatidyl-L-serine
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Substrates: important enzyme in the synthesis of phosphatidylethanolamine
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phosphatidyl-L-serine
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Substrates: important enzyme in the synthesis of phosphatidylethanolamine
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: localization of the phosphatidylserine-specific binding site in the enzyme
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: phosphatidyl-L-serine species with a 20:4 fatty acid on the sn-2 position are preferentially decarboxylated
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Micrococcus cerificans
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: phosphatidyl-L-serine species with a 20:4 fatty acid on the sn-2 position are preferentially decarboxylated
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: phosphatidylserine decarboxylase 1 is the major source of cellular and mitochondrial phosphatidylethanolamine
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 is the preferred substrate for phosphatidylcholine synthesis, phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 can be imported into mitochondria, although with moderate efficiency
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: high selectivity, preference for the formation of C34:2 and C32:2 species, phosphatidylserine decarboxylase 1
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: high selectivity, preference for the formation of C34:2 and C32:2 species, phosphatidylserine decarboxylase 2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: activity towards natural phosphatidylserine is greater than towards saturated phosphatidylserine
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: liposomal phosphatidyl-L-serine
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: liposomal phosphatidyl-L-serine
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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additional information
?
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Substrates: enzyme of the phospholipid metabolism
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?
additional information
?
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Substrates: side chain preferrence of phosphatidylserine in liver in decreasing order: 18:0/18:1, 18:0/22:6, 18:0/20:4, side chain preferrence of phosphatidylserine in brain in decreasing order: 18:0/22:6, 18:0/18:1, 18:0/20:4
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additional information
?
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Substrates: substrate preference of liver and cerebellum enzyme concerning 22:6n-3 content changes during aging
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additional information
?
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Substrates: the enzyme has both phosphatidylserine decarboxylase activity and phospholipid N-methyltransferase activity or two enzymes with identical electrophotetic properties
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?
additional information
?
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Substrates: effect of the enzyme in neural excitation. The carboxyl groups of phosphatidylserine function as ion exchange sites in the nerve membrane
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additional information
?
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Substrates: substrate transport to enzyme implicates specific lipid domains with pure phosphatidylserine vesicles being most effective
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additional information
?
-
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Substrates: the level of enzyme activity is partially and reversibly suppressed by inositol and further diminished by the combination of inositol and choline
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additional information
?
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Substrates: enzyme of the phospholipid metabolism
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidyl-L-serine
?
-
Substrates: the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine
Products: -
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?
phosphatidyl-L-serine
?
-
Substrates: important enzyme in the synthesis of phosphatidylethanolamine
Products: -
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?
phosphatidyl-L-serine
?
-
Substrates: important enzyme in the synthesis of phosphatidylethanolamine
Products: -
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?
phosphatidyl-L-serine
?
-
Substrates: important enzyme in the synthesis of phosphatidylethanolamine
Products: -
Products: -
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
Products: -
Products: -
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: -
Products: -
Products: -
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: -
Products: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: phosphatidylserine decarboxylase 1 is the major source of cellular and mitochondrial phosphatidylethanolamine
Products: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 is the preferred substrate for phosphatidylcholine synthesis, phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 can be imported into mitochondria, although with moderate efficiency
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
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Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Substrates: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: liposomal phosphatidyl-L-serine
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: -
Products: -
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Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
Substrates: liposomal phosphatidyl-L-serine
Products: -
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?
additional information
?
-
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Substrates: enzyme of the phospholipid metabolism
Products: -
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?
additional information
?
-
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Substrates: effect of the enzyme in neural excitation. The carboxyl groups of phosphatidylserine function as ion exchange sites in the nerve membrane
Products: -
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?
additional information
?
-
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Substrates: the level of enzyme activity is partially and reversibly suppressed by inositol and further diminished by the combination of inositol and choline
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additional information
?
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Substrates: enzyme of the phospholipid metabolism
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-chloro-N-(4-ethoxyphenyl)-4-quinolinamine
inhibitor with potent activity against Plasmodium falciparum, and low toxicity toward mammalian cells
7-chloro-N-(4-propylphenyl)-4-quinolinamine
0.01 mM, 29% inhibition, 0.1 mM, 76% inhibition of catalysis. Compound inhibits PSD activity and blocks Plasmodium falciparum blood stage development in the malaria murine model
Zwitterionic detergents
-
inactivation by dissociating the oligomeric enzyme
-
4-[7,9-dichloro-1H,2H,3H,3aH,4H,5H,9bH-cyclopenta[c]quinolin-4-yl]benzoic acid
-
inhibits native PSD activity in mitochondrial extracts by 63%, MIC increases from 15 microg/ml in the absence of ethanolamine to 60 microg/ml in the presence of ethanolamine
4-[7,9-dichloro-1H,2H,3H,3aH,4H,5H,9bH-cyclopenta[c]quinolin-4-yl]benzoic acid
71% inhibition at 0.072 mg/ml
Cyanoborohydride
-
inactivation in presence of phosphatidylserine, no inactivation in absence of phosphatidylserine
Triton X-100
-
Triton X-100, maximal activity, independent of phosphatidylserine concentration is expressed at Triton to phospholipid ration of 5.6, inhibition at a molar ratio higher than 5.6
Triton X-100
-
effect is related to the molar ratio of triton to phospholipid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pdr17
-
the presence of a phosphatidylinositol transfer protein called Pdr17 is required for Psd2 function
-
pyruvate
-
the pyruvate prosthetic group is in amide linkage to the amino terminus of the alpha-subunit. The prosthetic group is derived from Ser through a post-tranlational cleavage of a proenzyme
pyruvate
-
the pyruvoyl residue is covalently bound to the amino terminus of one of the two nonidentical subunits
Triton X-100
enzyme activity depends on presence of Triton X-100, optimum concentration 0.052%
Triton X-100
-
maximal activity, independent of phosphatidylserine concentration is expressed at Triton to phospholipid ratio of 5.6, inhibition at a molar ratio higher than 5.6
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Candidiasis
Candida albicans cannot acquire sufficient ethanolamine from the host to support virulence in the absence of de novo phosphatidylethanolamine synthesis.
Cataract
PISD is a mitochondrial disease gene causing skeletal dysplasia, cataracts, and white matter changes.
Hyperalgesia
Nerve injury-induced tactile allodynia is present in the absence of FOS labeling in retrogradely labeled post-synaptic dorsal column neurons.
Hyperalgesia
Sensitization of postsynaptic dorsal column neuronal responses by colon inflammation.
Hyperalgesia
Spinal Cord Stimulation Modulates Visceral Nociception and Hyperalgesia via the Spinothalamic Tracts and the Postsynaptic Dorsal Column Pathways: A Literature Review and Hypothesis.
Infections
Candida albicans cannot acquire sufficient ethanolamine from the host to support virulence in the absence of de novo phosphatidylethanolamine synthesis.
Neoplasms
NK-1-receptor-mediated lesion of spinal post-synaptic dorsal column neurons might improve intractable visceral pain of cancer origin.
Neuralgia
Spinal Cord Stimulation Modulates Visceral Nociception and Hyperalgesia via the Spinothalamic Tracts and the Postsynaptic Dorsal Column Pathways: A Literature Review and Hypothesis.
Neuroinflammatory Diseases
Evaluation of an alpha synuclein sensitized dendritic cell based vaccine in a transgenic mouse model of Parkinson's disease.
Parkinson Disease
Lipid disequilibrium in biological membranes, a possible pathway to neurodegeneration.
Retinal Degeneration
Autophagy-dependent rhodopsin degradation prevents retinal degeneration in Drosophila.
Starvation
The mitochondrial phosphatidylserine decarboxylase Psd1 is involved in nitrogen starvation-induced mitophagy in yeast.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.067
phosphatidyl-L-serine
-
in 60 mM potassium phosphate (pH 6.8), 0.17 M sucrose, 0.35 mM phenylmethylsulfonyl fluoride, 2 mM EDTA, 0.5 mM 2-mercaptoethanol, at 37°C
0.09
phosphatidyl-L-serine
-
in 100 mM potassium phosphate, pH 6.8, 10 mM EDTA, and 0.05% Triton X-100
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
pH 6.0: about 35% of maximal activity, pH 8.5: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
a strain harboring a hybrid plasmid in which the level of the enzyme phosphatidylserine decarboxylase may be 40 to 50times higher than wild-type levels
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
chemoheterotrophically and phototrophically grown
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
phosphatidylserine decarboxylase 1
brenda
-
high activity in cytoplasmic membrane and low activity in outer membrane of the cell envelope
brenda
PSD is catalytically active in both soluble and membrane fractions, with a membrane/soluble distribution of 3/1
brenda
-
the enzyme is equally distributed between membrane and soluble fractions
brenda
-
phosphatidylserine flows from the outer membrane to the inner membrane through contact sites between inner and outer membrane to become decarboxylated and the formed phosphatidylethanolamine flows directly back to the outer membrane, without mixing with inner membrane phosphatidylamine
brenda
-
exclusively in the inner mitochondrial membrane
brenda
-
inner mitochondrial membrane and Golgi/vacuole membrane
brenda
-
high activity in cytoplasmic membrane and low activity in outer membrane of the cell envelope
brenda
-
exclusively in the inner mitochondrial membrane
brenda
-
external side of the inner membrane
brenda
-
exclusively in the inner mitochondrial membrane
brenda
-
inner mitochondrial membrane, isoform Psd1p
brenda
-
the enzyme requires integration into the inner mitochondrial membrane for full enzymatic activity
brenda
anchored to the inner mitochondrial membrane
brenda
the 56 kDa precursor is processed upon import into mitochondria, leading to a 4 kDa alpha-subunit and a 47 kDa beta-subunit. Mutations in the conserved motif of the alpha-subunit affect processing and stability of Psd1, and consequently the enzyme's activity
brenda
autocatalytic processing in the mitochondrion
brenda
-
the enzyme requires integration into the inner mitochondrial membrane for full enzymatic activity
-
brenda
-
inner mitochondrial membrane, isoform Psd1p
-
brenda
PSD is catalytically active in both soluble and membrane fractions, with a membrane/soluble distribution of 3/1
-
brenda
-
the enzyme is equally distributed between membrane and soluble fractions
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the stability of endogenous Psd1 is influenced by inner membrane protease Yme1
physiological function
malfunction
-
deletion of PSD1 and/or PSD2 leads to depletion of total cellular and plasma membrane phosphatidylethanolamine level, whereas mutation in the other pathways has practically no effect
malfunction
-
mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3DELTA mutants) grow slowly in rich medium and are inviable in minimal medium. psd1-3_DELTAcells appear morphologically indistinguishable from wild type cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa.
malfunction
-
loss of Psd2 causes cells to acquire sensitivity to cadmium even though Psd1 remains intact, loss of Psd2 causes a specific reduction in vacuolar membrane phosphatidylethanolamine levels, whereas total phosphatidylethanolamine levels are not significantly affected
malfunction
-
psd1 and psd2 deletion mutants exhibit defects in filamentous growth
malfunction
-
deletion of isoform PSD1 causes loss of PSD activity in mitochondria, a severe growth defect on minimal media, and depletion of cellular and mitochondrial phosphatidylethanolamine levels. This defect cannot be compensated by Psd2p. In the homogenate of psd2DELTA, the PSD activity is only slightly reduced, whereas in psd1DELTA total PSD activity is only 25% of wild type
malfunction
-
the psd1-deficient strain shows reduced fusion kinetics and also has impaired mitochondrial activity such as oxidative phosphorylation and reduced mitochondrial ATP levels. The loss of Psd1 also impairs the biogenesis of s-Mgm1, a protein essential for mitochondrial fusion
malfunction
-
deletion of isoform PSD1 causes loss of PSD activity in mitochondria, a severe growth defect on minimal media, and depletion of cellular and mitochondrial phosphatidylethanolamine levels. This defect cannot be compensated by Psd2p. In the homogenate of psd2DELTA, the PSD activity is only slightly reduced, whereas in psd1DELTA total PSD activity is only 25% of wild type
-
malfunction
-
deletion of PSD1 and/or PSD2 leads to depletion of total cellular and plasma membrane phosphatidylethanolamine level, whereas mutation in the other pathways has practically no effect
-
malfunction
-
mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3DELTA mutants) grow slowly in rich medium and are inviable in minimal medium. psd1-3_DELTAcells appear morphologically indistinguishable from wild type cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa.
-
physiological function
-
the psd1, psd2, and psd3 gene products share overlapping functions essential for the normal growth of Schizosaccharomyces pombe cells
physiological function
-
the mitochondrial Psd1 provides roughly 70% of the phosphatidylethanolamine biosynthesis in the cell with Psd2 carrying out the remainder, Psd2 action enhances Ycf1-dependent transport activity
physiological function
-
phosphatidylserine decarboxylase is essential for cell wall integrity and virulence in Candida albicans
physiological function
-
phosphatidylserine decarboxylase is a Toll-like receptor 4 agonist, phosphatidylserine decarboxylase in concentrations as low as 100 ng/ml stimulates RAW264.7 murine macrophage cells and primary peritoneal macrophage cells to secrete tissue necrosis factor alpha and interleukin-6, respectively. PSD induces the production of interleukin-6, in part, via its enzymatic activity
physiological function
-
phosphatidylethanolamine from phosphatidylserine decarboxylase2 (PSD2) is essential for autophagy under cadmium stress in Saccharomyces cerevisiae. Overexpression of PSD2 confers resistance to cadmium
physiological function
-
isoform PSD1 reduces externalized phosphatidylserine on host cells, enabling evasion of phagocytosis
physiological function
-
the enzyme is required for an optimal parasite growth and replication
physiological function
-
Psd1 is required for normal mitochondrial morphology, proper mitochondrial fusion during yeast mating, and proper mitochondrial activity
physiological function
enzyme is able to complement a Saccharomyces cerevisiae PSD mutant lacking PSD1 and PSD2 and DPL1 activities
physiological function
enzyme is responsible for remodeling of human phosphatidylserine to bacterial phosphatidylethanolamine in human pathogen Chlamydia trachomatis
physiological function
the plasma membrane of a isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
physiological function
the plasma membrane of isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
physiological function
after 4 days of gene silencing, procyclic forms of Trypanosoma brucei show a growth defect compared to control parasites, while growth of PSD-depleted bloodstream forms is only slightly affected. In both life cycle forms, down-regulation of TbPSD leads to mitochondrial fragmentation and a decrease in ATP production via oxidative phosphorylation of more than 75% in PSD-depleted mitochondria
physiological function
deletion of isoform Psd2 results in a significant reduction of mycelial growth and conidiation. The Psd2 deletion mutant is defective in ascospore production and virulence in wheat and more sensitive to osmotic and oxygen stresses. Deletion of Psd2 reduces the formation of lipid droplets and aggravates autophagy
physiological function
isoform Psd1 is involved in mitophagy induction only after nitrogen starvation. Psd1 mutant cells show a mitophagy defect after nitrogen starvation, possibly due to a failure of ubiquitin-like protein Atg8 recruitment to mitochondria
physiological function
isoform Psd2 is required preferentially for mitophagy induction in the stationary phase of growth and to a lesser extent for nitrogen starvation-induced mitophagy
physiological function
PSD knockdown disrupts muscle phospholipid homeostasis leading to an about 25% reduction in PtdEtn and an about 45% increase in PtdSer content, accompanied by the development of a severe myopathy, a 40% loss in muscle mass as well as extensive myofiber damage with increased DNA synthesis and central nucleation. PSD knockdown causes marked accumulation of abnormally appearing mitochondria that exhibit severely disrupted inner membrane integrity and reduced OXPHOS protein content
physiological function
Q5B8E2
the growth of the PSDB deletion mutant is retarded on minimal medium at 25°C, 37°C and 42°C. Deletion of PSDB decreases conidiation efficiency and causes abnormal morphology and altered phospholipid composition
physiological function
-
phosphatidylethanolamine from phosphatidylserine decarboxylase2 (PSD2) is essential for autophagy under cadmium stress in Saccharomyces cerevisiae. Overexpression of PSD2 confers resistance to cadmium
-
physiological function
-
the psd1, psd2, and psd3 gene products share overlapping functions essential for the normal growth of Schizosaccharomyces pombe cells
-
physiological function
-
the plasma membrane of a isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
-
physiological function
-
the plasma membrane of isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
-
physiological function
-
the growth of the PSDB deletion mutant is retarded on minimal medium at 25°C, 37°C and 42°C. Deletion of PSDB decreases conidiation efficiency and causes abnormal morphology and altered phospholipid composition
-
physiological function
-
isoform PSD1 reduces externalized phosphatidylserine on host cells, enabling evasion of phagocytosis
-
physiological function
-
deletion of isoform Psd2 results in a significant reduction of mycelial growth and conidiation. The Psd2 deletion mutant is defective in ascospore production and virulence in wheat and more sensitive to osmotic and oxygen stresses. Deletion of Psd2 reduces the formation of lipid droplets and aggravates autophagy
-
physiological function
-
enzyme is responsible for remodeling of human phosphatidylserine to bacterial phosphatidylethanolamine in human pathogen Chlamydia trachomatis
-
physiological function
Trypanosoma brucei 927/4 GUTat10.1
-
after 4 days of gene silencing, procyclic forms of Trypanosoma brucei show a growth defect compared to control parasites, while growth of PSD-depleted bloodstream forms is only slightly affected. In both life cycle forms, down-regulation of TbPSD leads to mitochondrial fragmentation and a decrease in ATP production via oxidative phosphorylation of more than 75% in PSD-depleted mitochondria
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28579
35000
42600
x * 42600, deduced from gene sequence, x * 35000, SDS-PAGE
60000
-
x * 60000, probably a trimer, SDS-PAGE after treatment with 2-mercaptoethanol
60000 - 170000
-
sucrose density gradient centrifugation, in presence of Triton
65000
7332
28579
-
1 * 7332, alpha, + 1 * 28579, beta, calculation from nucleotide sequence
28579
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
35000
x * 42600, deduced from gene sequence, x * 35000, SDS-PAGE
7332
-
1 * 7332, alpha, + 1 * 28579, beta, calculation from nucleotide sequence
7332
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
oligomer
-
x * 60000, probably a trimer, SDS-PAGE after treatment with 2-mercaptoethanol
dimer
-
1 * 7332, alpha, + 1 * 28579, beta, calculation from nucleotide sequence
dimer
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylation
proteolytic modification
side-chain modification
-
the enzyme is synthesized as a single subunit proenzyme form, pi subunit, 35579 Da, which undergoes posttranslational processing in which an internal Ser residue becomes the covalently bound prosthetic group of one of the two resulting subunits
acylation
the pyruvoyl moiety is detected at the N-termini of alpha-subunits
acylation
-
the pyruvoyl moiety is detected at the N-termini of alpha-subunits
-
proteolytic modification
-
the proenzyme is sequentially processed from a size of 46000 Da to 34000 Da. Sequential removal of the mitochondrial targeting and inner membrane sorting sequence, followed by formation of the alpha and beta subunits. The final step in maturation is proposed to be cleavage and concerted prosthetic group attachment to the alpha subunit
proteolytic modification
amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity
proteolytic modification
the post-translational processing is inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride. Residues Asp139, His198, and Ser308 are all essential for endoproteolytic processing of PSD, which occurs in cis. Within the GS(S/T) motif found in all PSDs, the Gly307 residue is also essential, but the Ser/Thr309 is nonessential
proteolytic modification
-
the post-translational processing is inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride. Residues Asp139, His198, and Ser308 are all essential for endoproteolytic processing of PSD, which occurs in cis. Within the GS(S/T) motif found in all PSDs, the Gly307 residue is also essential, but the Ser/Thr309 is nonessential
-
proteolytic modification
a conserved LGST motif separates the enzyme into alpha- and beta-subunits. Only the serine residue of the motif is absolutely required for Psd1 autocatalysis and function. Yeast Psd1 does not require its substrate phosphatidylserine for autocatalysis. Yeast Psd1 autocatalysis does not require mitochondrion-specific phospholipids, proteins, or cofactors
proteolytic modification
autocatalytic processing, precursor acts as self-processing serine protease
proteolytic modification
presence of a putative proteolytic PSD cleavage recognition motif, WGSS, amino acids 316-319
proteolytic modification
Trypanosoma brucei 927/4 GUTat10.1
-
presence of a putative proteolytic PSD cleavage recognition motif, WGSS, amino acids 316-319
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures in the apo form and phosphatidylethanolamine-bound form at resolutions of 2.6 and 3.6 A, respectively. Psd forms a homodimer, and each protomer has a positively charged substrate binding pocket at the active site. Conserved residues in the pocket are involved in phosphatidylserine decarboxylation. An N-terminal hydrophobic helical region is important for membrane binding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A203F
mutant protein is autoprocessed. Decarboxylase activity is almost lost
H144A
mutant protein is partially impaired in autoprocessing. Decarboxylase activity is almost lost
S254C
S254T
V167A
mutant protein is autoprocessed. Mutation does not affect decarboxylase activity
Y137F
mutant protein is autoprocessed. Decarboxylase activity is decreased by 50%
V314L/S317T
processing occurs to a slightly greater extent as in wild type, enzyme is twice as active
H195A
mutation produces significant levels of enzyme processing, although the level of the beta-subunit is reduced compared with wild-type
S309A
proenzyme is processed comparably to wild-type, modest reductions in catalytic activity
S309T
proenzyme is processed comparably to wild-type, modest reductions in catalytic activity
H195A
-
mutation produces significant levels of enzyme processing, although the level of the beta-subunit is reduced compared with wild-type
-
G462A
mutation in the conserved LGST motif, mutant retains some, albeit reduced, phosphatidylserine decarboxylase activity
G482P
mutation in conserved glycin residue, no major growth defect. The autocatalytic processing of G482P imported into mitochondria is delayed
G488P
mutation in conserved glycin residue, causes a dramatic growth defect of the mutant similar to that observed for a gene deletion mutant
G492P
mutation in conserved glycin residue, no major growth defect
K356/RF397L/E429G/M448T
mutations in beta-subunit. Mutant is temperature sensitive and autocatalytically impaired. Inner membrane proteases, Oma1p and Yme1p are responsible for degradation of the mutant precursor. Upon heat exposure postautocatalysis, mutant subunits accumulate in protein aggregates that are resolved by Yme1p acting alone, while the released alpha subunit is degraded in parallel by an unidentified protease
L461A
mutation in the conserved LGST motif, mutant retains some, albeit reduced, phosphatidylserine decarboxylase activity
LGS461AAA
replaced the LGS tripeptide starting at position 461 with three alanine residues with the goal of preventing normal enzymatic maturation
S463A
T464I
mutation in the conserved LGST motif, mutant retains some, albeit reduced, phosphatidylserine decarboxylase activity
S463A
-
the mutant does not display detectable decarboxylase activity due to the inability to generate the active site of the enzyme
-
CS111 mutant
pss-deficient mutant, forms fewer nodules than the wild type on its alfalfa host plant. Membrane lipid composition between mutants and wild type differs
MAV01 mutant
MAV01/pRK404, MAV01/pTB2086. Sinorhizobial psd gene is deleted, accumulated PS to about 20% of total lipids when grown in complex growth medium, forms fewer nodules than the wild type on its alfalfa host plant. Nodule formation in the mutant MAV01 sets in about 20 days later than that in the wild type. Leaves of alfalfa plants inoculated with the mutant MAV01 are yellowish, indicating that the plants are starved for nitrogen. Membrane lipid composition between mutants and wild type differs
S318A
additional information
S254C
-
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
S254C
-
mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase
S254T
-
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
S254T
-
mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase
S463A
-
the mutant does not display detectable decarboxylase activity due to the inability to generate the active site of the enzyme
S463A
mutation of the conserved serine residue, completely abolishes decarboxylase activity
S318A
mutation in putative cleavage motif, inhibits processing of the proenzyme. Mutant corrextly localizes to the mitochondrion
S318A
Trypanosoma brucei 927/4 GUTat10.1
-
mutation in putative cleavage motif, inhibits processing of the proenzyme. Mutant corrextly localizes to the mitochondrion
-
additional information
-
enzyme knockout mutant, 6- to 9fold more mitochondrial enzyme mRNA and 9fold more mitochondrial enzyme activity, total enzyme activity in membranes is unchanged
additional information
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
additional information
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
additional information
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
additional information
amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity. During progressive removal of 10 amino acid segments between positions 1 and 70 of PSD, deletions up to residue 50 do not reduce the ability of the enzyme to complement a Saccharomyces cerevisiae mutant. Deletions of the first 60 or 70 residues result in loss of complementation in both solid and liquid media
additional information
-
deletion of PSD1 leads to a significant depletion of phosphatidylethanolamine in mitochondria and whole cells, in mitochondria of a psd1/psd2 double mutant phosphatidylethanolamine drops to a minimum level and also cardiolipin level decreases, in psd2 mutants, phosphatidylcholine levels decrease
additional information
-
deletion of C2 homology domain and/or Golgi retention/localization domain of PSD2, both single deletion mutants are catalytically active and proteins localize normally, c2 deletion mutant has a severe defect in formation of phosphatidylethanolamin in both intact and permeabilized cells
additional information
fluorescence microscopy, different GFP-tagged versions of Psd1
additional information
-
fluorescence microscopy, different GFP-tagged versions of Psd1
additional information
removal of the complete inner membrane-associated domain IM2 leads to an altered topology of the protein with the soluble domain exposed to the mitochondrial matrix and to decreased enzyme activity. Psd1 variants lacking portions of the N-terminal moiety of IM2 are inserted into the inner mitochondrial membrane with an altered topology. Psd1 variants with deletions of C-terminal portions of IM2 accumulate at the outer mitochondrial membrane and lose their enzyme activity
additional information
-
removal of the complete inner membrane-associated domain IM2 leads to an altered topology of the protein with the soluble domain exposed to the mitochondrial matrix and to decreased enzyme activity. Psd1 variants lacking portions of the N-terminal moiety of IM2 are inserted into the inner mitochondrial membrane with an altered topology. Psd1 variants with deletions of C-terminal portions of IM2 accumulate at the outer mitochondrial membrane and lose their enzyme activity
additional information
removal of three to six amino acids of the conserved motif of the alpha subunit compromises the function of Psd1 as reflected by impaired growth of the mutants. In mutant Ax3, substitution of all positively charged amino acids of the highly conserved motif of the alpha subunit by alanine, the autocatalytic processing after import into mitochondria is delayed
additional information
-
removal of three to six amino acids of the conserved motif of the alpha subunit compromises the function of Psd1 as reflected by impaired growth of the mutants. In mutant Ax3, substitution of all positively charged amino acids of the highly conserved motif of the alpha subunit by alanine, the autocatalytic processing after import into mitochondria is delayed
additional information
properties of PE-deficient mutants lacking either Pss or Psd are compared with those of the Sinorhizobium meliloti wild type. Mutants deficient in phosphatidylserine decarboxylase, accumulate phosphatidylserine and are strongly affected during symbiosis with alfalfa. PE-deficient mutants grow in a wild-type-like manner on many complex media, they are unable to grow on minimal medium containing high phosphate concentrations. The psd-deficient mutant can grow on minimal medium containing low concentrations of inorganic phosphate, while the pss-deficient mutant can not. Addition of choline to the minimal medium rescued growth of the pss-deficient mutant, CS111, to some extent but inhibited growth of the psd-deficient mutant, MAV01
additional information
-
enzyme cDNA lacking the targeting sequence and a chimeric construct in which the targeting and sorting sequences were replaced by those from yeast PSD1, both complemented the ethanolamine requirement of a yeast psd1 psd2 mutant, enzyme activity is detected in mitochondria of the complemented cells
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
stable in presence of phosphatidylserine, 75% loss of activity in presence of Triton without phosphatidylserine present
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.02 M maleate buffer, pH 5.8, 4 mM EDTA, more than 90% loss of activity after 7 days
-
-25°C, pH 6.0-7.8, 10% glycerol, 0.1% Triton X-100, stable for 1.5 years. 0°C, stable for several months. Room temperature, stable for at least 1 week
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-nitrilotriacetic acid-agarose affinity column chromatography, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain Rosetta (DE3) or Sf-9 insect cells
-
expressed in Saccharomyces cerevisiae, Escherichia coli strain BL21 and Escherichia coli strain Rosetta
-
expression in Escherichia coli
the 46000 Da pssC gene product is converted into mature phosphatidylserine decarboxylase through multiple steps of post-translational processing
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the specific enzyme activity increases by 3fold during the replication of Toxoplasma gondii
the specific enzyme activity increases by 3fold during the replication of Toxoplasma gondii
-
the specific enzyme activity increases by 3fold during the replication of Toxoplasma gondii
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
phosphatidylserine decarboxylase PISD is downregulated by 8fold in migratory cells. Breast cancer cells overexpressing PISD exhibit reduced tumor-initiating potential in a high-throughput microfluidic mammosphere device and mouse xenograft model
analysis
use of the complementation of a Saccharomyces cerevisiae mutant for screening inhibitors
analysis
development of a fluorescence-based assay for selectively monitoring production of phosphatidylethanolamine in reactions using a maltose-binding protein fusion with Plasmodium knowlesi PSD as the enzyme. The product detection by fluorescence occurs after the lipid reacts with a water-soluble distyrylbenzene-bis-aldehyde and provides strong discrimination against the phosphatidylserine substrate. The assay is amenable to application in 96- and 384-well microtiter plates
analysis
development of a fluorescence-based distyrylbenzenebisaldehyde assay to measure PSD activity in vitro
analysis
-
development of a fluorescence-based distyrylbenzenebisaldehyde assay to measure PSD activity in vitro
analysis
development of fluorescence-based assay specific for PSD. The presence of phosphatidylserine causes only negligible background. This assay uses 1,2-diacetyl benzene/2-mercaptoethanol, which forms a fluorescent iso-indole-mercaptide conjugate with phosphatidylethanolamine. Detection is very sensitive, the assay is robust, with a signal/background ratio of 24, and can readily detect formation of 100 pmol of phosphatidylethanolamine produced from Escherichia coli membranes, Candida albicans mitochondria, or HeLa cell mitochondria
analysis
-
development of a fluorescence-based assay for selectively monitoring production of phosphatidylethanolamine in reactions using a maltose-binding protein fusion with Plasmodium knowlesi PSD as the enzyme. The product detection by fluorescence occurs after the lipid reacts with a water-soluble distyrylbenzene-bis-aldehyde and provides strong discrimination against the phosphatidylserine substrate. The assay is amenable to application in 96- and 384-well microtiter plates
-
analysis
-
development of a fluorescence-based distyrylbenzenebisaldehyde assay to measure PSD activity in vitro
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Volker, D.R.; Golden, E.B.
Phosphatidylserine decarboxylase from rat liver
Methods Enzymol.
209
360-365
1992
Rattus norvegicus
brenda
Bell, R.M.; Mavis, R.D.; Osborn, M.J.; Vagelos, P.R.
Enzymes of phospholipid metabolism: localization in the cytoplasmic and outer membrane of the cell envelope of Escherichia coli and Salmonella typhimurium
Biochim. Biophys. Acta
249
628-635
1971
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Cook, A.M.; Low, E.; Ishijimi, M.
Effect of phosphatidyl serine decarboxylase on neural excitation
Nature New Biol.
239
150-151
1972
Rattus norvegicus
brenda
Dowhan, W.; Wickner, W.T.; Kennedy, E.P.
Purification and properties of phosphatidylserine decarboxylase from Escherichia coli
J. Biol. Chem.
249
3079-3084
1974
Escherichia coli
brenda
Suda, T.; Matsuda, M.
Studies on decarboxylation of phosphatidylserine
Biochim. Biophys. Acta
369
331-337
1974
Mus musculus
-
brenda
Warner, T.G.; Dennis, E.A.
Phosphatidylserine decarboxylase: analysis of its action towards unsaturated and saturated phosphatidylserine and the effect of Triton X-100 on activity
Arch. Biochem. Biophys.
167
761-768
1975
Tetrahymena pyriformis
brenda
Warner, T.G.; Dennis, E.A.
Action of the highly purified, membrane-bound enzyme phosphatidylserine decarboxylase Escherichia coli toward phosphatidylserine in mixed micelles and erythrocyte ghosts in the presence of surfactant
J. Biol. Chem.
250
8004-8009
1975
Escherichia coli
brenda
Dutt, A.; Dowhan, W.
Intracellular distribution of enzymes of phospholipid metabolism in several gram-negative bacteria
J. Bacteriol.
132
159-165
1977
Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Klebsiella aerogenes, Micrococcus cerificans
brenda
Satre, M.; Kennedy, E.P.
Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli
J. Biol. Chem.
253
479-483
1978
Escherichia coli
brenda
Tyhach, R.J.; Hawrot, E.; Satre, M.; Kennedy, P.
Increased synthesis of phosphatidylserine decarboxylase in a strain of Escherichia coli bearing a hybrid plasmid
J. Biol. Chem.
254
627-633
1979
Escherichia coli
brenda
Hostetler, K.Y.; Zenner, B.D.; Morris, H.P.
Phosphatidylserine biosynthesis in mitochondria from the Morris 7777 hepatoma
J. Lipid Res.
20
607-613
1979
Rattus norvegicus
brenda
Igarashi, K.; Kaneda, M.; Yamaji, A.; Saido, T.C.; Kikkawa, U.; Ono, Y.; Inoue, K.; Umeda, M.
A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody
J. Biol. Chem.
270
29075-29078
1995
Cricetulus griseus
brenda
Rizzolo, L.J.
Kinetics and protein subunit interactions of Escherichia coli phosphatidylserine decarboxylase in detergent solution
Biochemistry
20
868-873
1981
Escherichia coli
brenda
Silber, P.; Borie, R.P.; Mikowski, E.J.; Goldfine, H.
Phospholipid biosynthesis in some anaerobic bacteria
J. Bacteriol.
147
57-61
1981
Clostridium butyricum, Escherichia coli, Megasphaera elsdenii, Nitratidesulfovibrio vulgaris, Veillonella parvula
brenda
Hawrot, E.
Phosphatidylserine decarboxylase from Escherichia coli
Methods Enzymol.
71
571-576
1981
Escherichia coli
brenda
Percy, A.K.; Moore, J.F.; Carson, M.A.; Waechter, C.J.
Characterization of brain phosphatidylserine decarboxylase: localization in the mitochondrial inner membrane
Arch. Biochem. Biophys.
223
484-494
1983
Rattus norvegicus, Bos taurus
brenda
Zborowski, J.; Dygas, A.; Wojtczak, L.
Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane
FEBS Lett.
157
179-182
1983
Rattus norvegicus, Mus musculus
brenda
Cain, B.D.; Donohue, T.J.; Shepherd, W.D.; Kaplan, S.
Localization of phospholipid biosynthetic enzyme activities in cell-free fractions derived from Rhodopseudomonas sphaeroides
J. Biol. Chem.
259
942-948
1984
Cereibacter sphaeroides
brenda
Kuchler, K.; Daum, G.; Paltauf, F.
Subcellular and submitochondrial localization of phospholipid-synthesizing enzymes in Saccharomyces cerevisiae
J. Bacteriol.
165
901-910
1986
Saccharomyces cerevisiae
brenda
No, Z.; Sanders, C.R.; Dowhan, W.; Tsai, M.D.
Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli
Bioorg. Chem.
16
184-188
1988
Escherichia coli
-
brenda
Verma, J.N.; Goldfine, H.
Phosphatidylserine decarboxylase from Clostridium butyricum
J. Lipid Res.
26
610-616
1985
Clostridium butyricum
brenda
Kuge, O.; Saito, K.; Kojima, M.; Akamatsu, Y.; Nishijima, M.
Post-translational processing of the phosphatidylserine decarboxylase gene product in Chinese hamster ovary cells
Biochem. J.
319
33-38
1996
Cricetulus griseus
brenda
Voelker, D.R.
Phosphatidylserine decarboxylase
Biochim. Biophys. Acta
1348
236-244
1997
Arabidopsis thaliana, Caenorhabditis elegans, Escherichia coli, Homo sapiens, Mammalia, Mus musculus, Saccharomyces cerevisiae
brenda
Overmeyer, J.H.; Waechter, C.J.
Regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae by inositol and choline: kinetics of repression and derepression
Arch. Biochem. Biophys.
290
511-516
1991
Saccharomyces cerevisiae
brenda
Dowhan, W.
Phosphatidylserine decarboxylases: pyruvoyl-dependent enzymes from bacteria to mammals
Methods Enzymol.
280
81-88
1997
Escherichia coli, Cricetulus griseus, Saccharomyces cerevisiae, Homo sapiens
brenda
Dowhan, W.; Li, Q.X.
Phosphatidylserine decarboxylase from Escherichia coli
Methods Enzymol.
209
348-359
1992
Escherichia coli
brenda
Auchi, L.; Tsvetnitsky, V.; Yeboah, F.A.; Gibbons, W.A.
Purification of plasma membrane rat liver phosphatidylserine decarboxylase
Biochem. Soc. Trans.
21
488S
1993
Rattus norvegicus
brenda
Dygas, A.; Zborowski, J.
Effect of Triton X-100 on the activity and solubilization of rat liver mitochondrial phosphatidylserine decarboxylase
Acta Biochim. Pol.
36
131-141
1989
Rattus norvegicus
brenda
Li, Q.X.; Dowhan, W.
Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli
J. Biol. Chem.
265
4111-4115
1990
Escherichia coli
brenda
Li, Q.X.; Dowhan, W.
Structural characterization of Escherichia coli phosphatidylserine decarboxylase
J. Biol. Chem.
263
11516-11522
1988
Escherichia coli
brenda
Hovius, R.; Faber, B.; Brigot, B.; Nicolay, K.; de Kruijff, B.
On the mechanism of the mitochondrial decarboxylation of phosphatidylserine
J. Biol. Chem.
267
16790-16795
1992
Rattus norvegicus
brenda
Kevala, J.H.; Kim, H.Y.
Determination of substrate preference in phosphatidylserine decarboxylation by liquid chromatography-electrospray ionization mass spectrometry
Anal. Biochem.
292
130-138
2001
Rattus norvegicus
brenda
Kitamura, H.; Wu, W.I.; Voelker, D.R.
The C2 domain of phosphatidylserine decarboxylase 2 is not required for catalysis but is essential for in vivo function
J. Biol. Chem.
277
33720-33726
2002
Saccharomyces cerevisiae
brenda
Wu, W.I.; Voelker, D.R.
Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process
J. Biol. Chem.
279
6635-6642
2004
Saccharomyces cerevisiae
brenda
Salvador, G.A.; Lopez, F.M.; Giusto, N.M.
Age-related changes in central nervous system phosphatidylserine decarboxylase activity
J. Neurosci. Res.
70
283-289
2002
Rattus norvegicus
brenda
Baunaure, F.; Eldin, P.; Cathiard, A.M.; Vial, H.
Characterization of a non-mitochondrial type I phosphatidylserine decarboxylase in Plasmodium falciparum
Mol. Microbiol.
51
33-46
2004
Plasmodium falciparum (Q9GPP8), Plasmodium falciparum
brenda
Burgermeister, M.; Birner, R.; Hrastnik, C.; Daum, G.
Phosphatidylserine decarboxylation and CDP-ethanolamine pathway contribute to the supply of phosphatidylethanolamine to mitochondria of the yeast
NATO Asi Ser. Ser. A
322
19-25
2000
Saccharomyces cerevisiae
-
brenda
Rontein, D.; Wu, W.I.; Voelker, D.R.; Hanson, A.D.
Mitochondrial phosphatidylserine decarboxylase from higher plants. Functional complementation in yeast, localization in plants, and overexpression in Arabidopsis
Plant Physiol.
132
1678-1687
2003
Arabidopsis thaliana, Solanum lycopersicum, Solanum tuberosum
brenda
Nishibori, A.; Kusaka, J.; Hara, H.; Umeda, M.; Matsumoto, K.
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
J. Bacteriol.
187
2163-2174
2005
Bacillus subtilis
brenda
Brgermeister, M.; Birner-Grunberger, R.; Heyn, M.; Daum, G.
Contribution of different biosynthetic pathways to species selectivity of aminoglycerophospholipids assembled into mitochondrial membranes of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1686
148-160
2004
Saccharomyces cerevisiae
brenda
Brgermeister, M.; Birner-Grunberger, R.; Nebauer, R.; Daum, G.
Contribution of different pathways to the supply of phosphatidylethanolamine and phosphatidylcholine to mitochondrial membranes of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1686
161-168
2004
Saccharomyces cerevisiae
brenda
Steenbergen, R.; Nanowski, T.S.; Beigneux, A.; Kulinski, A.; Young, S.G.; Vance, J.E.
Disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
J. Biol. Chem.
280
40032-40040
2005
Mus musculus
brenda
Bleijerveld, O.B.; Brouwers, J.F.; Vaandrager, A.B.; Helms, J.B.; Houweling, M.
The CDP-ethanolamine pathway and phosphatidylserine decarboxylation generate different phosphatidylethanolamine molecular species
J. Biol. Chem.
282
28362-28372
2007
Rattus norvegicus, Cricetulus griseus
brenda
Forbes, C.D.; Toth, J.G.; Ozbal, C.C.; Lamarr, W.A.; Pendleton, J.A.; Rocks, S.; Gedrich, R.W.; Osterman, D.G.; Landro, J.A.; Lumb, K.J.
High-throughput mass spectrometry screening for inhibitors of phosphatidylserine decarboxylase
J. Biomol. Screen.
12
628-634
2007
Homo sapiens
brenda
Nerlich, A.; von Orlow, M.; Rontein, D.; Hanson, A.D.; Doermann, P.
Deficiency in phosphatidylserine decarboxylase activity in the psd1 psd2 psd3 triple mutant of Arabidopsis affects phosphatidylethanolamine accumulation in mitochondria
Plant Physiol.
144
904-914
2007
Arabidopsis thaliana (Q84V22), Arabidopsis thaliana (F4KAK5), Arabidopsis thaliana (A4GNA8)
brenda
Larsson, K.E.; Nystroem, B.; Liljenberg, C.
A phosphatidylserine decarboxylase activity in root cells of oat (Avena sativa) is involved in altering membrane phospholipid composition during drought stress acclimation
Plant Physiol. Biochem.
44
211-219
2006
Avena sativa
brenda
Vences-Guzman, M.A.; Geiger, O.; Sohlenkamp, C.
Sinorhizobium meliloti mutants deficient in phosphatidylserine decarboxylase accumulate phosphatidylserine and are strongly affected during symbiosis with alfalfa
J. Bacteriol.
190
6846-6856
2008
Sinorhizobium meliloti 1021 (Q9FDI9)
brenda
Vance, J.E.
Phosphatidylserine and phosphatidylethanolamine in mammalian cells: two metabolically related aminophospholipids
J. Lipid Res.
49
1377-1387
2008
Saccharomyces cerevisiae, Mus musculus
brenda
Federovitch, C.M.; Jones, Y.Z.; Tong, A.H.; Boone, C.; Prinz, W.A.; Hampton, R.Y.
Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum remodeling in Saccharomyces cerevisiae
Mol. Biol. Cell
19
4506-4520
2008
Saccharomyces cerevisiae
brenda
Gulshan, K.; Schmidt, J.A.; Shahi, P.; Moye-Rowley, W.S.
Evidence for the bifunctional nature of mitochondrial phosphatidylserine decarboxylase: role in Pdr3-dependent retrograde regulation of PDR5 expression
Mol. Cell. Biol.
28
5851-5864
2008
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Schuiki, I.; Schnabl, M.; Czabany, T.; Hrastnik, C.; Daum, G.
Phosphatidylethanolamine synthesized by four different pathways is supplied to the plasma membrane of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1801
480-486
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae FY1679
brenda
Luo, J.; Matsuo, Y.; Gulis, G.; Hinz, H.; Patton-Vogt, J.; Marcus, S.
Phosphatidylethanolamine is required for normal cell morphology and cytokinesis in the fission yeast Schizosaccharomyces pombe
Eukaryot. Cell
8
790-799
2009
Schizosaccharomyces pombe, Schizosaccharomyces pombe SP870
brenda
Wriessnegger, T.; Sunga, A.J.; Cregg, J.M.; Daum, G.
Identification of phosphatidylserine decarboxylases 1 and 2 from Pichia pastoris
FEMS Yeast Res.
9
911-922
2009
Komagataella pastoris, Komagataella pastoris GS115
brenda
Gulshan, K.; Shahi, P.; Moye-Rowley, W.S.
Compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance
Mol. Biol. Cell
21
443-455
2010
Saccharomyces cerevisiae
brenda
Chen, Y.L.; Montedonico, A.E.; Kauffman, S.; Dunlap, J.R.; Menn, F.M.; Reynolds, T.B.
Phosphatidylserine synthase and phosphatidylserine decarboxylase are essential for cell wall integrity and virulence in Candida albicans
Mol. Microbiol.
75
1112-1132
2010
Candida albicans
brenda
Thanawastien, A.; Montor, W.R.; Labaer, J.; Mekalanos, J.J.; Yoon, S.S.
Vibrio cholerae proteome-wide screen for immunostimulatory proteins identifies phosphatidylserine decarboxylase as a novel Toll-like receptor 4 agonist
PLoS Pathog.
5
e1000556
2009
Vibrio cholerae serotype O1
brenda
Hoerl, G.; Wagner, A.; Cole, L.K.; Malli, R.; Reicher, H.; Kotzbeck, P.; Koefeler, H.; Hoefler, G.; Frank, S.; Bogner-Strauss, J.G.; Sattler, W.; Vance, D.E.; Steyrer, E.
Sequential synthesis and methylation of phosphatidylethanolamine promote lipid droplet biosynthesis and stability in tissue culture and in vivo
J. Biol. Chem.
286
17338-17350
2011
Mus musculus
brenda
Muthukumar, K.; Nachiappan, V.
Phosphatidylethanolamine from phosphatidylserine decarboxylase2 is essential for autophagy under cadmium stress in Saccharomyces cerevisiae
Cell Biochem. Biophys.
67
1353-1363
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Choi, J.Y.; Augagneur, Y.; Ben Mamoun, C.; Voelker, D.R.
Identification of gene encoding Plasmodium knowlesi phosphatidylserine decarboxylase by genetic complementation in yeast and characterization of in vitro maturation of encoded enzyme
J. Biol. Chem.
287
222-232
2012
Plasmodium knowlesi
brenda
Gupta, N.; Hartmann, A.; Lucius, R.; Voelker, D.R.
The obligate intracellular parasite Toxoplasma gondii secretes a soluble phosphatidylserine decarboxylase
J. Biol. Chem.
287
22938-22947
2012
Toxoplasma gondii, Toxoplasma gondii TaTi
brenda
Horvath, S.E.; Boettinger, L.; Voegtle, F.N.; Wiedemann, N.; Meisinger, C.; Becker, T.; Daum, G.
Processing and topology of the yeast mitochondrial phosphatidylserine decarboxylase 1
J. Biol. Chem.
287
36744-36755
2012
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Chan, E.Y.; McQuibban, G.A.
Phosphatidylserine decarboxylase 1 (Psd1) promotes mitochondrial fusion by regulating the biophysical properties of the mitochondrial membrane and alternative topogenesis of mitochondrial genome maintenance protein 1 (Mgm1)
J. Biol. Chem.
287
40131-40139
2012
Saccharomyces cerevisiae
brenda
Riekhof, W.R.; Wu, W.I.; Jones, J.L.; Nikrad, M.; Chan, M.M.; Loewen, C.J.; Voelker, D.R.
An assembly of proteins and lipid domains regulates transport of phosphatidylserine to phosphatidylserine decarboxylase 2 in Saccharomyces cerevisiae
J. Biol. Chem.
289
5809-5819
2014
Saccharomyces cerevisiae
brenda
Hartmann, A.; Hellmund, M.; Lucius, R.; Voelker, D.R.; Gupta, N.
Phosphatidylethanolamine synthesis in the parasite mitochondrion is required for efficient growth but dispensable for survival of Toxoplasma gondii
J. Biol. Chem.
289
6809-6824
2014
Toxoplasma gondii
brenda
Gsell, M.; Mascher, G.; Schuiki, I.; Ploier, B.; Hrastnik, C.; Daum, G.
Transcriptional response to deletion of the phosphatidylserine decarboxylase Psd1p in the yeast Saccharomyces cerevisiae
PLoS ONE
8
e77380
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
brenda
Soupene, E.; Kuypers, F.A.
Phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis
Sci. Rep.
7
15767
2017
Chlamydia trachomatis (P0CD79), Chlamydia trachomatis, Chlamydia trachomatis serovar D (P0CD79)
brenda
Khandelwal, N.; Sarkar, P.; Gaur, N.; Chattopadhyay, A.; Prasad, R.
Phosphatidylserine decarboxylase governs plasma membrane fluidity and impacts drug susceptibilities of Candida albicans cells
Biochim. Biophys. Acta
1860
2308-2319
2018
Candida albicans (Q5ABC5), Candida albicans (Q5AK66), Candida albicans, Candida albicans ATCC MYA-2876 (Q5ABC5), Candida albicans ATCC MYA-2876 (Q5AK66)
brenda
Di Bartolomeo, F.; Doan, K.N.; Athenstaedt, K.; Becker, T.; Daum, G.
Involvement of a putative substrate binding site in the biogenesis and assembly of phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1862
716-725
2017
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Wagner, A.; Di Bartolomeo, F.; Klein, I.; Hrastnik, C.; Doan, K.N.; Becker, T.; Daum, G.
Identification and characterization of the mitochondrial membrane sorting signals in phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1863
117-125
2018
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Choi, J.Y.; Duraisingh, M.T.; Marti, M.; Ben Mamoun, C.; Voelker, D.R.
From protease to decarboxylase the molecular metamorphosis of phosphatidylserine decarboxylase
J. Biol. Chem.
290
10972-10980
2015
Plasmodium knowlesi (B3L2V1), Plasmodium knowlesi, Plasmodium knowlesi H (B3L2V1)
brenda
Onguka, O.; Calzada, E.; Ogunbona, O.B.; Claypool, S.M.
Phosphatidylserine decarboxylase 1 autocatalysis and function does not require a mitochondrial-specific factor
J. Biol. Chem.
290
12744-12752
2015
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Choi, J.Y.; Surovtseva, Y.V.; Van Sickle, S.M.; Kumpf, J.; Bunz, U.H.F.; Ben Mamoun, C.; Voelker, D.R.
A novel fluorescence assay for measuring phosphatidylserine decarboxylase catalysis
J. Biol. Chem.
293
1493-1503
2018
Plasmodium knowlesi (B3L2V1), Plasmodium knowlesi H (B3L2V1)
brenda
Ogunbona, O.; Onguka, O.; Calzada, E.; Claypool, S.
Multitiered and cooperative surveillance of mitochondrial phosphatidylserine decarboxylase 1
Mol. Cell. Biol.
37
e00049
2017
Saccharomyces cerevisiae (P39006)
brenda
Farine, L.; Jelk, J.; Choi, J.Y.; Voelker, D.R.; Nunes, J.; Smith, T.K.; Buetikofer, P.
Phosphatidylserine synthase 2 and phosphatidylserine decarboxylase are essential for aminophospholipid synthesis in Trypanosoma brucei
Mol. Microbiol.
104
412-427
2017
Trypanosoma brucei (Q38DZ5), Trypanosoma brucei, Trypanosoma brucei 927/4 GUTat10.1 (Q38DZ5)
brenda
Choi, J.Y.; Kumar, V.; Pachikara, N.; Garg, A.; Lawres, L.; Toh, J.Y.; Voelker, D.R.; Ben Mamoun, C.
Characterization of Plasmodium phosphatidylserine decarboxylase expressed in yeast and application for inhibitor screening
Mol. Microbiol.
99
999-1014
2016
Plasmodium falciparum (Q9GPP8)
brenda
Chen, Y.; Humphries, B.; Brien, R.; Gibbons, A.; Chen, Y.; Qyli, T.; Haley, H.; Pirone, M.; Chiang, B.; Xiao, A.; Cheng, Y.; Luan, Y.; Zhang, Z.; Cong, J.; Luker, K.; Luker, G.; Yoon, E.
Functional isolation of tumor-initiating cells using microfluidic-based migration identifies phosphatidylserine decarboxylase as a key regulator
Sci. Rep.
8
244
2018
Homo sapiens
brenda
Tang, L.; Chi, H.; Li, W.; Zhang, L.; Zhang, L.; Chen, L.; Zou, S.; Liu, H.; Liang, Y.; Yu, J.; Dong, H.
FgPsd2, a phosphatidylserine decarboxylase of Fusarium graminearum, regulates development and virulence
Fungal Genet. Biol.
146
103483
2021
Fusarium graminearum (I1RZZ6), Fusarium graminearum (I1RDZ5), Fusarium graminearum ATCC MYA-4620 (I1RZZ6), Fusarium graminearum ATCC MYA-4620 (I1RDZ5)
brenda
Hendricson, A.; Umlauf, S.; Choi, J.Y.; Thekkiniath, J.; Surovtseva, Y.V.; Fuller, K.K.; Reynolds, T.B.; Voelker, D.R.; Ben Mamoun, C.
High-throughput screening for phosphatidylserine decarboxylase inhibitors using a distyrylbenzene-bis-aldehyde (DSB-3)-based fluorescence assay
J. Biol. Chem.
294
12146-12156
2019
Plasmodium knowlesi (B3L2V1), Candida albicans, Plasmodium knowlesi H (B3L2V1)
brenda
Choi, J.Y.; Black, R.; Lee, H.; Di Giovanni, J.; Murphy, R.C.; Ben Mamoun, C.; Voelker, D.R.
An improved and highly selective fluorescence assay for measuring phosphatidylserine decarboxylase activity
J. Biol. Chem.
295
9211-9222
2020
Escherichia coli (P0A8K1)
brenda
Takagi, K.; Kikkawa, A.; Iwama, R.; Fukuda, R.; Horiuchi, H.
Type II phosphatidylserine decarboxylase is crucial for the growth and morphogenesis of the filamentous fungus Aspergillus nidulans
J. Biosci. Bioeng.
131
139-146
2021
Aspergillus nidulans (Q5B8E2), Aspergillus nidulans ATCC 38163 (Q5B8E2)
brenda
Vigie, P.; Cougouilles, E.; Bhatia-Kissova, I.; Salin, B.; Blancard, C.; Camougrand, N.
The mitochondrial phosphatidylserine decarboxylase Psd1 is involved in nitrogen starvation-induced mitophagy in yeast
J. Cell Sci.
132
jcs221655
2019
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae (P53037)
brenda
Selathurai, A.; Kowalski, G.M.; Mason, S.A.; Callahan, D.L.; Foletta, V.C.; Della Gatta, P.A.; Lindsay, A.; Hamley, S.; Kaur, G.; Curtis, A.R.; Burch, M.L.; Ang, T.; McGee, S.L.; Bruce, C.R.
Phosphatidylserine decarboxylase is critical for the maintenance of skeletal muscle mitochondrial integrity and muscle mass
Mol. Metab.
27
33-46
2019
Mus musculus (Q8BSF4)
brenda
Watanabe, Y.; Watanabe, Y.; Watanabe, S.
Structural basis for phosphatidylethanolamine biosynthesis by bacterial phosphatidylserine decarboxylase
Structure
28
799-809.e5
2020
Escherichia coli (P0A8K1)
brenda
EXTERNAL LINKS (specific for EC-Number 4.1.1.65)
Transporter Classification Database (TCDB): 2.A.25.1.6
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